Stoichiometry of SecYEG in the active translocase of Escherichia coli varies with precursor species

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. A...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2013-07, Vol.110 (29), p.11815-11820
Main Authors: Mao, Chunfeng, Cheadle, Carl E., Hardy, Simon J. S., Lilly, Angela A., Suo, Yuying, Gari, Raghavendar Reddy Sanganna, King, Gavin M., Randall, Linda L.
Format: Article
Language:English
Subjects:
Adenosine triphosphatases
Binding sites
Biological Sciences
Calcium-Binding Proteins - metabolism
Carbon Radioisotopes - metabolism
Cell membranes
Cytoplasm
E coli
Escherichia coli
Escherichia coli - enzymology
Escherichia coli Proteins - genetics
Escherichia coli Proteins - metabolism
Hydrolysis
Lipids
Liposomes
Membrane Proteins - genetics
Membrane Proteins - metabolism
Membranes
Microscopy, Atomic Force
Monosaccharide Transport Proteins - metabolism
Periplasmic Binding Proteins - metabolism
Protein precursors
Protein subunits
Protein transport
Proteins
Proteolipids - metabolism
SEC Translocation Channels
Sulfur Radioisotopes - metabolism
Transport Vesicles - metabolism
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1303289110