ArticleProceedings of the National Academy of Sciences of the United States of America1994
Residues essential for the function of SecE, a membrane component of the Escherichia coli secretion apparatus, are located in a conserved cytoplasmic region.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 66 citations in OpenAlex.
- Pro-SMP finder-A systematic approach for discovering small membrane proteins in prokaryotes.PloS one · 2024Article
- Nuclear lamin functions and disease.Trends in genetics : TIG · 2012Review
- The bacterial Sec-translocase: structure and mechanism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Stability and function of the Sec61 translocation complex depends on the Sss1p tail-anchor sequence.The Biochemical journal · 2011Article
- SecA, a remarkable nanomachine.Cellular and molecular life sciences : CMLS · 2011Review
- Cryo-EM structure of the ribosome-SecYE complex in the membrane environment.Nature structural & molecular biology · 2011Article
- Regulation of the protein-conducting channel by a bound ribosome.Structure (London, England : 1993) · 2009Article
- Extreme secretion: protein translocation across the archael plasma membrane.Journal of bioenergetics and biomembranes · 2004Review
- Interfering mutations provide in vivo evidence that Escherichia coli SecE functions in multimeric states.Molecular genetics and genomics : MGG · 2003Article
- The secE gene of Helicobacter pylori.Journal of bacteriology · 2002Article
- Preprotein translocation by a hybrid translocase composed of Escherichia coli and Bacillus subtilis subunits.Journal of bacteriology · 1999Article
- Linkage map of Escherichia coli K-12, edition 10: the traditional map.Microbiology and molecular biology reviews : MMBR · 1998Review
- A novel sec-independent periplasmic protein translocation pathway in Escherichia coli.The EMBO journal · 1998Article
- Domain-swapping analysis of FtsI, FtsL, and FtsQ, bitopic membrane proteins essential for cell division in Escherichia coli.Journal of bacteriology · 1997Article
- In vivo membrane assembly of the E.coli polytopic protein, melibiose permease, occurs via a Sec-independent process which requires the protonmotive force.The EMBO journal · 1996Article
- A new genetic selection identifies essential residues in SecG, a component of the Escherichia coli protein export machinery.The EMBO journal · 1995Article
- Multicopy suppression of cold-sensitive sec mutations in Escherichia coli.Journal of bacteriology · 1995Article
- Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter.Journal of bacteriology · 1995Article
- The allele-specific synthetic lethality of prlA-prlG double mutants predicts interactive domains of SecY and SecE.The EMBO journal · 1995Article
- How proteins cross the bacterial cytoplasmic membrane.The Journal of membrane biology · 1994Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein export in Escherichia coli is absolutely dependent on two integral membrane proteins, SecY and SecE. Previous deletion mutagenesis of the secE gene showed that only the third of three membrane-spanning segments and a portion of the second cytoplasmic region are necessary for its function in protein export. Here we further define the residues important for SecE function. Alignment of the SecE homologues of various eubacteria reveals that they all contain one membrane-spanning segment, compared with three in E. coli SecE, and that the most conserved region among them lies in their putative cytoplasmic amino termini; little homology exists in their membrane-spanning segments. The SecE homologue of the extreme thermophilic bacterium Thermotoga maritima was cloned and found to complement a deletion of secE in E. coli. Deletion or replacement of the cytoplasmic region of E. coli SecE eliminated SecE function, indicating that this sequence is essential for a functional secretion machinery. Mutant analysis suggests that the most important function of the third membrane-spanning segment is to maintain the proper topological arrangement of the conserved cytoplasmic domain.
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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.