rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1992-2-14
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pubmed:abstractText |
The phosphoprotein (P) and the large protein (L) constitute the RNA-dependent RNA polymerase of vesicular stomatitis virus (VSV). We show that phosphate-free P protein expressed in bacteria is transcriptionally inactive when reconstituted with L protein and viral N-RNA template free of cellular protein kinase. Phosphorylation of P protein by a cellular kinase(s) was essential for transcription as well as for further phosphorylation by an L-associated kinase, the two kinases acting in a sequential (cascade) manner. Phosphate groups introduced by cell kinase were stable, whereas those due to L kinase underwent a turnover which was coupled to ongoing transcription. We present a model for the phosphorylation pathway of P protein and propose that continued phosphorylation and dephosphorylation of P protein may represent a transcriptional regulatory (on-off) switch of nonsegmented negative-strand RNA viruses.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-1650349,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-1651598,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-1655011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-167189,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-168405,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-1848304,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-2119171,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-2137373,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-214246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-2155516,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-2159527,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-2161940,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-2166816,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-227166,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-2302733,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-2441389,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-2525256,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-2549856,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-2827161,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-2845648,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-2847150,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-2985822,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-2987394,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1309893-6322412
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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 |
66
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1109-18
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:1309893-Animals,
pubmed-meshheading:1309893-Cell Line,
pubmed-meshheading:1309893-Cloning, Molecular,
pubmed-meshheading:1309893-Escherichia coli,
pubmed-meshheading:1309893-Kinetics,
pubmed-meshheading:1309893-Models, Biological,
pubmed-meshheading:1309893-Phosphoproteins,
pubmed-meshheading:1309893-Phosphorylation,
pubmed-meshheading:1309893-Protein Kinases,
pubmed-meshheading:1309893-RNA Replicase,
pubmed-meshheading:1309893-Recombinant Proteins,
pubmed-meshheading:1309893-Transcription, Genetic,
pubmed-meshheading:1309893-Transcriptional Activation,
pubmed-meshheading:1309893-Vesicular stomatitis Indiana virus
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pubmed:year |
1992
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pubmed:articleTitle |
Sequential phosphorylation of the phosphoprotein of vesicular stomatitis virus by cellular and viral protein kinases is essential for transcription activation.
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pubmed:affiliation |
Department of Molecular Biology, Research Institute, Cleveland Clinic Foundation, Ohio 44195.
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