共 20 条
Functioning of outer membrane protein assembly factor Omp85 requires a single POTRA domain
被引:92
作者:

Bos, Martine P.
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机构:
Univ Utrecht, Inst Biomembranes, Dept Mol Microbiol, NL-3584 CH Utrecht, Netherlands Univ Utrecht, Inst Biomembranes, Dept Mol Microbiol, NL-3584 CH Utrecht, Netherlands

Robert, Viviane
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机构:
Univ Utrecht, Inst Biomembranes, Dept Mol Microbiol, NL-3584 CH Utrecht, Netherlands Univ Utrecht, Inst Biomembranes, Dept Mol Microbiol, NL-3584 CH Utrecht, Netherlands

Tommassen, Jan
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机构:
Univ Utrecht, Inst Biomembranes, Dept Mol Microbiol, NL-3584 CH Utrecht, Netherlands Univ Utrecht, Inst Biomembranes, Dept Mol Microbiol, NL-3584 CH Utrecht, Netherlands
机构:
[1] Univ Utrecht, Inst Biomembranes, Dept Mol Microbiol, NL-3584 CH Utrecht, Netherlands
来源:
关键词:
beta-barrel;
Omp85;
outer membrane;
POTRA domain;
D O I:
10.1038/sj.embor.7401092
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
beta-Barrel proteins are present in the outer membranes of Gram-negative bacteria, mitochondria and chloroplasts. The central component of their assembly machinery is called Omp85 in bacteria. Omp85 is predicted to consist of an integral membrane domain and an amino-terminal periplasmic extension containing five polypeptide-transport-associated (POTRA) domains. We have addressed the function of these domains by creating POTRA domain deletions in Omp85 of Neisseria meningitidis. Four POTRA domains could be deleted with only slight defects in Omp85 function. Only the most carboxy-terminal POTRA domain was essential, as was the membrane domain. Thus, similar to the mitochondrial Omp85 homologue, the functional core of bacterial Omp85 consists of its membrane domain and a single POTRA domain, that is, POTRA5.
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页码:1149 / 1154
页数:6
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