Team:Rutgers/Etch a Sketch

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Abstract

The Etch-a-Sketch project aims to create a lawn of bacteria that can be drawn on with a laser pointer. This seemingly inconsequential task actually presents many interesting engineering challenges. In particular, the bacteria need to be extremely sensitive in order to respond to a short light pulse from a laser, but they still must be “selective” enough to use in ambient lighting. We have designed a novel genetic switch that we hope will tackle these problems. If our work proves successful, it will serve as a useful model for future projects that require massive signal amplification. For example, researchers creating biosensors may find our work very helpful.

General Overview

Our project can be broken down into three parts: light input, signal amplification, and color output. We used LovTAP to receive the light input; we designed a switch based on Peking 2007’s Bi-stable switch to amplify the signal; and finally (after dabbling with some of Cambridge 2009’s E. Chromi colors) decided to use mRFP1 as a color output.

LovTAP

Overview

In order to draw on bacteria with a laser pointer, we need bacteria to be able to respond to light. Previous iGEM teams have worked on many different ways to do this each with different advantages and disadvantages. We were struck by the simplicity and beauty of LovTAP. In particular, it functions by itself as a single protein; it is a brilliantly engineered fusion protein; and, finally, it does not require any exotic supplements or strains of bacteria in order to function.

LovTAP Parts

As mentioned previously, LovTAP is a fusion protein. It consists of a light-response domain and a DNA binding domain, each of which are parts of other natural proteins.

Light response

The light-response domain is LOV2, the photoactive domain (i.e. the light responsive part) of AsLOV2 (Avena sativa phototropin 1). AsLOV2 is a protein which allows Avena sativa to respond to 470 nm light. It does this by undergoing a major conformational change upon being struck by a photon with a wavelenght near 470 nm. In detail, the absorption of the photon leads to the formation of a covalent bond between a flavin mononucleotide (FMN) cofactor and a conserved cysteine residue. This new bond distorts the conformation of the protein, causing the detachment and unfolding of the Jα-helix (see figure X). Detachment and unfolding of the Jα-helix can result in further downstream signalling. However, we will be most interested in the fact that the Jα-helix detaches when LOV2 is hit by blue light.

Figure X.

DNA Binding

The DNA binding domain of LovTAP is the well-known bacterial transcription factor trpR. As part of E. coli’s natural trp operon, in the presence of tryptophan, trpR will repress transcription at the trp promoter by binding the trp operator region and, thus, blocking RNA polymerase.

Figure Y.

LovTAP

Overview

The two seemingly unrelated parts described above share one crucial feature, an alpha helix. LOV2 binds and unbinds an alpha-helix in response to light and, trpR’s functional structure has one domain “bound” to an alpha-helix. Strickland et al.’s brilliant idea was to force them to “fight over” (since share implies that both can use the alpha helix simultaneously) a single alpha helix. Thus, since LOV2 has a higher affinity for the helix in the dark than trpR, there is no trpR activity in the dark. However, in the light, LOV2 releases the alpha helix, allowing trpR to bind it and, thus, result in trpR activity (which of course is repression of the trp promoter).

Details

AsLOV2 was ligated via its Jα-helix to a succession of 13-amino terminal truncations of trpR (11-108 residues). One construct, referred to as LovTAP (the LOV- and tryptophan-activated protein), preferentially protected trp operator DNA from digestion when illuminated, suggesting that LovTAP can bind the trp operator in the light. (The particular construct joins the Jα-helix of the LOV domain to the middle of the amino-terminal helix of trpR at Phe22). Further tests showed that upon light exposure LovTAP binds DNA in a manner that is characteristic of the TrpR domain. Additionally, mutation of the previously mentioned conserved cysteine of the LOV2 domain abolished the light sensitivity of DNA protection. As this cysteine has been shown to be crucial in the function of LOV2, this suggests that the observed light sensitivity is due to LOV2 (rather than some black magic).

Mechanism of Action:

Taken from Strickland et al.

A. Dark state-DNA dissociated: The shared helix contacts the LOV domain and trpR is in an inactive conformation.

B. Photoexcitation occurs at 470nm (represented by the FMN chromophore going from yellow to white) causing the contact between the LOV domain and the shared helix to be disrupted. trpR now binds the helix and assumes its active conformation (represented by the helix going from blue to red).

C. The active trpR domain of LovTAP binds the trp operator

D. Cessation of light causes the LOV domain to return to its dark state, dissociating LovTAP from the DNA and reinstating contact between the LOV domain and shared helix.

iGEM & LovTAP

EPFL

LovTAP was cloned into a biobrick and characterized by the EPF-Lausanne 2009 team. Strickland et al. measured only a 5-fold change in DNA binding affinity from dark state to light state in LovTAP. Though this change is miniscule (in biological scales), EPF-Lausanne found that there is a significant change in transcriptional output in response to 470nm light. Using molecular dynamics simulations, EPF-Lausanne found two mutations that may help improve LovTAP’s function by increasing the stability of the light state and decreasing the time it takes to flip from dark state to light state.

UNAM

A new LovTAP part was synthesized by the UNAM 2010 team via the alteration of EPF-Lausanne’s LovTAP. Primary changes include the removal of two 2 PstI restriction sites from the coding region of LovTAP and the addition of one of the point mutations that was proposed by EPF-Lausanne.

Our Project

For our circuit we will be using UNAM’s modified LovTAP, K360127. For the trp promoter and operator, we will be using ptrpL, K360023.

Possible issues

UNAM appeared to not have nearly as much success with LovTAP as EPF-Lausanne. Whether this was due to the mutation that was introduced or some other factor is unclear. We hoped to study UNAM’s LovTAP and possibly introduce other mutations to improve LovTAP’s function. For example, Strickland et al. identified mutations that increased LovTAP’s dynamic range (i.e. the difference in repression in the dark state vs. the light state) from 5 to 70.

