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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1990-2-14
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pubmed:abstractText |
The peripheral membrane M protein of vesicular stomatitis virus purified by detergent extraction of virions and ion-exchange chromatography was determined to be a monomer in the absence of detergent at high salt concentrations. Reduction of the ionic strength below 0.2 M resulted in a rapid aggregation of M protein. This self-association was reversible by the detergent Triton X-100 even in low salt. However, aggregation was not reversible by high salt concentration alone. M protein is initially synthesized as a soluble protein in the cytosol of infected cells, thus raising the question of how the solubility of M protein is maintained at physiological ionic strength. Addition of radiolabeled M protein purified from virions to unlabeled cytosol from either infected or uninfected cells inhibited the self-association reaction. Cytosolic fractions from infected or uninfected cells were equally effective at preventing the self-association of M protein. Self-association could also be prevented by an irrelevant protein such as bovine serum albumin. Sedimentation velocity analysis indicated that most of the newly synthesized M protein is monomeric, suggesting that the solubility of M protein in the cytosol is maintained by either low-affinity interaction with macromolecules in the cytosol or interaction of a small population of M-protein molecules with cytosolic components.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-1175627,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-169263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-178880,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-189082,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-191640,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-194063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-19431482,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-200480,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-219213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-229234,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-230485,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-2419040,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-2422402,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-2829424,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-2845149,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-29135,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-3005636,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-3016338,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-3033263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-3282178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-3282179,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-3413981,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-3527055,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-4352411,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-5329026,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-6255216,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-6261791,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-6268151,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-6268840,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-6274380,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-6284961,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153251-6296818
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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 |
Feb
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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 |
64
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
902-6
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pubmed:dateRevised |
2010-9-9
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pubmed:meshHeading |
pubmed-meshheading:2153251-Animals,
pubmed-meshheading:2153251-Cell Line,
pubmed-meshheading:2153251-Cell Transformation, Viral,
pubmed-meshheading:2153251-Chromatography, Gel,
pubmed-meshheading:2153251-Chromatography, Ion Exchange,
pubmed-meshheading:2153251-Cytosol,
pubmed-meshheading:2153251-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2153251-Macromolecular Substances,
pubmed-meshheading:2153251-Molecular Weight,
pubmed-meshheading:2153251-Solubility,
pubmed-meshheading:2153251-Vesicular stomatitis Indiana virus,
pubmed-meshheading:2153251-Viral Matrix Proteins,
pubmed-meshheading:2153251-Virion
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pubmed:year |
1990
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pubmed:articleTitle |
Solubility of vesicular stomatitis virus M protein in the cytosol of infected cells or isolated from virions.
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pubmed:affiliation |
Department of Microbiology and Immunology, Bowman Gray School of Medicine of Wake Forest University, Winston-Salem, North Carolina 27103.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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