ArticleProceedings of the National Academy of Sciences of the United States of America1998
Roles of SecG in ATP- and SecA-dependent protein translocation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 39 citations in OpenAlex.
- The SecA protein deeply penetrates into the SecYEG channel during insertion, contacting most channel transmembrane helices and periplasmic regions.The Journal of biological chemistry · 2017Article
- YidC and SecYEG form a heterotetrameric protein translocation channel.Scientific reports · 2017Article
- Silver enhances antibiotic activity against gram-negative bacteria.Science translational medicine · 2013Article
- The bacterial Sec-translocase: structure and mechanism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Mapping of the SecA·SecY and SecA·SecG interfaces by site-directed in vivo photocross-linking.The Journal of biological chemistry · 2011Article
- Article
- Inter-species complementation of the translocon beta subunit requires only its transmembrane domain.PloS one · 2008Article
- Different modes of SecY-SecA interactions revealed by site-directed in vivo photo-cross-linking.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Topologically fixed SecG is fully functional.Journal of bacteriology · 2006Article
- Peculiar properties of DsbA in its export across the Escherichia coli cytoplasmic membrane.Journal of bacteriology · 2005Article
- Mutational analysis of transmembrane regions 3 and 4 of SecY, a central component of protein translocase.Journal of bacteriology · 2004Article
- Interfering mutations provide in vivo evidence that Escherichia coli SecE functions in multimeric states.Molecular genetics and genomics : MGG · 2003Article
- Critical regions of secM that control its translation and secretion and promote secretion-specific secA regulation.Journal of bacteriology · 2002Article
- Roles of the C-terminal end of SecY in protein translocation and viability of Escherichia coli.Journal of bacteriology · 2002Article
- Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome.Microbiology and molecular biology reviews : MMBR · 2000Review
- A mutation in secY that causes enhanced SecA insertion and impaired late functions in protein translocation.Journal of bacteriology · 2000Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SecA, the translocation ATPase in Escherichia coli, undergoes cycles of conformational changes (insertion/deinsertion) in response to ATP and a preprotein. The membrane-embedded portion of protein translocase, SecYEG, has crucial roles in the SecA-driven preprotein translocation reaction. We previously identified a secY mutation (secY205) that did not allow an ATP- and preprotein-dependent (productive) insertion of SecA as well as secA mutations that suppressed the secY205 translocation defect. One of the suppressor mutations, secA36, also suppressed the cold-sensitive phenotype of the secG deletion mutant. In vitro experiments at 20 degreesC showed that inverted membrane vesicles lacking SecG were almost inactive in combination with the wild-type SecA protein in translocation of proOmpA as well as in the accompanying ATP hydrolysis. In contrast, the SecA36 mutant protein was found to be able to execute the translocation activity fully at this temperature, even in the absence of SecG. A SecG requirement and its alleviation by the SecA36 alteration also were shown for the SecA insertion reaction. The finding that the SecA36 protein no longer requires assistance from SecG in its insertion and in its catalysis of protein translocation agrees with the idea that SecG normally assists in the functioning of SecA. In agreement with this notion, when the intrinsic SecA function was compromised by a lowered ATP concentration, SecG became essential even at 37 degreesC and even for the SecA36 protein. We propose that in the normal translocase, SecG cooperates with SecA to facilitate efficient movement of preprotein in each catalytic cycle of SecA.
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