The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
Protein Translocation Across the Bacterial Cytoplasmic Membrane
Abstract
About 25% to 30% of the bacterial proteins function in the cell envelope or outside of the cell. These proteins are synthesized in the cytosol, and the vast majority is recognized as a ribosome-bound nascent chain by the signal recognition particle (SRP) or by the secretion-dedicated chaperone SecB. Subsequently, they are targeted to the Sec translocase in the cytoplasmic membrane, a multimeric membrane protein complex composed of a highly conserved protein-conducting channel, SecYEG, and a peripherally bound ribosome or ATP-dependent motor protein SecA. The Sec translocase mediates the translocation of proteins across the membrane and the insertion of membrane proteins into the cytoplasmic membrane. Translocation requires the energy sources of ATP and the proton motive force (PMF) while the membrane protein insertion is coupled to polypeptide chain elongation at the ribosome. This review summarizes the present knowledge of the mechanism and structure of the Sec translocase, with a special emphasis on unresolved questions and topics of current research.
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Escherichia coli YidC is a membrane insertase for Sec-independent proteins.
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Nanopore-based technologies beyond DNA sequencing
Ying, Y.-L., Hu, Z.-L., Zhang, S., Qing, Y., Fragasso, A., Maglia, G., Meller, A., Bayley, H., Dekker, C., & Long, Y.-T. (2022) · Nature Nanotechnology · doi:10.1038/s41565-022-01193-2 · Cited by 538
Superresolution imaging of ribosomes and RNA polymerase in live Escherichia coli cells
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Membrane Protein Structure, Function, and Dynamics: a Perspective from Experiments and Theory
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Metadata
- Authors
- Driessen, A. J. M., & Nouwen, N.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2008-06-01
- Volume
- 77
- Issue
- 1
- Pages
- 643-667
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2103188931
- Cited by
- 614
- References
- 16
- FWCI
- 3.69
- Type
- journal article
- Language
- en
- Open access
- closed
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