Difference between revisions of "Part:BBa K811000"

(Usage and Biology)
(Usage and Biology)
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ClyA is a 34kDa protein that is composed primarily of α-helical bundles that form a rod-shaped molecule. The membrane insertion domain is known as a β tongue and is critical for hemolytic activity. If the β tongue is mutated, the hemolytic activity of clyA is abrogated.  
 
ClyA is a 34kDa protein that is composed primarily of α-helical bundles that form a rod-shaped molecule. The membrane insertion domain is known as a β tongue and is critical for hemolytic activity. If the β tongue is mutated, the hemolytic activity of clyA is abrogated.  
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The regulation of clyA secretion is not well characterized. To date, the method by which newly synthesized clyA is localized to the periplasm is unknown. All that is known about this process is that the secretion of clyA is not dependent on any known signal sequence, nor does it require cytolytic activity of clyA.
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===Characterization===
  
 
<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>

Revision as of 02:26, 6 October 2012

Cytolysin A (ClyA) Cytolysin A (ClyA) pore forming protein causes cell lysis.

Usage and Biology

ClyA is a protein native to E. coli, Shigella flexneri, and Salmonella typhi that is capable of forming 13-mer pore complexes in a redox-independent manner. Expression of clyA in the absence of other hemolytic toxins is sufficient to induce hemolysis experimentally, and is therefore considered to be a potent cytolytic agent. Unlike a similar protein, HlyA, ClyA is not synthesized as a protoxin, which requires further posttranslational modifications to become active. ClyA functional immediately following translation of mRNA to protein.

ClyA is a 34kDa protein that is composed primarily of α-helical bundles that form a rod-shaped molecule. The membrane insertion domain is known as a β tongue and is critical for hemolytic activity. If the β tongue is mutated, the hemolytic activity of clyA is abrogated.

The regulation of clyA secretion is not well characterized. To date, the method by which newly synthesized clyA is localized to the periplasm is unknown. All that is known about this process is that the secretion of clyA is not dependent on any known signal sequence, nor does it require cytolytic activity of clyA.

Characterization

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]