Difference between revisions of "Team:NTU-LIHPAO-Taiwan/Parts"

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{{NTU-LIHPAO-Taiwan}}
 
 
<html>
 
<html>
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<head>
  
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<h2> Part Documentation</h2>
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<script src="https://ajax.googleapis.com/ajax/libs/jquery/1.6.2/jquery.min.js"></script>
  
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<p>Each team will make new parts during iGEM and will submit them to the Registry of Standard Biological Parts. The iGEM software provides an easy way to present the parts your team has created. The <code>&lt;groupparts&gt;</code> tag (see below) will generate a table with all of the parts that your team adds to your team sandbox.</p>
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<script type="text/javascript" charset="utf-8">
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<p>Remember that the goal of proper part documentation is to describe and define a part, so that it can be used without needing to refer to the primary literature. Registry users in future years should be able to read your documentation and be able to use the part successfully. Also, you should provide proper references to acknowledge previous authors and to provide for users who wish to know more.</p>
+
  
 +
//-----Hover Facebook Icon-----//
 +
$(document).ready(function(){
 +
$('#Facebook_icon_hover').hover(function () {
 +
this.src = "https://static.igem.org/mediawiki/2015/3/35/NTU-Top-Facebook_icon2.png";
 +
}, function () {
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this.src = "https://static.igem.org/mediawiki/2015/9/98/NTU-Top-Facebook_icon1.png";
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});
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});
  
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<div class="highlightBox">
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//-----Hover iGem Icon-----//
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<h4>Note</h4>
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$(document).ready(function(){
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<p>Note that parts must be documented on the <a href="http://parts.igem.org/Main_Page"> Registry</a>. This page serves to <i>showcase</i> the parts you have made. Future teams and other users and are much more likely to find parts by looking in the Registry than by looking at your team wiki.</p>
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</div>
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this.src = "https://static.igem.org/mediawiki/2015/0/0a/NTU-Top-iGEM_icon2.png";
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});
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});
  
 +
</script>
  
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<h4>Adding parts to the registry</h4>
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<meta http-equiv="Content-Type" content="text/html; charset=utf-8" />
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<p>You can add parts to the Registry at our <a href="http://parts.igem.org/Add_a_Part_to_the_Registry">Add a Part to the Registry</a> link.</p>
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<title>NTU-LIHPAO-Taiwan</title>
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<p>We encourage teams to start completing documentation for their parts on the Registry as soon as you have it available. The sooner you put up your parts, the better you will remember all the details about your parts. Remember, you don't need to send us the DNA sample before you create an entry for a part on the Registry. (However, you <b>do</b> need to send us the DNA sample before the Jamboree. If you don't send us a DNA sample of a part, that part will not be eligible for awards and medal criteria.)</p>
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<style type="text/css">
  
 +
/*-------------------------------------------*/
 +
/*--------------Wiki Page Reset--------------*/
 +
/*-------------------------------------------*/
  
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<h4>What information do I need to start putting my parts on the Registry?</h4>
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<p>The information needed to initially create a part on the Registry is:</p>
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display: none;
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<ul>
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}
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<li>Part Name</li>
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<li>Part type</li>
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<li>Creator</li>
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−
<li>Sequence</li>
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<li>Short Description (60 characters on what the DNA does)</li>
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<li>Long Description (Longer description of what the DNA does)</li>
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<li>Design considerations</li>
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</ul>
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<p>
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#globalWrapper, #content {
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We encourage you to put up <em>much more</em> information as you gather it over the summer. If you have images, plots, characterization data and other information, please also put it up on the part page. </p>
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<h4>Inspiration</h4>
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<p>We have a created  a <a href="http://parts.igem.org/Well_Documented_Parts">collection of well documented parts</a> that can help you get started.</p>
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<p> You can also take a look at how other teams have documented their parts in their wiki:</p>
+
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<ul>
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<li><a href="https://2014.igem.org/Team:MIT/Parts"> 2014 MIT </a></li>
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<li><a href="https://2014.igem.org/Team:Heidelberg/Parts"> 2014 Heidelberg</a></li>
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<li><a href="https://2014.igem.org/Team:Tokyo_Tech/Parts">2014 Tokyo Tech</a></li>
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−
<h4>Part Table </h4>
 
