ArticleThe EMBO journal1999
Membrane deinsertion of SecA underlying proton motive force-dependent stimulation of protein translocation.
Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed.
- SecA-Mediated Protein Translocation through the SecYEG Channel.Microbiology spectrum · 2019Review
- The Sec System: Protein Export inEcoSal Plus · 2017Review
- SecA: a potential antimicrobial target.Future medicinal chemistry · 2015Review
- Position-dependent effects of polylysine on Sec protein transport.The Journal of biological chemistry · 2012Article
- Multiple SecA molecules drive protein translocation across a single translocon with SecG inversion.The Journal of biological chemistry · 2012Article
- An energy transduction mechanism used in bacterial flagellar type III protein export.Nature communications · 2011Article
- SecA, a remarkable nanomachine.Cellular and molecular life sciences : CMLS · 2011Review
- Bacterial Sec protein transport is rate-limited by precursor length: a single turnover study.Molecular biology of the cell · 2009Article
- Interactions that drive Sec-dependent bacterial protein transport.Biochemistry · 2007Review
- Molecular determinants for PspA-mediated repression of the AAA transcriptional activator PspF.Journal of bacteriology · 2005Article
- The archaeal Sec-dependent protein translocation pathway.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004Review
- Ring-like pore structures of SecA: implication for bacterial protein-conducting channels.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Biochemical characterization of a mutationally altered protein translocase: proton motive force stimulation of the initiation phase of translocation.Journal of bacteriology · 2003Article
- A novel class of secA alleles that exert a signal-sequence-dependent effect on protein export in Escherichia coli.Genetics · 2002Article
- Overexpression of yccL (gnsA) and ydfY (gnsB) increases levels of unsaturated fatty acids and suppresses both the temperature-sensitive fabA6 mutation and cold-sensitive secG null mutation of Escherichia coli.Journal of bacteriology · 2001Article
- Sec-dependent membrane protein insertion: sequential interaction of nascent FtsQ with SecY and YidC.EMBO reports · 2001Article
- A mutation in secY that causes enhanced SecA insertion and impaired late functions in protein translocation.Journal of bacteriology · 2000Article
- Role of lipids in the translocation of proteins across membranes.The Biochemical journal · 2000Review
- SecYEG assembles into a tetramer to form the active protein translocation channel.The EMBO journal · 2000Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The proton motive force (PMF) renders protein translocation across the Escherichia coli membrane highly efficient, although the underlying mechanism has not been clarified. The membrane insertion and deinsertion of SecA coupled to ATP binding and hydrolysis, respectively, are thought to drive the translocation. We report here that PMF significantly decreases the level of membrane-inserted SecA. The prlA4 mutation of SecY, which causes efficient protein translocation in the absence of PMF, was found to reduce the membrane-inserted SecA irrespective of the presence or absence of PMF. The PMF-dependent decrease in the membrane-inserted SecA caused an increase in the amount of SecA released into the extra-membrane milieu, indicating that PMF deinserts SecA from the membrane. The PMF-dependent deinsertion reduced the amount of SecA required for maximal translocation activity. Neither ATP hydrolysis nor exchange with external SecA was required for the PMF-dependent deinsertion of SecA. These results indicate that the SecA deinsertion is a limiting step of protein translocation and is accelerated by PMF, efficient protein translocation thereby being caused in the presence of PMF.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.