| Association of reovirus outer capsid proteins sigma 3 and mu 1 causes a conformational change that renders sigma 3 protease sensitive. | |
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MedLine Citation:
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PMID: 7494347 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Association of the reovirus proteins sigma 3 and mu 1 influences viral entry, initiation of outer capsid assembly, and modulation of the effect of sigma 3 on cellular translation. In this study, we have addressed whether structural changes occur in sigma 3 as a result of its interaction with mu 1. Using differences in protease sensitivity to detect conformationally distinct forms of sigma 3, we showed that association of sigma 3 with mu 1 caused a conformational change in sigma 3 that converted it from a protease-resistant to a protease-sensitive structure and occurred posttranslationally. The effect of mu 1 on the structure of sigma 3 was stoichiometric. Our results are consistent with a model in which sigma 3's association with mu 1 shifts its function from translational control to assembly of an outer capsid in which sigma 3 is folded into the protease-sensitive conformation that is required for its cleavage during the next round of infection. |
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Authors:
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D A Shepard; J G Ehnstrom; L A Schiff |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Journal of virology Volume: 69 ISSN: 0022-538X ISO Abbreviation: J. Virol. Publication Date: 1995 Dec |
Date Detail:
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Created Date: 1996-01-11 Completed Date: 1996-01-11 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 0113724 Medline TA: J Virol Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 8180-4 Citation Subset: IM |
Affiliation:
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Department of Microbiology, University of Minnesota, Minneapolis 55455, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Capsid / biosynthesis, chemistry, metabolism* Capsid Proteins* Endopeptidase K Kinetics Peptide Fragments / chemistry, isolation & purification Protein Binding Protein Biosynthesis Protein Conformation* Protein Folding RNA-Binding Proteins* Rabbits Reoviridae / metabolism* Reticulocytes / metabolism Serine Endopeptidases / metabolism* Transcription, Genetic Viral Proteins / biosynthesis, chemistry*, metabolism* Virion / metabolism |
| Grant Support | |
ID/Acronym/Agency:
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1F32AI0902001A1/AI/NIAID NIH HHS; 5T32CA09138/CA/NCI NIH HHS; R29 AI32139/AI/NIAID NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Capsid Proteins; 0/Peptide Fragments; 0/RNA-Binding Proteins; 0/Viral Proteins; 0/mu1 protein, Reovirus; 0/sigma protein 3, Reovirus; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.64/Endopeptidase K |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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