Difference between revisions of "Part:BBa K3429001"
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The TasA protein (also known as the major biofilm matrix component) is essential for biofilm structures and polymerizes into long fibers attached to the B. subtilis cells. We designed TasA fusion proteins with CotA, CuO and EreB to immobilize our degrading enzymes while producing a high number of fusion proteins. Protein secretion into the biofilm matrix is regulated by the Sec-dependent signal recognition partice (sec-SRP) pathway.  
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The TasA protein (also known as the major biofilm matrix component) is essential for biofilm structures and polymerizes into long fibers attached to the B. subtilis cells. <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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We designed TasA fusion proteins with CotA, CuO and EreB to immobilize our degrading enzymes in the biofilm matrix. Protein secretion into the biofilm matrix is regulated by the Sec-dependent signal recognition partice (sec-SRP) pathway. <sup id="cite_ref-1” class=”reference">
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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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<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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                                Branda, S.; Chu, F.; Kearns, D. (2006): A major protein component of the Bacillus subtilis biofilm matrix. In: Molecular microbiology 59 (4), S. 1229–1238, DOI 10.1111/j.1365-2958.2005.05020.x.
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                            <a rel="nofollow" class="external autonumber" href="https://doi.org/10.1111/j.1365-2958.2005.05020.x.">[3] </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">
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                                Romero, D.; Aguilar, C.; Losick, R. (2010): Amyloid fibers provide structural integrity to Bacillus subtilis biofilms. In: Proceedings of the National Academy of Sciences of the United States of America 107 (5), S. 2230–2234,DOI 10.1073/pnas.0910560107x.
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                            <a rel="nofollow" class="external autonumber" href="https://doi.org/10.1073/pnas.0910560107x.">[2] </a>
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                            </span>
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                        </li>
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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">
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                                Stöver, A.; Driks, A. (1999): Secretion, Localization, and Antibacterial Activity of TasA, a Bacillus subtilis Spore-Associated Protein. In: Journal of Bacteriology 181 (5), S. 1664–1672.
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                            <a rel="nofollow" class="external autonumber" href="https://doi.org/10.1111/j.1365-2958.2005.05020.x.">[3] </a>
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                            </span>
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                        </li>
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                    </ol>
  
 
<!-- Add more about the biology of this part here
 
<!-- Add more about the biology of this part here

Revision as of 13:52, 25 October 2020


TasA matrix protein

TasA protein


The TasA protein (also known as the major biofilm matrix component) is essential for biofilm structures and polymerizes into long fibers attached to the B. subtilis cells. <a href="#cite_note-1">[1] 

                            </a> 
                   </sup> 


                           <a href="#cite_note-2">[2]
                            </a>

We designed TasA fusion proteins with CotA, CuO and EreB to immobilize our degrading enzymes in the biofilm matrix. Protein secretion into the biofilm matrix is regulated by the Sec-dependent signal recognition partice (sec-SRP) pathway. 


                           <a href="#cite_note-3">[3]
                            </a>


References

  1. <a href="#cite_ref-1">↑</a> Branda, S.; Chu, F.; Kearns, D. (2006): A major protein component of the Bacillus subtilis biofilm matrix. In: Molecular microbiology 59 (4), S. 1229–1238, DOI 10.1111/j.1365-2958.2005.05020.x. <a rel="nofollow" class="external autonumber" href="https://doi.org/10.1111/j.1365-2958.2005.05020.x.">[3] </a>
  2. <a href="#cite_ref-2">↑</a> Romero, D.; Aguilar, C.; Losick, R. (2010): Amyloid fibers provide structural integrity to Bacillus subtilis biofilms. In: Proceedings of the National Academy of Sciences of the United States of America 107 (5), S. 2230–2234,DOI 10.1073/pnas.0910560107x. <a rel="nofollow" class="external autonumber" href="https://doi.org/10.1073/pnas.0910560107x.">[2] </a>
  3. <a href="#cite_ref-3">↑</a> Stöver, A.; Driks, A. (1999): Secretion, Localization, and Antibacterial Activity of TasA, a Bacillus subtilis Spore-Associated Protein. In: Journal of Bacteriology 181 (5), S. 1664–1672. <a rel="nofollow" class="external autonumber" href="https://doi.org/10.1111/j.1365-2958.2005.05020.x.">[3] </a>

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]