−
</html>
 
−
<groupparts>iGEM015 Example</groupparts>
 
−
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<span class="title">Prototype</span>
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<ul class="sub-Content">
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<li><a href="#First">Prototype</a></li>
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</ul>
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</li>
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<li>
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<span class="title">Main Part</span>
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<ul class="sub-Content">
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<li><a href="#Second1">Part:BBa_K1841001</a></li>
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<li><a href="#Second2">Part:BBa_K1841004</a></li>
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<li><a href="#Second3">Part:BBa_K1841007</a></li>
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</ul>
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<li>
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<span class="title">Test Part</span>
 +
<ul class="sub-Content">
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<li><a href="#Third1">RFP</a></li>
 +
<li><a href="#Third2">His-PYY</a></li>
 +
<li><a href="#Third3">Signal peptide-PYY-His</a></li>
 +
<li><a href="#Third4">Y2R</a></li>
 +
</ul>
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</li>
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<li>
 +
<span class="title">References</span>
 +
<ul class="sub-Content">
 +
<li><a href="#Fourth">References</a></li>
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<div class="Text1">Prototype</div>
 +
<div class="Text2" id="First">Prototype</div>
 +
<div class="Text3">
 +
The iGEM Team NTU-LIHPAO-Taiwan 2015 had built a new biological system for the iGEM community. The original design of the system making up the (Product) contains the three elements listed below, in a probiotic – <i>Lactobacillus casei</i> ATCC 393.
 +
</div>
 +
<div class="Container_Article_Picture1">
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<div class="Article_Picture1">
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<img src="https://static.igem.org/mediawiki/2015/a/a8/NTU_LASMID.jpg" width="368px"/>
 +
<div class="Article_PictureText1"><div class="Text_Picture">[Fig.1-1] Designed Plasmid</div></div>
 +
</div>
 +
</div>
 +
 +
<div class="Text1">Main Part</div>
 +
<div class="Text2" id="Second1">Part: BBa_K1841001</div>
 +
<div class="Text3"><div class="Text_TitleUnderline">nisI</div></div>
 +
<div class="Text3">
 +
Research from Torsten <i>et al.</i> revealed that the highest level of acquired nisin tolerance was achieved after coordinated expression of all four nisin immunity genes, containing <i>nisI</i>, <i>nisF</i>, <i>nisE</i>, and <i>nisG</i>.<a href="#Reference1">[1]</a>  Functional analyses provided evidence that NisI acts as a nisin-sequestering protein and that NisFEG acts as a nisin exporter that expels nisin molecules from the cytoplasmic membrane into the environment.
 +
</div>
 +
<div class="Container_Article_Picture">
 +
<div class="Article_Picture">
 +
<img src="https://static.igem.org/mediawiki/2015/3/34/NTU-Team-nisI.jpg" width="480px"/>
 +
<div class="Article_PictureText"><div class="Text_Picture">[Fig.2-1] Nisin Selection</div></div>
 +
</div>
 +
</div>
 +
<div class="Text2" id="Second2">Part: BBa_K1841004</div>
