Specificity of SecYEG for PhoA precursors and SecA homologs on SecA protein-conducting channels.

Biochem Biophys Res Commun

Department of Biology and Center of Biotechnology and Drug Design, Georgia State University, Atlanta, GA 30303.

Published: July 2013

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Article Abstract

Previous studies showed that Escherichia coli membranes depleted of SecYEG are capable of translocating certain precursor proteins, but not other precursors such as pPhoA, indicating a differential requirement for SecYEG. In this study, we examined the role of SecYEG in pPhoA translocation using a purified reconstituted SecA-liposomes system. We found that translocation of pPhoA, in contrast to that of pOmpA, requires the presence of purified SecYEG. A differential specificity of the SecYEG was also revealed in its interaction with SecA: EcSecYEG did not enhance SecA-mediated pOmpA translocation by purified SecA either from Pseudomonas aeruginosa or Bacillus subtilis. Neither was SecYEG required for eliciting ion channel activity, which could be opened by unfolded pPhoA or unfolded PhoA. Addition of the SecYEG complex did restore the specificity of signal peptide recognition in the ion-channel activity. We concluded that SecYEG confers specificity in interacting with protein precursors and SecAs.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3740335PMC
http://dx.doi.org/10.1016/j.bbrc.2013.06.039DOI Listing

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