期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 110, 期 29, 页码 11815-11820出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1303289110
关键词
SecA; SecB; secretion; export
资金
- Hugo Wurdack Trust at the University of Missouri
- National Institutes of Health [GM29798]
- National Science Foundation [1054832]
- Burroughs Wellcome Fund
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1054832] Funding Source: National Science Foundation
We have established a reconstitution system for the translocon SecYEG in proteoliposomes in which 55% of the accessible translocons are active. This level corresponds to the fraction of translocons that are active in vitro when assessed in their native environment of cytoplasmic membrane vesicles. Assays using these robust reconstituted proteoliposomes and cytoplasmic membrane vesicles have revealed that the number of SecYEG units involved in an active translocase depends on the precursor undergoing transfer. The active translocase for the precursor of periplasmic galactose-binding protein contains twice the number of heterotrimeric units of SecYEG as does that for the precursor of outer membrane protein A.
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