 +
<div class="Text3"><div class="Text_TitleUnderline">plac promoter</div></div>
 +
<div class="Text3">
 +
Lactose operon of <i>Lactobacillus casei</i> In <i>Lactobacillus casei</i> ATCC393 [pLZ15–], the lactose genes are grouped in a cluster transcribed as single operon. The cluster lacTEGF encodes an antiterminator protein (LacT), lactose-specific elements (LacE and LacF) of the phosphotransferase system (PTS) and a phospho-β-galactosidase (LacG).
 +
The promoter region contains a cre element (catabolite responsive element) overlapping the –35 region, which is followed by a highly conserved sequence, the ribonucleic antiterminator (RAT) sequence, and a terminator structure.
 +
The antiterminator activity of LacT is also negatively controlled by glucose, possibly by PTS-mediated phosphorylation as explained below.<a href="#Reference2">[2]</a>
 +
<div class="Container_Article_Picture">
 +
<div class="Article_Picture">
 +
<img src="https://static.igem.org/mediawiki/2015/a/a4/NTU-Team-plac-cl.jpg" width="480px"/>
 +
<div class="Article_PictureText"><div class="Text_Picture">[Fig.2-2-1] Suicide Sense Part</div></div>
 +
</div>
 +
</div>
 +
<div class="Container_Article_Picture">
 +
<div class="Article_Picture">
 +
<img src="https://static.igem.org/mediawiki/2015/9/9a/NTU-Team-nuca.jpg" width="480px"/>
 +
<div class="Article_PictureText"><div class="Text_Picture">[Fig.2-2-2] Suicide Kill Part</div></div>
 +
</div>
 +
</div>
 +
<div class="Text2" id="Second3">Part: BBa_K1841007</div>
 +
<div class="Text3"><div class="Text_TitleUnderline">TAT-PYY</div></div>
 +
<div class="Text3">
 +
TAT can bring the big molecule substance like DNA, protein, peptide to penetrate the cell. Usually, named as protein transduction domain or membrane transduction domain, it is less than 40 amino acid.<a href="#Reference3">[3]</a> PYY belongs to the gastrointestinal hormones. Once the intestine detects the nutrition, the epidermal cell, L cell of ileum and colon will secrete the PYY. While the blood pass the hypothalamus, PYY will bind to the neuropeptide Y receptor in ventromedial nuclei causing the sense of satiation.<a href="#Reference4">[4]</a>
 +
</div>
 +
<div class="Container_Article_Picture">
 +
<div class="Article_Picture">
 +
<img src="https://static.igem.org/mediawiki/2015/6/6a/NTU-Team-tat-pyy-his.jpg" width="480px"/>
 +
<div class="Article_PictureText"><div class="Text_Picture">[Fig.2-3] Cell penetrating peptide + PYY</div></div>
 +
</div>
 +
</div>
 +
<div class="Text3">
 +
In this part, we use the constitutive promoter BBa_J23100 to produce signal peptide-PYY-histidine fusion protein. With the His-tag, we can easily purify the signal peptide-PYY from other non-His-tag protein. This part is constructed to test the amount of the PYY that can secret out of the <i>L. casei</i>.
 +
</div>
 +
<div class="Text1">Test Part</div>
 +
<div class="Text2" id="Third1">RFP</div>
 +
<div class="Container_Article_Picture">
 +
<div class="Article_Picture">
 +
<img src="https://static.igem.org/mediawiki/2015/4/4d/NTU-Team-plac-gfp.jpg" width="480px"/>
 +
<div class="Article_PictureText"><div class="Text_Picture">[Fig.3-1] Suicide sense test</div></div>
 +
</div>
 +
</div>
 +
<div class="Text3">
 +
In this part, we use the RFP protein to testify the function of the lactose operon.
 +
</div>
 +
<div class="Text2" id="Third2">His-PYY</div>
 +
<div class="Container_Article_Picture">
 +
<div class="Article_Picture">
 +