Another issue is that LovTAP’s light state is unstable. Upon removal of the light source, LovTAP quickly returns to its inactive dark state. Thus, long exposure times might be necessary in order for the circuit to react to the light, which would be undesirable for drawing with a laser pointer. We may have to search for mutations that stabilize the light state, and thus allow LovTAP to remain in the light state for a longer time after being activated.

Peking Bi-stable Switch

Overview

The Peking 2007 iGEM team designed a switch that can be flipped between two stable states (on and off), a so called bi-stable switch. Such a switch would be desirable in the Etch-a-Sketch circuit because it would allow the bacteria to “remember” if it was exposed to light, and, thus, only a short exposure to light would be necessary in order to draw on our bacteria (rather than keeping the light on the bacteria until color appeared). However, Peking’s original design was not ideal because one state was not completely stable; once the switch is flipped on, it will slowly decay back to the off state. We would like our drawings to be permanent (to some degree), so we would need the on state to be stable. We redesigned the Peking bi-stable switch for this purpose.

Original Design

The Peking 2007 switch uses pR, pRM, cI, and cI434. Avoiding unnecessary detail: cI activates pRM and represses pR; cI434 represses pRM; pR has high basal transcription; and pRM has low basal transcription.

State 1

In the first state, cI434 levels are high and cI levels are low. This leads to high transcription from pR and low transcription from pRM, which, in this particular circuit, results in GFP production. The switch can be flipped by increasing cI levels.

State 2

In the second state, cI levels are high and cI434 levels are low. This leads to high transcription from pR, low transcription from pRM, and thus RFP production. Empirical evidence shows the switch will spontaneously decay back to state 1. This is probably due to the high basal transcription levels of pR.

Our design: Locking Switch

For our switch, we desired a simple circuit with a stable on state. The parts we used are ptrpL, cI434, pRM, trpR, and cI. As in the Peking switch, cI activates pRM and cI434 represses pRM. We cloned two additional parts for our switch: ptrpL and trpR. ptrpL is the well-known trp operon/promoter/leader sequence. trpR is the corresponding repressor which is induced by tryptophan. In our system, we will assume there are constantly high levels of tryptophan so that trpR will always act as a repressor.

State 1

In the first state, cI434 levels are high, trpR levels are low, and cI levels are low. This results in high transcription from ptrpL, low transcription from pRM, and thus low output signal. The switch can be flipped by reducing transcription from ptrpL.

State 2

In the second state, cI434 levels are low, trpR levels are high, and cI levels are high. This results in low transcription from ptrpL, high transcription from pRM, and thus high output signal. Since trpR is a strong repressor for ptrpL, we expect state 2 to be stable.

mRFP1

For our output signal, we decided to use mRFP1. It has many attractive qualities: the color is visible in normal lighting; no special supplements are necessary in order for the color to develop; the sequence is short (as compared to other pigment generating proteins); the protein itself generates the color, which hopefully will result in faster image development than a protein which catalyzes a reaction that generates color.

mRFP1 is a red fluorescent protein based on DsRed. Natural DsRed requires tetramerization in order to fluoresce. mRFP1 contains 33 mutations that, one, allow it to function as a monomer and, two, allow it to fold more quickly.

Home	Team	Official Team Profile	Etch-a-Sketch	Full Adder	MYS!S	Parts Submitted to the Registry	Modeling	Notebook	Safety	Acknowledgements

