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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<p>
 
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<ul>
 
  
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<li>Name: PolyG tag </li>
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                <h3>Profile</h3>
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<li>bp: 12</li>
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                <table style=“width:80%“>
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<li>Da: 300</li>
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                <tr>
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<li>Properties: second sequence for Sortase A</li>
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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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</ul>
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                <tr>
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</p>
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                <td><b>Base pairs</b></td>
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                <td> 12</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>Molecular weight</b></td>
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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 <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>300 Da</td>
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</p>
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                </tr>
  
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                <tr>
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                <td><b>Origin</b></td>
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                <td> Synthetic </td>
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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” alt="Italian Trulli">
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[[Image:https://2019.igem.org/wiki/images/5/52/T--TU_DARMSTADT--invitro_UZ_TEM.png|450px|thumb|left|'''Figure 1:''' Fermentation]]
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                </table>
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                <h3> Usage and Biology</h3>
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<h4>Sequence:</h4>
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                <p>
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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 <a href="https://parts.igem.org/Part:BBa_K3187019">
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GGCggaggcggt
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(BBa_K3187019)</a> and a N-terminal poly glycine motif (<a href="https://parts.igem.org/Part:BBa_K3187018"target="_blank">BBa_K3187018</a>)
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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 sequence below is coding for four glycines that can be used as the second recognition motif in a sortase-mediated reaction. For more results visit <a
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                    href="https://parts.igem.org/Part:BBa_K3187028"
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                    target="_blank">BBa_K3187028</a>
 
</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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<br>
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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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                    <h2>References</h2>
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                    <ol class="references">
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                        <li id="cite_note-1">
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                            <span class="mw-cite-backlink">
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                                <a href="#cite_ref-1">↑</a>
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                            </span>
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                            <span class="reference-text">
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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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                            <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>
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                        <li id="cite_note-2">
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                            <span class="mw-cite-backlink">
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                                <a href="#cite_ref-2">↑</a>
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                            </span>
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                            <span class="reference-text">
 +
                                Proft, T. (2010) Sortase-mediated protein ligation: an emerging biotechnology tool for protein modification and immobilisation
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                            <a rel="nofollow" class="external autonumber" href="https://doi.org/10.1007/s10529-009-0116-0">[2] </a>
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                            </span>
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                        </li>
  
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</p>  
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<li id="cite_note-3">
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                            <span class="mw-cite-backlink">
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                                <a href="#cite_ref-3">↑</a>
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                            </span>
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                            <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
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                            <a rel="nofollow" class="external autonumber" href="https://doi.org/10.1021/ja039915e">[3] </a>
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                            </span>
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                        </li>
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                    </ol>
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</html>
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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">
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Latest revision as of 17:51, 21 October 2019


PolyG Tag (GGGG) for Sortase-mediated Ligation

Profile

Name PolyG-tag
Base pairs 12
Molecular weight 300 Da
Origin Synthetic

Usage and Biology

The enzyme Sortase A is able to form a peptide bond between a C-terminal LPXTG motif (BBa_K3187019) and a N-terminal poly glycine motif (BBa_K3187018) [1] [2] [3] . The sequence below is coding for four glycines that can be used as the second recognition motif in a sortase-mediated reaction. For more results visit BBa_K3187028

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]