Specificity of SecYEG for PhoA precursors and SecA homologs on SecA protein-conducting channels
| Autor: | Phang C. Tai, Hao Zhang, Sen-Fang Sui, Li-Yan Yu, Chun Jiang, Hsiuchin Yang, Bor-ruei Lin, Ying-Hsin Hsieh |
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| Rok vydání: | 2013 |
| Předmět: |
Signal peptide
Escherichia coli Proteins Xenopus Biophysics Chromosomal translocation Cell Biology Bacillus subtilis Biology medicine.disease_cause biology.organism_classification Biochemistry environment and public health Article Protein Transport Membrane Ion channel activity medicine Homologous chromosome Escherichia coli bacteria Animals Molecular Biology SEC Translocation Channels |
| Zdroj: | Biochemical and biophysical research communications. 437(2) |
| ISSN: | 1090-2104 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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