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Caf1M assists in the assembly of Caf1 molecules into the chain-like structure. Specifically, Caf1M is a molecular chaperone, a protein assisting the folding or unfolding of large proteins. Without Caf1M, Caf1 molecules might aggregate together by sticking their sticky ends together, losing the chain-like structure into a long polymer. In order to preserve the chain-like structure for limiting the movement of P. acne bacteria, Caf1M is needed to assembly Caf1 molecules.  
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===What is it?===
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Caf1M assists in the assembly of Caf1 molecules into the chain-like structure. Specifically, Caf1M is a molecular chaperone, a protein assisting the folding or unfolding of large proteins. Without Caf1M, Caf1 molecules might aggregate together by sticking their sticky ends together, losing the chain-like structure into a long polymer. In order to preserve the chain-like structure for limiting the movement of P. acne bacteria, Caf1M is needed to assembly Caf1 molecules.
  
 
===Usage and Biology===
 
===Usage and Biology===
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     <td align="center"><img src="https://static.igem.wiki/teams/4897/wiki/parts/caf1m-explanation.png" width="900" height="auto" /> </td>
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Latest revision as of 13:12, 9 October 2023

Caf1M

What is it?

Caf1M assists in the assembly of Caf1 molecules into the chain-like structure. Specifically, Caf1M is a molecular chaperone, a protein assisting the folding or unfolding of large proteins. Without Caf1M, Caf1 molecules might aggregate together by sticking their sticky ends together, losing the chain-like structure into a long polymer. In order to preserve the chain-like structure for limiting the movement of P. acne bacteria, Caf1M is needed to assembly Caf1 molecules.

Usage and Biology

Fig. 1. Structure and Function of Caf1M.
Caf1M can preclude the aggregation of subunits by capping the extensive hydrophobic surface of activated Caf1 [1]. It delivers one Caf1 molecule at a time to the outer membrane usher, Caf1A, to assemble the monomers into polymers.

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]


References

[1]Zavialov, A. V., & Knight, S. D. (2007). A novel self-capping mechanism controls aggregation of periplasmic chaperone Caf1M. Molecular Microbiology, 64(1), 153–164. https://doi.org/10.1111/j.1365-2958.2007.05644.x
[2] Peters, D. T., Waller, H., Birch, M., & Lakey, J. H. (2019). Engineered mosaic protein polymers; a simple route to multifunctional biomaterials. Journal of Biological Engineering, 13(1). https://doi.org/10.1186/s13036-019-0183-2