Difference between revisions of "Part:BBa K3429001"

 
(16 intermediate revisions by one other user not shown)
Line 1: Line 1:
  
 
__NOTOC__
 
__NOTOC__
<partinfo>BBa_K3429001 short</partinfo>
+
<partinfo>BBa_K3429001 short</partinfo>  
  
TasA protein  
+
<h2>Profile</h2>
 +
            <table style=“width:80%“>
 +
                <tr>
 +
                    <td><b>Name</b></td>
 +
                    <td>TasA matrix protein</td>
 +
                </tr>
 +
                <tr>
 +
                    <td><b>Base pairs</b></td>
 +
                    <td>786</td>
 +
                </tr>
 +
                <tr>
 +
                    <td><b>Molecular weight</b></td>
 +
                    <td>28.15&nbsp;kDa</td>
 +
                </tr>
 +
                <tr>
 +
                    <td><b>Origin</b></td>
 +
                    <td><i>Bacillus subtilis</i></td>
 +
                </tr>
 +
            </table>
  
<br>  
+
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<sup>[1, 2]</sup>.  <br> We designed TasA fusion proteins with CotA, CueO 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 particle (sec-SRP) pathway<sup>[3]</sup>.
  
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. <sup> [1] </sup>
 
                             
 
                   
 
  
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">
 
                           
 
 
<sup id="cite_ref-3” class=”reference">
 
                            <a href="#cite_note-3">[3]
 
                            </a>
 
                    </sup>
 
 
<br>
 
  
 
<h2>References</h2>
 
<h2>References</h2>
  
 +
[1] 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, https://doi.org/10.1111/j.1365-2958.2005.05020.x
 
<br>
 
<br>
  
[1] 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 href="https://2020.igem.org/Team:TU_Darmstadt/Model/Enzyme_Modeling#EreB_CM">hallo</a>
+
[2] 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, https://doi.org/10.1073/pnas.0910560107x
 
+
<br>
+
 
+
[2] 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 href = https://2020.igem.org/Team:TU_Darmstadt/Model/Enzyme_Modeling#EreB_CM></a>
+
 
+
 
<br>
 
<br>
  
[3] 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.
+
[3] 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, https://doi.org/10.1128/JB.181.5.1664-1672.1999
 
                              
 
                              
  

Latest revision as of 09:27, 26 October 2020


TasA matrix protein

Profile

Name TasA matrix protein
Base pairs 786
Molecular weight 28.15 kDa
Origin Bacillus subtilis

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[1, 2].
We designed TasA fusion proteins with CotA, CueO 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 particle (sec-SRP) pathway[3].


References

[1] 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, https://doi.org/10.1111/j.1365-2958.2005.05020.x

[2] 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, https://doi.org/10.1073/pnas.0910560107x

[3] 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, https://doi.org/10.1128/JB.181.5.1664-1672.1999


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]