| A chemically cross-linked nonlinear proOmpA molecule can be translocated into everted membrane vesicles of Escherichia coli in the presence of the proton motive force. | |
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MedLine Citation:
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PMID: 1648509 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The chemical cross-linking between the two cysteine residues at positions + 290 and + 302 of proOmpA was performed with N,N'-bis(3-maleimidopropionyl)-2-hydroxy-1,3-propanediamine. In the absence of the proton motive force (delta muH+), the cross-linked proOmpA was only partially translocated into everted membrane vesicles, leading to accumulation of translocation intermediates. In the presence of delta mu H+, the cross-linked proOmpA was completely translocated. The translocated OmpA still possessed the cross-linked loop composed of 13 amino acid residues and the cross-linker. It is concluded that polypeptide chains need not be necessarily linear and fully expanded to be translocated. |
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Authors:
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K Tani; S Mizushima |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: FEBS letters Volume: 285 ISSN: 0014-5793 ISO Abbreviation: FEBS Lett. Publication Date: 1991 Jul |
Date Detail:
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Created Date: 1991-08-14 Completed Date: 1991-08-14 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0155157 Medline TA: FEBS Lett Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 127-31 Citation Subset: IM |
Affiliation:
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Institute of Applied Microbiology, University of Tokyo, Japan. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Bacterial Outer Membrane Proteins / metabolism* Biological Transport, Active Cell Membrane / metabolism Cell-Free System Cross-Linking Reagents Cysteine / metabolism Diamines Escherichia coli / metabolism* Exocytosis / physiology* Maleimides Molecular Sequence Data Protein Conformation Protons Serine Endopeptidases / metabolism |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Outer Membrane Proteins; 0/Cross-Linking Reagents; 0/Diamines; 0/Maleimides; 0/Protons; 115388-98-2/N,N'-bis(3-maleimidepropionyl)-2-hydroxy-1,3-propanediamine; 52-90-4/Cysteine; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.50/lysyl endopeptidase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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