ArticleMolecular genetics and genomics : MGG2003
Interfering mutations provide in vivo evidence that Escherichia coli SecE functions in multimeric states.
Article in Molecular genetics and genomics : MGG, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
3 citing papers in PubMed, 8 citations in OpenAlex.
- Two copies of the SecY channel and acidic lipids are necessary to activate the SecA translocation ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Regulation of the protein-conducting channel by a bound ribosome.Structure (London, England : 1993) · 2009Article
- Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase.The EMBO journal · 2003Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SecY, SecE and SecG form a heterotrimer, which functions as a protein translocation channel in Escherichia coli. The cytosolic loop of SecE contains a segment that is conserved among different organisms. Here we show that mutational alterations in this segment not only inactivate the SecE function but confer dominant interfering properties on the altered SecE molecule. Such effects were especially evident in mutant cells in which the requirement for SecE function was increased. Overproduction of SecE, but not of SecY, alleviated the dominant negative effects. These results suggest that the inactive SecE molecule sequesters wild-type SecE. It was also found that an amino acid substitution, D112P, in the C-terminal periplasmic region intragenically suppressed the dominant interference. These results are consistent with a notion that there is significant SecE-SecE interaction in vivo, in which the C-terminal region has an important role. The data hence suggest that dimeric SecE participates in the formation of the functional translocation channel.
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Registered trials
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.