| Literature DB >> 11891220 |
Fenglei Jiang1, Liang Yi, Misty Moore, Minyong Chen, Thomas Rohl, Klaas-Jan Van Wijk, Jan-Willem L De Gier, Ralph Henry, Ross E Dalbey.
Abstract
A new component of the bacterial translocation machinery, YidC, has been identified that specializes in the integration of membrane proteins. YidC is homologous to the mitochondrial Oxa1p and the chloroplast Alb3, which functions in a novel pathway for the insertion of membrane proteins from the mitochondrial matrix and chloroplast stroma, respectively. We find that Alb3 can functionally complement the Escherichia coli YidC depletion strain and promote the membrane insertion of the M13 procoat and leader peptidase that were previously shown to depend on the bacterial YidC for membrane translocation. In addition, the chloroplast Alb3 that is expressed in bacteria is essential for the insertion of chloroplast cpSecE protein into the bacterial inner membrane. Surprisingly, Alb3 is not required for the insertion of cpSecE into the thylakoid membrane. These results underscore the importance of Oxa1p homologs for membrane protein insertion in bacteria and demonstrate that the requirement for Oxa1p homologs is different in the bacterial and thylakoid membrane systems.Entities:
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Year: 2002 PMID: 11891220 DOI: 10.1074/jbc.M110857200
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157