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 <p class=MsoNormal><span style='font-size:12.0pt'><span style='mso-tab-count:
 '>            </span>Our project can be broken down into three parts: light
-input, signal amplification, and color output. We used <span class=SpellE>LovTAP</span>
+input, signal amplification, and color output. We used LovTAP to receive the
-to receive the light input; we designed a switch based on Peking 2007’s
+light input; we designed a switch based on Peking 2007’s Bi-stable switch to
-Bi-stable switch to amplify the signal; and finally (after dabbling with some
+amplify the signal; and finally (after dabbling with some of Cambridge 2009’s
-of Cambridge 2009’s E. <span class=SpellE>Chromi</span> colors) decided to use
+E. Chromi colors) decided to use mRFP1 as a color output. <o:p></o:p></span></p>
-mRFP1 as a color output. <o:p></o:p></span></p>
 <p class=MsoNormal><span style='font-size:12.0pt'><o:p>&nbsp;</o:p></span></p>
-<p class=MsoNormal><span class=SpellE><b><u><span style='font-size:12.0pt'>LovTAP</span></u></b></span><b><u><span
+<p class=MsoNormal><b><u><span style='font-size:12.0pt'>LovTAP<o:p></o:p></span></u></b></p>
-style='font-size:12.0pt'><o:p></o:p></span></u></b></p>
 <p class=MsoNormal style='margin-bottom:5.0pt'><b><span style='font-size:12.0pt'>Overview<o:p></o:p></span></b></p>
@@ Line 830: / Line 853: @@
 <p class=MsoNormal style='margin-bottom:5.0pt;text-indent:.5in'><span
 style='font-size:12.0pt'>In order to draw on bacteria with a laser pointer, we
-need bacteria to be able to respond to light. Previous <span class=SpellE>iGEM</span>
+need bacteria to be able to respond to light. Previous iGEM teams have worked
-teams have worked on many different ways to do this each with different
+on many different ways to do this each with different advantages and
-advantages and disadvantages. We were struck by the simplicity and beauty of <span
+disadvantages. We were struck by the simplicity and beauty of LovTAP. In
-class=SpellE>LovTAP</span>. In particular, it functions by itself as a single
+particular, it functions by itself as a single protein; it is a brilliantly
-protein; it is a brilliantly engineered fusion protein; and, finally, it does
+engineered fusion protein; and, finally, it does not require any exotic supplements
-not require any exotic supplements or strains of bacteria in order to function.
+or strains of bacteria in order to function. <o:p></o:p></span></p>
-<o:p></o:p></span></p>
 <p class=MsoNormal style='margin-bottom:5.0pt'><span style='font-size:12.0pt'><o:p>&nbsp;</o:p></span></p>
-<p class=MsoNormal style='margin-bottom:5.0pt'><span class=SpellE><b><span
+<p class=MsoNormal style='margin-bottom:5.0pt'><b><span style='font-size:12.0pt'>LovTAP
-style='font-size:12.0pt'>LovTAP</span></b></span><b><span style='font-size:
+Parts<o:p></o:p></span></b></p>
-.0pt'> Parts<o:p></o:p></span></b></p>
 <p class=MsoNormal style='margin-bottom:5.0pt;text-indent:.5in'><span
-style='font-size:12.0pt'>As mentioned previously, <span class=SpellE>LovTAP</span>
+style='font-size:12.0pt'>As mentioned previously, LovTAP is a fusion protein.
-is a fusion protein. It consists of a light-response domain and a DNA binding
+It consists of a light-response domain and a DNA binding domain, each of which
-domain, each of which are parts of other natural proteins.<o:p></o:p></span></p>
+are parts of other natural proteins.<o:p></o:p></span></p>
 <p class=MsoNormal style='margin-bottom:5.0pt'><span style='font-size:12.0pt'><o:p>&nbsp;</o:p></span></p>
@@ Line 857: / Line 878: @@
 style='mso-tab-count:1'>            </span></span></i><span style='font-size:
 .0pt'>The light-response domain is LOV2, the photoactive domain (i.e. the
-light responsive part) of AsLOV2 (<span class=SpellE>Avena</span> sativa <span
+light responsive part) of AsLOV2 (Avena sativa phototropin 1). AsLOV2 is a
-class=SpellE>phototropin</span> 1). AsLOV2 is a protein which allows <span
+protein which allows Avena sativa to respond to 470 nm light. It does this by
-class=SpellE>Avena</span> sativa to respond to 470 nm light. It does this by
+undergoing a major conformational change upon being struck by a photon with a
-undergoing a major conformational change upon being struck by a photon with a <span
+wavelenght near 470 nm. In detail, the absorption of the photon leads to the
-class=SpellE>wavelenght</span> near 470 nm. In detail, the absorption of the
+formation of a covalent bond between a flavin mononucleotide (FMN) cofactor and
-photon leads to the formation of a covalent bond between a <span class=SpellE>flavin</span>
+a conserved cysteine residue. This new bond distorts the conformation of the
-mononucleotide (FMN) cofactor and a conserved cysteine residue. This new bond
+protein, causing the detachment and unfolding of the J&#945;-helix (see figure
-distorts the conformation of the protein, causing the detachment and unfolding
+X). Detachment and unfolding of the J&#945;-helix can result in further
-of the J&#945;-helix (see figure X). Detachment and unfolding of the
+downstream signalling. However, we will be most interested in the fact that the
-J&#945;-helix can result in further downstream <span class=SpellE>signalling</span>.
+J&#945;-helix detaches when LOV2 is hit by blue light.<i><o:p></o:p></i></span></p>
-However, we will be most interested in the fact that the J&#945;-helix detaches
-when LOV2 is hit by blue light.<i><o:p></o:p></i></span></p>
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 <p class=MsoNormal style='margin-bottom:5.0pt;text-indent:.5in'><span
-style='font-size:12.0pt'>The DNA binding domain of <span class=SpellE>LovTAP</span>
+style='font-size:12.0pt'>The DNA binding domain of LovTAP is the well-known
