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Functioning of outer membrane protein assembly factor Omp85 requires a single POTRA domain
Author(s) -
Bos Martine P,
Robert Viviane,
Tommassen Jan
Publication year - 2007
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7401092
Subject(s) - bacterial outer membrane , periplasmic space , biology , domain (mathematical analysis) , membrane , outer membrane efflux proteins , microbiology and biotechnology , biophysics , biochemistry , escherichia coli , mathematical analysis , mathematics , gene
β‐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.