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Science. 2010 May 14;328(5980):890-2. doi: 10.1126/science.1188919. Epub 2010 Apr 8.

Reconstitution of outer membrane protein assembly from purified components.

Author information

1
Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.

Abstract

Beta-barrel membrane proteins in Gram-negative bacteria, mitochondria, and chloroplasts are assembled by highly conserved multi-protein complexes. The mechanism by which these molecular machines fold and insert their substrates is poorly understood. It has not been possible to dissect the folding and insertion pathway because the process has not been reproduced in a biochemical system. We purified the components that fold and insert Escherichia coli outer membrane proteins and reconstituted beta-barrel protein assembly in proteoliposomes using the enzymatic activity of a protein substrate to report on its folding state. The assembly of this protein occurred without an energy source but required a soluble chaperone in addition to the multi-protein assembly complex.

PMID:
20378773
PMCID:
PMC2873164
DOI:
10.1126/science.1188919
[Indexed for MEDLINE]
Free PMC Article

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