-is the well-known bacterial transcription factor <span class=SpellE>trpR</span>.
+bacterial transcription factor trpR. As part of E. <i>coli</i>’s natural trp
-As part of E. <i>coli</i>’s natural <span class=SpellE>trp</span> operon, in
+operon, in the presence of tryptophan, trpR will repress transcription at the trp
-the presence of tryptophan, <span class=SpellE>trpR</span> will repress
+promoter by binding the trp operator region and, thus, blocking RNA polymerase.<o:p></o:p></span></p>
-transcription at the <span class=SpellE>trp</span> promoter by binding the <span
-class=SpellE>trp</span> operator region and, thus, blocking RNA polymerase.<o:p></o:p></span></p>
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@@ Line 924: / Line 941: @@
 <p class=MsoNormal style='margin-bottom:15.0pt'><span style='font-size:12.0pt'><o:p>&nbsp;</o:p></span></p>
-<p class=MsoNormal style='margin-bottom:15.0pt'><span class=SpellE><b><span
+<p class=MsoNormal style='margin-bottom:15.0pt'><b><span style='font-size:12.0pt'>LovTAP<o:p></o:p></span></b></p>
-style='font-size:12.0pt'>LovTAP</span></b></span><b><span style='font-size:
-.0pt'><o:p></o:p></span></b></p>
 <p class=MsoNormal style='margin-bottom:15.0pt'><i><span style='font-size:12.0pt'>Overview<o:p></o:p></span></i></p>
@@ Line 933: / Line 948: @@
 style='font-size:12.0pt'>The two seemingly unrelated parts described above
 share one crucial feature, an alpha helix. LOV2 binds and unbinds an
-alpha-helix in response to light and, <span class=SpellE>trpR’s</span>
+alpha-helix in response to light and, trpR’s functional structure has one
-functional structure has one domain “bound” to an alpha-helix. Strickland et
+domain “bound” to an alpha-helix. Strickland et al.’s brilliant idea was to
-al.’s brilliant idea was to force them to “fight over” (since share implies
+force them to “fight over” (since share implies that both can use the alpha
-that both can use the alpha helix simultaneously) a single alpha helix. Thus,
+helix simultaneously) a single alpha helix. Thus, since LOV2 has a higher
-since LOV2 has a higher affinity for the helix in the dark than <span
+affinity for the helix in the dark than trpR, there is no trpR activity in the
-class=SpellE>trpR</span>, there is no <span class=SpellE>trpR</span> activity
+dark. However, in the light, LOV2 releases the alpha helix, allowing trpR to
-in the dark. However, in the light, LOV2 releases the alpha helix, allowing <span
+bind it and, thus, result in trpR activity (which of course is repression of the
-class=SpellE>trpR</span> to bind it and, thus, result in <span class=SpellE>trpR</span>
+trp promoter).<o:p></o:p></span></p>
-activity (which of course is repression of the <span class=SpellE>trp</span>
-promoter).<o:p></o:p></span></p>
 <p class=MsoNormal style='margin-bottom:15.0pt;text-indent:.5in'><span
@@ Line 951: / Line 964: @@
 <p class=MsoNormal style='margin-bottom:5.0pt;text-indent:.5in'><span
 style='font-size:12.0pt'>AsLOV2 was ligated via its J&#945;-helix to a
-succession of 13-amino terminal truncations of <span class=SpellE>trpR</span>
+succession of 13-amino terminal truncations of trpR (11-108 residues). One
-(11-108 residues). One construct, referred to as <span class=SpellE>LovTAP</span>
+construct, referred to as LovTAP (the <b>LOV</b>- and <b>t</b>ryptophan-<b>a</b>ctivated
-(the <b>LOV</b>- and <b>t</b>ryptophan-<b>a</b>ctivated <b>p</b>rotein), preferentially
+<b>p</b>rotein), preferentially protected trp operator DNA from digestion when
-protected <span class=SpellE>trp</span> operator DNA from digestion when
+illuminated, suggesting that LovTAP can bind the trp operator in the light.
-illuminated, suggesting that <span class=SpellE>LovTAP</span> can bind the <span
+(The particular construct joins the J&#945;-helix of the LOV domain to the
-class=SpellE>trp</span> operator in the light. (The particular construct joins
+middle of the amino-terminal helix of trpR at Phe22). Further tests showed that
-the J&#945;-helix of the LOV domain to the middle of the amino-terminal helix
+upon light exposure LovTAP binds DNA in a manner that is characteristic of the
-of <span class=SpellE>trpR</span> at Phe22). Further tests showed that upon
+TrpR domain. Additionally, mutation of the previously mentioned conserved
-light exposure <span class=SpellE>LovTAP</span> binds DNA in a manner that is
+cysteine of the LOV2 domain abolished the light sensitivity of DNA protection.
-characteristic of the <span class=SpellE>TrpR</span> domain. Additionally,
+As this cysteine has been shown to be crucial in the function of LOV2, this
-mutation of the previously mentioned conserved cysteine of the LOV2 domain
+suggests that the observed light sensitivity is due to LOV2 (rather than some
-abolished the light sensitivity of DNA protection. As this cysteine has been
+black magic).<o:p></o:p></span></p>
-shown to be crucial in the function of LOV2, this suggests that the observed
-light sensitivity is due to LOV2 (rather than some black magic).<o:p></o:p></span></p>
-<p class=MsoNormal><!--[if gte vml 1]><v:group id="Group_x0020_9" o:spid="_x0000_s1030"
+<p class=MsoNormal><!--[if gte vml 1]><v:group id="Group_x0020_9" o:spid="_x0000_s1062"
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       <div>
-      <p class=MsoNormal>3 ring FMN <span class=SpellE>chromophore</span> <o:p></o:p></p>
+      <p class=MsoNormal>3 ring FMN chromophore </p>
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       <td><![endif]>
       <div>
-      <p class=MsoNormal><span class=SpellE>TrpR</span> domain<span
+      <p class=MsoNormal>TrpR domain<span style='mso-spacerun:yes'>  </span></p>
-     style='mso-spacerun:yes'>  </span><o:p></o:p></p>
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@@ Line 1,481: / Line 1,491: @@
       <td><![endif]>