<img src="https://static.igem.org/mediawiki/2015/1/12/NTU-Team-his-pyy.jpg" width="480px"/>
 +
<div class="Article_PictureText"><div class="Text_Picture">[Fig.3-2] PYY</div></div>
 +
</div>
 +
</div>
 +
<div class="Text3">
 +
In this part, we use the constitutive promoter BBa_J23100 to produce histidine-PYY fusion protein. With the His-tag, we can easily purify the PYY from other non-His-tag protein. This part is constructed to test the amount of the PYY under the constitutive promoter in the <i>L. casei</i>.
 +
</div>
 +
<div class="Text2" id="Third3">Signal peptide-PYY-His</div>
 +
<div class="Container_Article_Picture">
 +
<div class="Article_Picture">
 +
<img src="https://static.igem.org/mediawiki/2015/3/39/NTU-Team-sp-pyy-his.jpg" width="480px"/>
 +
<div class="Article_PictureText"><div class="Text_Picture">[Fig.3-3] Signal peptide + PYY</div></div>
 +
</div>
 +
</div>
 +
<div class="Text3">
 +
In this part, we use the constitutive promoter BBa_J23100 to produce signal peptide-PYY-histidine fusion protein. With the His-tag, we can easily purify the signal peptide-PYY from other non-His-tag protein. This part is constructed to test the amount of the PYY that can secret out of the <i>L. casei</i>.
 +
</div>
 +
<div class="Text2" id="Third4">Y2R</div>
 +
<div class="Container_Article_Picture">
 +
<div class="Article_Picture">
 +
<img src="https://static.igem.org/mediawiki/2015/e/ea/NTU-Team-y2r.jpg" width="480px"/>
 +
<div class="Article_PictureText"><div class="Text_Picture">[Fig.3-4] Y2R</div></div>
 +
</div>
 +
</div>
 +
<div class="Text3">
 +
In this part, we use the constitutive promoter BBa_J23100 to produce Y2R. This part is constructed to verify the function of PYY.
 +
</div>
 +
<div class="Text1">References</div>
 +
<div class="Text2" id="Fourth">References</div>
 +
<div class="Text3" id="Reference1">
 +
[1] Torsten, S., Stefan, H., Irina, S., and K. D. Entian. Function of Lactococcus lactis Nisin Immunity Genes nisI and nisFEG after Coordinated Expression in the Surrogate Host Bacillus subtilis. The Jurnal of Biological Chemistry, USA. , Vol. 278, pp. 89 -94 (2003)
 +
</div>
 +
<div class="Text3" id="Reference2">
 +
[2] Yu-Kuo Tsai, Hung- Wen Chen, Ta-Chun Lo and Thy-Hou Lin. Specific point mutation in <i>Lactobacillus casei</i> ATCC 27139 cause the phenotype switch from Lac- to Lac+. Microbiology, pp. 751-760(2009)
 +
</div>
 +
<div class="Text3" id="Reference3">
 +
[3] Ju-Chen Cheng, 2009, Investigation on the Characteristic of Heparin-Binding Haemagglutinin 3 Adhesin (HBHA)-Related Peptides and their Transcytosis
 +
</div>
 +
<div class="Text3" id="Reference4">
 +
[4] C. W. le Roux and S. R. Bloom. Peptide YY, appetite and food intake.(2005)
 +
</div>
 +
 +
<div class="Container_Bottom1"></div>
 +
<div class="Container_Bottom2">
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<div id="LIHPAO_logo"><a href="http://www.llsc.com.tw/"><img src="https://static.igem.org/mediawiki/2015/d/d4/LIHPAO_logo.png" style="max-width: 100%; max-height: 70px"/></a></div>
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<div id="NTUBST_logo"><a href="http://www.bst.ntu.edu.tw/BST-new/NTUBST.html"><img src="https://static.igem.org/mediawiki/2015/6/68/NTUBST_logo.png" style="max-width: 100%; max-height: 70px"/></a></div>
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 +
Maintained by the iGEM team NTU-LIHPAO-Taiwan&nbsp;&nbsp;&nbsp;&nbsp;©2015 NTU-LIHPAO-Taiwan
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Latest revision as of 13:19, 18 September 2015

