ArticleThe EMBO journal2000
Evaluating the oligomeric state of SecYEG in preprotein translocase.
Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Glycolipozyme MPIase is essential for topology inversion of SecG during preprotein translocation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- A single copy of SecYEG is sufficient for preprotein translocation.The EMBO journal · 2011Article
- Biogenesis of bacterial inner-membrane proteins.Cellular and molecular life sciences : CMLS · 2010Review
- Structure of monomeric yeast and mammalian Sec61 complexes interacting with the translating ribosome.Science (New York, N.Y.) · 2009Article
- Visualization of distinct entities of the SecYEG translocon during translocation and integration of bacterial proteins.Molecular biology of the cell · 2009Article
- Assembly of the translocase motor onto the preprotein-conducting channel.Molecular microbiology · 2008Article
- Oligomeric states of the SecA and SecYEG core components of the bacterial Sec translocon.Biochimica et biophysica acta · 2007Review
- Molecular dynamics studies of the archaeal translocon.Biophysical journal · 2006Article
- Investigating the SecY plug movement at the SecYEG translocation channel.The EMBO journal · 2005Article
- Dimeric SecA is essential for protein translocation.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Article
- The ribosome and YidC. New insights into the biogenesis of Escherichia coli inner membrane proteins.EMBO reports · 2003Review
- Nucleotide binding induces changes in the oligomeric state and conformation of Sec A in a lipid environment: a small-angle neutron-scattering study.Journal of molecular biology · 2003Article
- Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase.The EMBO journal · 2003Article
- 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
- Interfering mutations provide in vivo evidence that Escherichia coli SecE functions in multimeric states.Molecular genetics and genomics : MGG · 2003Article
- The thylakoid membrane protein ALB3 associates with the cpSecY-translocase in Arabidopsis thaliana.The Biochemical journal · 2002Article
- A novel class of secA alleles that exert a signal-sequence-dependent effect on protein export in Escherichia coli.Genetics · 2002Article
- The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure.The EMBO journal · 2002Article
- Projection structure and oligomeric properties of a bacterial core protein translocase.The EMBO journal · 2001Article
Corrections and comments
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2 authors.
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Abstract
SecA insertion and deinsertion through SecYEG drive preprotein translocation at the Escherichia coli inner membrane. We present three assessments of the theory that oligomers of SecYEG might form functional translocation sites. (i) Formaldehyde cross- linking of translocase reveals cross-links between SecY, SecE and SecG, but not higher order oligomers. (ii) Cross-linking of membranes containing unmodified SecE and hemagglutinin-tagged SecE (SecE(HA)) reveals cross-links between SecY and SecE and between SecY and SecE(HA). However, anti-HA immunoprecipitates contain neither untagged SecE nor SecY cross-linked to SecE. (iii) Membranes containing similar amounts of SecE and SecE(HA) were saturated with translocation intermediate (I(29)) and detergent solubilized. Anti-HA immunoprecipitation of I(29) required SecYE(HA)G and SecA, yet untagged SecE was not present in this translocation complex. Likewise, anti-HA immunoprecipitates of membranes containing equal amounts of SecY and SecY(HA) were found to contain SecY(HA) but not SecY. Both immunoprecipitates contain more moles of I(29) than of the untagged subunit, again suggesting that translocation intermediates are not engaged with multiple copies of SecYEG. These studies suggest that the active form of preprotein translocase is monomeric SecYEG.
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