       <div>
-      <p class=MsoNormal>LOV Domain <o:p></o:p></p>
+      <p class=MsoNormal>LOV Domain </p>
       </div>
       <![if !mso]></td>
@@ Line 1,487: / Line 1,497: @@
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       <div>
       <p class=MsoNormal>Shared helix, contacting the LOV domain<span
-      style='mso-spacerun:yes'>   </span><o:p></o:p></p>
+      style='mso-spacerun:yes'>   </span></p>
       </div>
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@@ Line 1,636: / Line 1,646: @@
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-  id="_x0000_i1027" type="#_x0000_t75" style='width:423.05pt;height:303.15pt'>
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-<p class=MsoNormal style='margin-bottom:15.0pt'><span class=GramE><span
+<p class=MsoNormal style='margin-bottom:15.0pt'><span style='font-size:12.0pt'>Taken
-style='font-size:12.0pt'>Taken from Strickland et al.</span></span><span
+from Strickland et al. <o:p></o:p></span></p>
-style='font-size:12.0pt'> <o:p></o:p></span></p>
 <p class=MsoNormal style='margin-left:.5in;text-indent:-.25in;mso-list:l0 level1 lfo2;
@@ Line 2,064: / Line 2,073: @@
 style='mso-list:Ignore'>A.<span style='font:7.0pt "Times New Roman"'>&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;
 </span></span></span><![endif]><span style='font-size:12.0pt'>Dark state-DNA
-dissociated: The shared helix contacts the LOV domain and <span class=SpellE>trpR</span>
+dissociated: The shared helix contacts the LOV domain and trpR is in an
-is in an inactive conformation. <o:p></o:p></span></p>
+inactive conformation. <o:p></o:p></span></p>
 <p class=MsoNormal style='margin-left:.5in;text-indent:-.25in;mso-list:l0 level1 lfo2;
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-</span></span></span><![endif]><span class=SpellE><span style='font-size:12.0pt'>Photoexcitation</span></span><span
+</span></span></span><![endif]><span style='font-size:12.0pt'>Photoexcitation
-style='font-size:12.0pt'> occurs at 470nm (represented by the FMN <span
+occurs at 470nm (represented by the FMN chromophore going from yellow to white)
-class=SpellE>chromophore</span> going from yellow to white) causing the contact
+causing the contact between the LOV domain and the shared helix to be
-between the LOV domain and the shared helix to be disrupted. <span
+disrupted. trpR now binds the helix and assumes its active conformation
-class=SpellE><span class=GramE>trpR</span></span> now binds the helix and
+(represented by the helix going from blue to red).<o:p></o:p></span></p>
-assumes its active conformation (represented by the helix going from blue to
-red).<o:p></o:p></span></p>
 <p class=MsoNormal style='margin-left:.5in;text-indent:-.25in;mso-list:l0 level1 lfo2;
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-</span></span></span><![endif]><span style='font-size:12.0pt'>The active <span
+</span></span></span><![endif]><span style='font-size:12.0pt'>The active trpR
-class=SpellE>trpR</span> domain of <span class=SpellE>LovTAP</span> binds the <span
+domain of LovTAP binds the trp operator<o:p></o:p></span></p>
-class=SpellE>trp</span> operator<o:p></o:p></span></p>
 <p class=MsoNormal style='margin-left:.5in;text-indent:-.25in;mso-list:l0 level1 lfo2;
@@ Line 2,089: / Line 2,095: @@
 style='mso-list:Ignore'>D.<span style='font:7.0pt "Times New Roman"'>&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;
 </span></span></span><![endif]><span style='font-size:12.0pt'>Cessation of
-light causes the LOV domain to return to its dark state, dissociating <span
+light causes the LOV domain to return to its dark state, dissociating LovTAP
-class=SpellE>LovTAP</span> from the DNA and reinstating contact between the LOV
+from the DNA and reinstating contact between the LOV domain and shared helix. <o:p></o:p></span></p>
-domain and shared helix. <o:p></o:p></span></p>
 <p class=MsoNormal><span style='font-size:12.0pt'><o:p>&nbsp;</o:p></span></p>
-<p class=MsoNormal><span class=SpellE><span class=GramE><b><span
+<p class=MsoNormal><b><span style='font-size:12.0pt'>iGEM &amp; LovTAP <o:p></o:p></span></b></p>
-style='font-size:12.0pt'>iGEM</span></b></span></span><b><span
-style='font-size:12.0pt'> &amp; <span class=SpellE>LovTAP</span> <o:p></o:p></span></b></p>
 <p class=MsoNormal><i><span style='font-size:12.0pt'>EPFL<o:p></o:p></span></i></p>
-<p class=MsoNormal style='text-indent:.5in'><span class=SpellE><span
+<p class=MsoNormal style='text-indent:.5in'><span style='font-size:12.0pt'>LovTAP
-style='font-size:12.0pt'>LovTAP</span></span><span style='font-size:12.0pt'> was
+was cloned into a biobrick and characterized by the EPF-Lausanne 2009 team.
-cloned into a <span class=SpellE>biobrick</span> and characterized by the
+Strickland et al. measured only a 5-fold change in DNA binding affinity from
-EPF-Lausanne 2009 team. Strickland et al. measured only a 5-fold change in DNA
+dark state to light state in LovTAP. Though this change is miniscule (in
-binding affinity from dark state to light state in <span class=SpellE>LovTAP</span>.
+biological scales), EPF-Lausanne found that there is a significant change in transcriptional
-Though this change is miniscule (in biological scales), EPF-Lausanne found that
+output in response to 470nm light. Using molecular dynamics simulations,
-there is a significant change in transcriptional output in response to 470nm
+EPF-Lausanne found two mutations that may help improve LovTAP’s function by
-light. Using molecular dynamics simulations, EPF-Lausanne found two mutations
+increasing the stability of the light state and decreasing the time it takes to
-that may help improve <span class=SpellE>LovTAP’s</span> function by increasing
+flip from dark state to light state.<o:p></o:p></span></p>
