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The conserved third transmembrane segment of YidC contacts nascent Escherichia coli inner membrane proteins.


ABSTRACT: Escherichia coli YidC is a polytopic inner membrane protein that plays an essential and versatile role in the biogenesis of inner membrane proteins. YidC functions in Sec-dependent membrane insertion but acts also independently as a separate insertase for certain small membrane proteins. We have used a site-specific cross-linking approach to show that the conserved third transmembrane segment of YidC contacts the transmembrane domains of both nascent Sec-dependent and -independent substrates, indicating a generic recognition of insertion intermediates by YidC. Our data suggest that specific residues of the third YidC transmembrane segment alpha-helix is oriented toward the transmembrane domains of nascent inner membrane proteins that, in contrast, appear quite flexibly positioned at this stage in biogenesis.

SUBMITTER: Yu Z 

PROVIDER: S-EPMC3259860 | biostudies-other | 2008 Dec

REPOSITORIES: biostudies-other

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The conserved third transmembrane segment of YidC contacts nascent Escherichia coli inner membrane proteins.

Yu Zhong Z   Koningstein Gregory G   Pop Ana A   Luirink Joen J  

The Journal of biological chemistry 20081006 50


Escherichia coli YidC is a polytopic inner membrane protein that plays an essential and versatile role in the biogenesis of inner membrane proteins. YidC functions in Sec-dependent membrane insertion but acts also independently as a separate insertase for certain small membrane proteins. We have used a site-specific cross-linking approach to show that the conserved third transmembrane segment of YidC contacts the transmembrane domains of both nascent Sec-dependent and -independent substrates, in  ...[more]

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