Preprotein transfer to the Escherichia coli translocase requires the co‐operative binding of SecB and the signal sequence to SecA
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In Escherichia coli, precursor proteins are targeted to the membrane‐bound translocase by the cytosolic chaperone SecB. SecB binds to the extreme carboxy‐terminus of the SecA ATPase translocase subunit, and this interaction is promoted by preproteins. The mutant SecB proteins, L75Q and E77K, which interfere with preprotein translocation in vivo, are unable to stimulate in vitro translocation. Both mutants bind proOmpA but fail to support the SecA‐dependent membrane binding of proOmpA because of a marked reduction in their binding affinities for SecA. The stimulatory effect of preproteins on the interaction between SecB and SecA exclusively involves the signal sequence domain of the preprotein, as it can be mimicked by a synthetic signal peptide and is not observed with a mutant preprotein (Δ8proOmpA) bearing a non‐functional signal sequence. Δ8proOmpA is not translocated across wild‐type membranes, but the translocation defect is suppressed in inner membrane vesicles derived from a prlA4 strain. SecB reduces the translocation of Δ8proOmpA into these vesicles and almost completely prevents translocation when, in addition, the SecB binding site on SecA is removed. These data demonstrate that efficient targeting of preproteins by SecB requires both a functional signal sequence and a SecB binding domain on SecA. It is concluded that the SecB–SecA interaction is needed to dissociate the mature preprotein domain from SecB and that binding of the signal sequence domain to SecA is required to ensure efficient transfer of the preprotein to the translocase.
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SecYEG-bound SecA primarily recognizes its substrates after they have been released from the ribosome.
“SecYEG-bound SecA primarily recognizes its substrates after they have been released from the ribosome”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Fekkes et al., 1998
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- Authors
- Fekkes, P., De Wit, J. G., Van Der Wolk, J. P. W., Kimsey, H. H., Kumamoto, C. A., & Driessen, A. J. M.
- Affiliations
- University of Groningen (NL)
- Tufts University (US)
- Corresponding author
- Driessen, Arnold J. M.
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 1998-09
- Volume
- 29
- Issue
- 5
- Pages
- 1179-1190
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W2133779882
- Cited by
- 111
- References
- 57
- Citations by year
- 2024: 2 · 2023: 1 · 2022: 2 · 2021: 3 · 2020: 4 · 2019: 3 · 2018: 1 · 2017: 4 · 2016: 2 · 2015: 1 · 2014: 4 · 2013: 3 · 2012: 5
- FWCI
- 4.19
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Microbiology (publishedVersion)
- PubMed (publishedVersion)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (publishedVersion, other-oa)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (submittedVersion, other-oa)
- Funders
- National Institutes of Health (5r01gm036415-12)
- National Institute of General Medical Sciences (GM 36415)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- SecB, SecA, preprotein translocation, signal peptide, OmpA, molecular chaperones, Escherichia coli
- MeSH terms
- SEC Translocation Channels, SecA Proteins, Adenosine Triphosphatases, Bacterial Outer Membrane Proteins, Bacterial Proteins, Binding Sites, Biological Transport, Cell Membrane, Escherichia coli, Mutation, Phenotype, Protein Binding, Protein Precursors, Recombinant Fusion Proteins, Protein Sorting Signals, Membrane Transport Proteins, Escherichia coli Proteins
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