-the stability of the light state and decreasing the time it takes to flip from
-dark state to light state.<o:p></o:p></span></p>
 <p class=MsoNormal style='text-indent:.5in'><span style='font-size:12.0pt'><o:p>&nbsp;</o:p></span></p>
@@ Line 2,117: / Line 2,118: @@
 <p class=MsoNormal><i><span style='font-size:12.0pt'>UNAM<o:p></o:p></span></i></p>
-<p class=MsoNormal><span style='font-size:12.0pt'>A new <span class=SpellE>LovTAP</span>
+<p class=MsoNormal><span style='font-size:12.0pt'>A new LovTAP part was
-part was synthesized by the UNAM 2010 team via the alteration of EPF-Lausanne’s
+synthesized by the UNAM 2010 team via the alteration of EPF-Lausanne’s LovTAP.
-<span class=SpellE>LovTAP</span>. Primary changes include the removal of two
+Primary changes include the removal of two 2&nbsp;PstI restriction sites from
-&nbsp;<span class=SpellE>PstI</span> restriction sites from the coding region
+the coding region of LovTAP and the addition of one of the point mutations that
-of <span class=SpellE>LovTAP</span> and the addition of one of the point
+was proposed by EPF-Lausanne. <o:p></o:p></span></p>
-mutations that was proposed by EPF-Lausanne. <o:p></o:p></span></p>
 <p class=MsoNormal style='margin-bottom:15.0pt'><span style='font-size:12.0pt'><o:p>&nbsp;</o:p></span></p>
@@ Line 2,130: / Line 2,130: @@
 <p class=MsoNormal style='text-indent:.5in'><span style='font-size:12.0pt'>For
-our circuit we will be using UNAM’s modified <span class=SpellE>LovTAP</span>,
+our circuit we will be using UNAM’s modified LovTAP, K360127. For the trp
-K360127. For the <span class=SpellE>trp</span> promoter and operator, we will be
+promoter and operator, we will be using ptrpL, K360023. <o:p></o:p></span></p>
-using <span class=SpellE>ptrpL</span>, K360023. <o:p></o:p></span></p>
 <p class=MsoNormal><span style='font-size:12.0pt'><o:p>&nbsp;</o:p></span></p>
@@ Line 2,139: / Line 2,138: @@
 <p class=MsoNormal><i><span style='font-size:12.0pt'><span style='mso-tab-count:
-'>            </span></span></i><span style='font-size:12.0pt'>UNAM appeared
+'>            </span></span></i><span style='font-size:12.0pt'>UNAM appeared to
-to not have nearly as much success with <span class=SpellE>LovTAP</span> as
+not have nearly as much success with LovTAP as EPF-Lausanne. Whether this was
-EPF-Lausanne. Whether this was due to the mutation that was introduced or some
+due to the mutation that was introduced or some other factor is unclear. We
-other factor is unclear. We hoped to study UNAM’s <span class=SpellE>LovTAP</span>
+hoped to study UNAM’s LovTAP and possibly introduce other mutations to improve
-and possibly introduce other mutations to improve <span class=SpellE>LovTAP’s</span>
+LovTAP’s function. For example, Strickland et al. identified mutations that
-function. For example, Strickland et al. identified mutations that increased <span
+increased LovTAP’s dynamic range (i.e. the difference in repression in the dark
-class=SpellE>LovTAP’s</span> dynamic range (i.e. the difference in repression
+state vs. the light state) from 5 to 70.<i><o:p></o:p></i></span></p>
-in the dark state vs. the light state) from 5 to 70.<i><o:p></o:p></i></span></p>
 <p class=MsoNormal><span style='font-size:12.0pt'><span style='mso-tab-count:
-'>            </span>Another issue is that <span class=SpellE>LovTAP’s</span>
+'>            </span>Another issue is that LovTAP’s light state is unstable.
-light state is unstable. Upon removal of the light source, <span class=SpellE>LovTAP</span>
+Upon removal of the light source, LovTAP quickly returns to its inactive dark
-quickly returns to its inactive dark state. Thus, long exposure times might be
+state. Thus, long exposure times might be necessary in order for the circuit to
-necessary in order for the circuit to react to the light, which would be
+react to the light, which would be undesirable for drawing with a laser
-undesirable for drawing with a laser pointer. We may have to search for
+pointer. We may have to search for mutations that stabilize the light state,
-mutations that stabilize the light state, and thus allow <span class=SpellE>LovTAP</span>
+and thus allow LovTAP to remain in the light state for a longer time after
-to remain in the light state for a longer time after being activated.<o:p></o:p></span></p>
+being activated.<o:p></o:p></span></p>
 <p class=MsoNormal><span style='font-size:12.0pt'><o:p>&nbsp;</o:p></span></p>
@@ Line 2,165: / Line 2,163: @@
 <p class=MsoNormal><span style='font-size:12.0pt'><span style='mso-tab-count:
-'>            </span>The Peking 2007 <span class=SpellE>iGEM</span> team
+'>            </span>The Peking 2007 iGEM team designed a switch that can be
-designed a switch that can be flipped between two stable states (on and off), a
+flipped between two stable states (on and off), a so called bi-stable switch.
-so called bi-stable switch. Such a switch would be desirable in the
+Such a switch would be desirable in the Etch-a-Sketch circuit because it would
-Etch-a-Sketch circuit because it would allow the bacteria to “remember” if it
+allow the bacteria to “remember” if it was exposed to light, and, thus, only a
-was exposed to light, and, thus, only a short exposure to light would be
+short exposure to light would be necessary in order to draw on our bacteria
-necessary in order to draw on our bacteria (rather than keeping the light on
+(rather than keeping the light on the bacteria until color appeared). However,
-the bacteria until color appeared). However, Peking’s original design was not
+Peking’s original design was not ideal because one state was not completely
-ideal because one state was not completely stable; once the switch is flipped
+stable; once the switch is flipped on, it will slowly decay back to the off
-on, it will slowly decay back to the off state. We would like our drawings to
