Difference between revisions of "Part:BBa K3187018"
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<partinfo>BBa_K3187018 short</partinfo>
 
<partinfo>BBa_K3187018 short</partinfo>
 
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<html>
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<p>
 
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<ul>
 
  
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                <h3>Profile</h3>
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                <table style=“width:80%“>
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                <tr>
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                <td><b>Name</b></td>
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                <td>PolyG Tag</td>
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                </tr>
  
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<li>Name: PolyG tag </li>
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                <tr>
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<li>bp: 12</li>
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                <td><b>Base pairs</b></td>
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<li>Da: 300</li>
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                <td> 12</td>
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<li>Properties: second sequence for Sortase A</li>
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                </tr>
  
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</ul>
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                <tr>
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</p>
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                <td><b>Molecular weight</b></td>
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                <td>300 Da</td>
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                </tr>
  
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<h4>Introduction:</h4>
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                <tr>
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<p>
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                <td><b>Origin</b></td>
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The enzyme Sortase A <partinfo>BBa_K3187016</partinfo> is able to form a peptide bond between a C-terminal LPXTG motif and a N-terminal poly glycine motif <sup>[1][2][3]</sup>. The DNA sequence below is coding for four glycines that can be used as the second recognition motif in a Sortase reaction.
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                <td> Synthetic </td>
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</p>
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                </tr>
  
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<img src="https://2019.igem.org/wiki/images/5/52/T--TU_DARMSTADT--invitro_UZ_TEM.png" style="width:40%;height:40%;">
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                <tr>
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                <td><b>Properties</b></td>
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                <td> second sequence for a Sortase A mediated reaction</td>
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<h4>Sequence:</h4>
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                </tr>
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<p>
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                </table>
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GGCggaggcggt
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                <h3> Usage and Biology</h3>
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                <p>
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The enzyme Sortase A is able to form a peptide bond between a C-terminal LPXTG motif and a N-terminal poly glycine motif
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<sup id="cite_ref-1” class=”reference">
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                            <a href="#cite_note-1">[1]
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                            </a>
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                    </sup>
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<sup id="cite_ref-2” class=”reference">
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                            <a href="#cite_note-2">[2]
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                            </a>
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                    </sup>  
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<sup id="cite_ref-3” class=”reference">
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                            <a href="#cite_note-3">[3]
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                            </a>  
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                    </sup>
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. The DNA sequence below is coding for four glycines that can be used as the second recognition motif in a Sortase reaction.
 
</p>
 
</p>
  
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<h4>References:</h4>
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<p>
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[1] Tsukiji, S. and Nagamune, T. (2009) Sortase-Mediated Ligation: A Gift from Gram-Positive Bacteria to Protein Engineering ChemBioChem
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<br>
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<br>
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[2] Proft, T. (2010) Sortase-mediated protein ligation: an emerging biotechnology tool for protein modification and immobilisation  
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<br>
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                    <h2>References</h2>
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<br>
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                    <ol class="references">
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                        <li id="cite_note-1">
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[3] Mao, H., Hart, S. A., Schink, A., and Pollok, B. A. (2004) Sortase-mediated protein ligation: a new method for protein engineering
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                            <span class="mw-cite-backlink">
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                                <a href="#cite_ref-1">↑</a>
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</p>  
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                            </span>
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                            <span class="reference-text">
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Lorem ipsum dolor sit amet, consetetur sadipscing elitr, sed diam nonumy eirmod tempor invidunt ut labore et dolore magna aliquyam erat, sed
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                            Tsukiji, S. and Nagamune, T. (2009) Sortase-Mediated Ligation: A Gift from Gram-Positive Bacteria to Protein Engineering
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diam voluptua. At vero eos et accusam et justo duo dolores et ea rebum. Stet clita kasd gubergren, no sea takimata sanctus est Lorem ipsum dolor sit amet. Lorem ipsum dolor sit amet, consetetur sadipscing elitr, sed diam nonumy eirmod tempor invidunt ut labore et dolore magna aliquyam erat, sed diam voluptua. At vero eos et accusam et justo duo dolores et ea rebum. Stet clita kasd gubergren, no sea takimata sanctus est Lorem ipsum dolor sit amet.
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                            <a rel="nofollow" class="external autonumber" href="https://doi.org/10.1002/cbic.200800724">[1] </a>
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                            </span>
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                        </li>
 +
                   
 +
                        <li id="cite_note-2">
 +
                            <span class="mw-cite-backlink">
 +
                                <a href="#cite_ref-2">↑</a>
 +
                            </span>
 +
                            <span class="reference-text">
 +
                                Proft, T. (2010) Sortase-mediated protein ligation: an emerging biotechnology tool for protein modification and immobilisation  
 +
                            <a rel="nofollow" class="external autonumber" href="https://doi.org/10.1007/s10529-009-0116-0">[2] </a>
 +
                            </span>
 +
                        </li>
  
 +
<li id="cite_note-3">
 +
                            <span class="mw-cite-backlink">
 +
                                <a href="#cite_ref-3">↑</a>
 +
                            </span>
 +
                            <span class="reference-text">
 +
                                Mao, H., Hart, S. A., Schink, A., and Pollok, B. A. (2004) Sortase-mediated protein ligation: a new method for protein engineering
 +
                            <a rel="nofollow" class="external autonumber" href="https://doi.org/10.1021/ja039915e">[3] </a>
 +
                            </span>
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                        </li>
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                    </ol>
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<partinfo>BBa_K3187016</partinfo>
 
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<!-- Add more about the biology of this part here -->
 
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===Usage and Biology===
 
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<img src="https://2019.igem.org/wiki/images/5/52/T--TU_DARMSTADT--invitro_UZ_TEM.png" alt="Italian Trulli" style="width:40%;height:40%;">
 
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>

Revision as of 10:01, 16 October 2019


PolyG Tag (GGGG) for Sortase-mediated Ligation

Profile

Name PolyG Tag
Base pairs 12
Molecular weight 300 Da
Origin Synthetic
Properties second sequence for a Sortase A mediated reaction

Usage and Biology

The enzyme Sortase A is able to form a peptide bond between a C-terminal LPXTG motif and a N-terminal poly glycine motif [1] [2] [3] . The DNA sequence below is coding for four glycines that can be used as the second recognition motif in a Sortase reaction.

References

  1. ↑ Tsukiji, S. and Nagamune, T. (2009) Sortase-Mediated Ligation: A Gift from Gram-Positive Bacteria to Protein Engineering [1]
  2. ↑ Proft, T. (2010) Sortase-mediated protein ligation: an emerging biotechnology tool for protein modification and immobilisation [2]
  3. ↑ Mao, H., Hart, S. A., Schink, A., and Pollok, B. A. (2004) Sortase-mediated protein ligation: a new method for protein engineering [3]

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]