NTU-LIHPAO-Taiwan

Prototype
Prototype
The iGEM Team NTU-LIHPAO-Taiwan 2015 had built a new biological system for the iGEM community. The original design of the system making up the (Product) contains the three elements listed below, in a probiotic – Lactobacillus casei ATCC 393.
[Fig.1-1] Designed Plasmid
Main Part
Part: BBa_K1841001
nisI
Research from Torsten et al. revealed that the highest level of acquired nisin tolerance was achieved after coordinated expression of all four nisin immunity genes, containing nisI, nisF, nisE, and nisG.[1] Functional analyses provided evidence that NisI acts as a nisin-sequestering protein and that NisFEG acts as a nisin exporter that expels nisin molecules from the cytoplasmic membrane into the environment.
[Fig.2-1] Nisin Selection
Part: BBa_K1841004
plac promoter
Lactose operon of Lactobacillus casei In Lactobacillus casei ATCC393 [pLZ15–], the lactose genes are grouped in a cluster transcribed as single operon. The cluster lacTEGF encodes an antiterminator protein (LacT), lactose-specific elements (LacE and LacF) of the phosphotransferase system (PTS) and a phospho-β-galactosidase (LacG). The promoter region contains a cre element (catabolite responsive element) overlapping the –35 region, which is followed by a highly conserved sequence, the ribonucleic antiterminator (RAT) sequence, and a terminator structure. The antiterminator activity of LacT is also negatively controlled by glucose, possibly by PTS-mediated phosphorylation as explained below.[2]
[Fig.2-2-1] Suicide Sense Part
[Fig.2-2-2] Suicide Kill Part
Part: BBa_K1841007
TAT-PYY
TAT can bring the big molecule substance like DNA, protein, peptide to penetrate the cell. Usually, named as protein transduction domain or membrane transduction domain, it is less than 40 amino acid.[3] PYY belongs to the gastrointestinal hormones. Once the intestine detects the nutrition, the epidermal cell, L cell of ileum and colon will secrete the PYY. While the blood pass the hypothalamus, PYY will bind to the neuropeptide Y receptor in ventromedial nuclei causing the sense of satiation.[4]
[Fig.2-3] Cell penetrating peptide + PYY
In this part, we use the constitutive promoter BBa_J23100 to produce signal peptide-PYY-histidine fusion protein. With the His-tag, we can easily purify the signal peptide-PYY from other non-His-tag protein. This part is constructed to test the amount of the PYY that can secret out of the L. casei.
Test Part
RFP
[Fig.3-1] Suicide sense test
In this part, we use the RFP protein to testify the function of the lactose operon.
His-PYY
[Fig.3-2] PYY
In this part, we use the constitutive promoter BBa_J23100 to produce histidine-PYY fusion protein. With the His-tag, we can easily purify the PYY from other non-His-tag protein. This part is constructed to test the amount of the PYY under the constitutive promoter in the L. casei.
Signal peptide-PYY-His
[Fig.3-3] Signal peptide + PYY
In this part, we use the constitutive promoter BBa_J23100 to produce signal peptide-PYY-histidine fusion protein. With the His-tag, we can easily purify the signal peptide-PYY from other non-His-tag protein. This part is constructed to test the amount of the PYY that can secret out of the L. casei.
Y2R
[Fig.3-4] Y2R
In this part, we use the constitutive promoter BBa_J23100 to produce Y2R. This part is constructed to verify the function of PYY.
References
References
[1] Torsten, S., Stefan, H., Irina, S., and K. D. Entian. Function of Lactococcus lactis Nisin Immunity Genes nisI and nisFEG after Coordinated Expression in the Surrogate Host Bacillus subtilis. The Jurnal of Biological Chemistry, USA. , Vol. 278, pp. 89 -94 (2003)
[2] Yu-Kuo Tsai, Hung- Wen Chen, Ta-Chun Lo and Thy-Hou Lin. Specific point mutation in Lactobacillus casei ATCC 27139 cause the phenotype switch from Lac- to Lac+. Microbiology, pp. 751-760(2009)
[3] Ju-Chen Cheng, 2009, Investigation on the Characteristic of Heparin-Binding Haemagglutinin 3 Adhesin (HBHA)-Related Peptides and their Transcytosis
[4] C. W. le Roux and S. R. Bloom. Peptide YY, appetite and food intake.(2005)
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