Difference between revisions of "Part:BBa K2036001"

Revision as of 07:19, 28 September 2016

CIII

Inhibitor of Ftsh( ATP-dependent host metalloprotease).
The CIII protein encoded by the temperate coliphage lambda acts as an inhibitor of the ubiquitous Escherichia coli metalloprotease HflB (FtsH). This inhibition results in the stabilization of transcription factor lambdaCII, thereby helping the phage to lysogenize the host bacterium.LambdaCIIIalso protects sigma(32), another specific substrate of HflB.
It have be recently shown that the protection of CII from HflB by CIII involves direct CIII-HflB binding, without any interaction between CII and CIII. Such a mode of action for lambdaCIII would be independent of the HflBsubstrate. In this study, we tested the ability of CIII to protect sigma(32) from HflB digestion. The inhibition of HflB-mediated proteolysis of sigma(32) by CIII is very similar to that of lambdaCII, characterized by an enhanced protection by the core CIII peptide CIIIC (amino acids 14-41 oflambdaCIII) and a lack of interaction between sigma(32) and CIII. 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]

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 <partinfo>BBa_K2036001 short</partinfo>
-inhibitor of Ftsh( ATP-dependent host metalloprotease).
+Inhibitor of Ftsh( ATP-dependent host metalloprotease).
 <br>The CIII protein encoded by the temperate coliphage lambda acts as an inhibitor of the ubiquitous Escherichia coli metalloprotease HflB (FtsH). This inhibition results in the stabilization of transcription factor lambdaCII, thereby helping the phage to lysogenize the host bacterium.LambdaCIIIalso protects sigma(32), another specific substrate of HflB.
 <br>It have be recently shown that the protection of CII from HflB by CIII involves direct CIII-HflB binding, without any interaction between CII and CIII. Such a mode of action for lambdaCIII would be independent of the HflBsubstrate. In this study, we tested the ability of CIII to protect sigma(32) from HflB digestion. The inhibition of HflB-mediated proteolysis of sigma(32) by CIII is very similar to that of lambdaCII, characterized by an enhanced protection by the core CIII peptide CIIIC (amino acids 14-41 oflambdaCIII) and a lack of interaction between sigma(32) and CIII.