期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 109, 期 9, 页码 3487-3491出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1201362109
关键词
Omp85; membrane protein folding; conditional lethal; allele-specific
资金
- National Institute of General Medical Sciences [GM34821]
- National Institute of Allergy and Infectious Disease [AI081059]
- National Science Foundation
The outer membrane (OM) of Gram-negative bacteria such as Escherichia coli contains lipoproteins and integral beta-barrel proteins (outer-membrane proteins, OMPs) assembled into an asymmetrical lipid bilayer. Insertion of beta-barrel proteins into the OM is mediated by a protein complex that contains the OMP BamA and four associated lipoproteins (BamBCDE). The mechanism by which the Bam complex catalyzes the assembly of OMPs is not known. We report here the isolation and characterization of a temperature-sensitive lethal mutation, bamAE373K, which alters the fifth polypeptide transport-associated domain and disrupts the interaction between the BamAB and BamCDE subcomplexes. Suppressor mutations that map to codon 197 in bamD restore Bam complex function to wildtype levels. However, these suppressors do not restore the interaction between BamA and BamD; rather, they bypass the requirement for stable holocomplex formation by activating BamD. These results imply that BamA and BamD interact directly with OMP substrates.
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