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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
1996-1-11
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pubmed:abstractText |
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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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-1266045,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-1328674,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-1501278,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-1548757,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-1719233,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-1885768,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-2002551,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-2724407,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-2885424,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-3275434,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-3275869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-3354207,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-3657575,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-4107549,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-4311639,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-4349495,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-4672416,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-4673489,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-4833545,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-5012651,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-5064083,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-5167655,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-5463865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-6183822,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-664215,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-6740943,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-7086953,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-716218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-716219,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-7175500,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-7175501,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-7527088,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-8350400,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7494347-8394844
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0022-538X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
69
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8180-4
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7494347-Animals,
pubmed-meshheading:7494347-Capsid,
pubmed-meshheading:7494347-Capsid Proteins,
pubmed-meshheading:7494347-Endopeptidase K,
pubmed-meshheading:7494347-Kinetics,
pubmed-meshheading:7494347-Peptide Fragments,
pubmed-meshheading:7494347-Protein Binding,
pubmed-meshheading:7494347-Protein Biosynthesis,
pubmed-meshheading:7494347-Protein Conformation,
pubmed-meshheading:7494347-Protein Folding,
pubmed-meshheading:7494347-RNA-Binding Proteins,
pubmed-meshheading:7494347-Rabbits,
pubmed-meshheading:7494347-Reoviridae,
pubmed-meshheading:7494347-Reticulocytes,
pubmed-meshheading:7494347-Serine Endopeptidases,
pubmed-meshheading:7494347-Transcription, Genetic,
pubmed-meshheading:7494347-Viral Proteins,
pubmed-meshheading:7494347-Virion
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pubmed:year |
1995
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pubmed:articleTitle |
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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pubmed:affiliation |
Department of Microbiology, University of Minnesota, Minneapolis 55455, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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