+state. We would like our drawings to be permanent (to some degree), so we would
-be permanent (to some degree), so we would need the on state to be stable. We
+need the on state to be stable. We redesigned the Peking bi-stable switch for
-redesigned the Peking bi-stable switch for this purpose.<o:p></o:p></span></p>
+this purpose.<o:p></o:p></span></p>
 <p class=MsoNormal><span style='font-size:12.0pt'><o:p>&nbsp;</o:p></span></p>
@@ Line 2,182: / Line 2,180: @@
 <p class=MsoNormal><span style='font-size:12.0pt'><span style='mso-tab-count:
-'>            </span>The Peking 2007 switch uses <span class=SpellE>pR</span>,
+'>            </span>The Peking 2007 switch uses pR, pRM, cI, and cI434. Avoiding
-<span class=SpellE>pRM</span>, <span class=SpellE>cI</span>, and cI434.
+unnecessary detail: cI activates pRM and represses pR; cI434 represses pRM; pR
-Avoiding unnecessary detail: <span class=SpellE>cI</span> activates <span
+has high basal transcription; and pRM has low basal transcription. <o:p></o:p></span></p>
-class=SpellE>pRM</span> and represses <span class=SpellE>pR</span>; cI434
-represses <span class=SpellE>pRM</span>; <span class=SpellE>pR</span> has high
-basal transcription; and <span class=SpellE>pRM</span> has low basal
-transcription. <o:p></o:p></span></p>
 <p class=MsoNormal><span style='font-size:12.0pt'><o:p>&nbsp;</o:p></span></p>
@@ Line 2,195: / Line 2,189: @@
 <p class=MsoNormal><span style='mso-no-proof:yes'><!--[if gte vml 1]><v:shape
-  id="Picture_x0020_4" o:spid="_x0000_i1026" type="#_x0000_t75" style='width:468pt;
+  id="Picture_x0020_4" o:spid="_x0000_i1028" type="#_x0000_t75" style='width:468pt;
   height:156pt;visibility:visible;mso-wrap-style:square'>
   <v:imagedata src="EaSwriteup_files/image009.png" o:title=""/>
@@ Line 2,203: / Line 2,197: @@
 <p class=MsoNormal><span style='font-size:12.0pt'>In the first state, cI434
-levels are high and <span class=SpellE>cI</span> levels are low. This leads to
+levels are high and cI levels are low. This leads to high transcription from pR
-high transcription from <span class=SpellE>pR</span> and low transcription from
+and low transcription from pRM, which, in this particular circuit, results in
-<span class=SpellE>pRM</span>, which, in this particular circuit, results in
+GFP production. The switch can be flipped by increasing cI levels.<o:p></o:p></span></p>
-GFP production. The switch can be flipped by increasing <span class=SpellE>cI</span>
-levels.<o:p></o:p></span></p>
 <p class=MsoNormal><span style='font-size:12.0pt'><o:p>&nbsp;</o:p></span></p>
@@ Line 2,214: / Line 2,206: @@
 <p class=MsoNormal><span style='mso-no-proof:yes'><!--[if gte vml 1]><v:shape
-  id="Picture_x0020_5" o:spid="_x0000_i1025" type="#_x0000_t75" style='width:468pt;
+  id="Picture_x0020_5" o:spid="_x0000_i1027" type="#_x0000_t75" style='width:468pt;
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@@ Line 2,221: / Line 2,213: @@
 style='font-size:12.0pt'><o:p></o:p></span></i></p>
-<p class=MsoNormal><span style='font-size:12.0pt'>In the second state, <span
+<p class=MsoNormal><span style='font-size:12.0pt'>In the second state, cI
-class=SpellE>cI</span> levels are high and cI434 levels are low. This leads to
+levels are high and cI434 levels are low. This leads to high transcription from
-high transcription from <span class=SpellE>pR</span>, low transcription from <span
+pR, low transcription from pRM, and thus RFP production. Empirical evidence
-class=SpellE>pRM</span>, and thus RFP production. Empirical evidence shows the
+shows the switch will spontaneously decay back to state 1. This is probably due
-switch will spontaneously decay back to state 1. This is probably due to the
+to the high basal transcription levels of pR.<o:p></o:p></span></p>
-high basal transcription levels of <span class=SpellE>pR.</span><o:p></o:p></span></p>
 <p class=MsoNormal><span style='font-size:12.0pt'><o:p>&nbsp;</o:p></span></p>
@@ Line 2,233: / Line 2,224: @@
 <p class=MsoNormal><span style='font-size:12.0pt'>For our switch, we desired a
-simple circuit with a stable on state. The parts we used are <span
+simple circuit with a stable on state. The parts we used are ptrpL, cI434, pRM,
-class=SpellE>ptrpL</span>, cI434, <span class=SpellE>pRM</span>, <span
+trpR, and cI. As in the Peking switch, cI activates pRM and cI434 represses
-class=SpellE>trpR</span>, and <span class=SpellE>cI</span>. As in the Peking
+pRM. We cloned two additional parts for our switch: ptrpL and trpR. ptrpL is
-switch, <span class=SpellE>cI</span> activates <span class=SpellE>pRM</span>
+the well-known trp operon/promoter/leader sequence. trpR is the corresponding
-and cI434 represses <span class=SpellE>pRM</span>. We cloned two additional
+repressor which is induced by tryptophan. In our system, we will assume there
-parts for our switch: <span class=SpellE>ptrpL</span> and <span class=SpellE>trpR</span>.
+are constantly high levels of tryptophan so that trpR will always act as a
-<span class=SpellE><span class=GramE>ptrpL</span></span> is the well-known <span
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-by tryptophan. In our system, we will assume there are constantly high levels
-of tryptophan so that <span class=SpellE>trpR</span> will always act as a
 repressor. <o:p></o:p></span></p>
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+   <table cellpadding=0 cellspacing=0 width="100%">
+    <tr>
+     <td><![endif]>
+     <div>
+     <p style='margin-top:0in;margin-right:0in;margin-bottom:10.0pt;margin-left:
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+     mso-bidi-font-family:"Times New Roman";color:black;mso-themecolor:text1;
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+   <![if !mso]>
+   <table cellpadding=0 cellspacing=0 width="100%">
