A Single Amino Acid Substitution in SecY Stabilizes the Interaction with SecA *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 274, Issue: 34, Page: 23868-23874
1999
- 18Citations
- 11Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations18
- Citation Indexes18
- 18
- CrossRef17
- Captures11
- Readers11
- 11
Article Description
The SecYEG complex constitutes a protein conducting channel across the bacterial cytoplasmic membrane. It binds the peripheral ATPase SecA to form the translocase. When isoleucine 278 in transmembrane segment 7 of the SecY subunit was replaced by a unique cysteine, SecYEG supported an increased preprotein translocation and SecA translocation ATPase activity, and allowed translocation of a preprotein with a defective signal sequence. SecY(I278C)EG binds SecA with a higher affinity than normal SecYEG, in particular in the presence of ATP. The increased translocation activity of SecY(I278C)EG was confirmed in a purified system consisting of SecYEG proteoliposomes, while immunoprecipitation in detergent solution reveal that translocase-preprotein complexes are more stable with SecY(I278C) than with normal SecY. These data imply an important role for SecY transmembrane segment 7 in SecA binding. As improved SecA binding to SecY was also observed with the prlA4 suppressor mutation, it may be a general mechanism underlying signal sequence suppression.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925819555041; http://dx.doi.org/10.1074/jbc.274.34.23868; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0033588165&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/10446151; https://linkinghub.elsevier.com/retrieve/pii/S0021925819555041; https://dx.doi.org/10.1074/jbc.274.34.23868
Elsevier BV
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