+    <tr>
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+     color:black;mso-themecolor:text1;mso-font-kerning:12.0pt'>Output Signal</span></b><o:p></o:p></p>
+     </div>
+     <![if !mso]></td>
+    </tr>
+   </table>
+   <![endif]></v:textbox>
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+</v:group><![endif]--><![if !vml]><img width=703 height=149
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+style='font-size:12.0pt'><o:p></o:p></span></i></p>
 <p class=MsoNormal><span style='font-size:12.0pt'>In the first state, cI434
-levels are high, <span class=SpellE>trpR</span> levels are low, and <span
+levels are high, trpR levels are low, and cI levels are low. This results in
-class=SpellE>cI</span> levels are low. This results in high transcription from <span
+high transcription from ptrpL, low transcription from pRM, and thus low output
-class=SpellE>ptrpL</span>, low transcription from <span class=SpellE>pRM</span>,
+signal. The switch can be flipped by reducing transcription from ptrpL.<o:p></o:p></span></p>
-and thus low output signal. The switch can be flipped by reducing transcription
-from <span class=SpellE>ptrpL</span>.<o:p></o:p></span></p>
 <p class=MsoNormal><span style='font-size:12.0pt'><o:p>&nbsp;</o:p></span></p>
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 <p class=MsoNormal><i><span style='font-size:12.0pt'>State 2<o:p></o:p></span></i></p>
-<p class=MsoNormal><span style='font-size:12.0pt'><br>
+<p class=MsoNormal><!--[if mso & !supportInlineShapes & supportFields]><span
-In the second state, cI434 levels are low, <span class=SpellE>trpR</span>
+style='mso-element:field-begin;mso-field-lock:yes'></span><span
-levels are high, and <span class=SpellE>cI</span> levels are high. This results
+style='mso-spacerun:yes'> </span>SHAPE <span
-in low transcription from <span class=SpellE>ptrpL</span>, high transcription from
+style='mso-spacerun:yes'> </span>\* MERGEFORMAT <span style='mso-element:field-separator'></span><![endif]--><!--[if gte vml 1]><v:group
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+     <p style='margin-top:0in;margin-right:0in;margin-bottom:10.0pt;margin-left:
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+    </tr>
+   </table>
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+   <table cellpadding=0 cellspacing=0 width="100%">
+    <tr>
+     <td><![endif]>
+     <div>
+     <p style='margin-top:0in;margin-right:0in;margin-bottom:10.0pt;margin-left:
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+     </div>
+     <![if !mso]></td>
+    </tr>
+   </table>
+   <![endif]></v:textbox>
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+" filled="f" stroked="f">
+  <v:textbox>
+   <![if !mso]>
+   <table cellpadding=0 cellspacing=0 width="100%">
+    <tr>
+     <td><![endif]>
+     <div>
+     <p style='margin:0in;margin-bottom:.0001pt'><b><span style='font-size:
+.0pt;font-family:"Calibri","sans-serif";mso-ascii-theme-font:minor-latin;
+     mso-bidi-font-family:"Times New Roman";mso-bidi-theme-font:minor-bidi;
+     color:black;mso-themecolor:text1;mso-font-kerning:12.0pt'>Output Signal</span></b><o:p></o:p></p>
+     </div>
+     <![if !mso]></td>
+    </tr>
+   </table>
+   <![endif]></v:textbox>
+ </v:shape><w:wrap type="none"/>
+ <w:anchorlock/>
+</v:group><![endif]--><![if !vml]><img width=725 height=149
+src="EaSwriteup_files/image014.gif" v:shapes="_x0000_s1026 Straight_x0020_Connector_x0020_60 Text_x0020_Box_x0020_2 Text_x0020_Box_x0020_10 Text_x0020_Box_x0020_2 Elbow_x0020_Connector_x0020_64 Text_x0020_Box_x0020_2 Straight_x0020_Connector_x0020_66 Text_x0020_Box_x0020_2 Elbow_x0020_Connector_x0020_68 Text_x0020_Box_x0020_2 Text_x0020_Box_x0020_16 Text_x0020_Box_x0020_2 Text_x0020_Box_x0020_16 Text_x0020_Box_x0020_2 TextBox_x0020_10"><![endif]><!--[if mso & !supportInlineShapes & supportFields]><v:shape
+ id="_x0000_i1025" type="#_x0000_t75" style='width:538.45pt;height:105.15pt'>
+ <v:imagedata croptop="-65520f" cropbottom="65520f"/>
+</v:shape><span style='mso-element:field-end'></span><![endif]--><span
+style='font-size:12.0pt'><br>
+In the second state, cI434 levels are low, trpR levels are high, and cI levels
+are high. This results in low transcription from ptrpL, high transcription from
+pRM, and thus high output signal. Since trpR is a strong repressor for ptrpL,
 we expect state 2 to be stable.<o:p></o:p></span></p>
@@ Line 2,280: / Line 3,475: @@
 in order for the color to develop; the sequence is short (as compared to other
 pigment generating proteins); the protein itself generates the color, which
-hopefully will result in faster image development than a protein which catalyzes
+hopefully will result in faster image development than a protein which
-a reaction that generates color.<o:p></o:p></span></p>
+catalyzes a reaction that generates color.<o:p></o:p></span></p>
-<p class=MsoNormal style='text-indent:.5in'><span class=GramE><span
+<p class=MsoNormal style='text-indent:.5in'><span style='font-size:12.0pt'>mRFP1
-style='font-size:12.0pt'>mRFP1</span></span><span style='font-size:12.0pt'> is
+is a red fluorescent protein based on DsRed. Natural DsRed requires
-a red fluorescent protein based on <span class=SpellE>DsRed</span>. Natural <span
+tetramerization in order to fluoresce. mRFP1 contains 33 mutations that, one,
-class=SpellE>DsRed</span> requires <span class=SpellE>tetramerization</span> in
+allow it to function as a monomer and, two, allow it to fold more quickly. <o:p></o:p></span></p>
-order to fluoresce. <span class=GramE>mRFP1</span> contains 33 mutations that,
-one, allow it to function as a monomer and, two, allow it to fold more quickly.
-<o:p></o:p></span></p>
 </div>
@@ Line 2,296: / Line 3,488: @@
 </html>
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