Linked Life Data

3020780

Source:http://linkedlifedata.com/resource/pubmed/id/3020780

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1986-10-31
pubmed:abstractText
The phosphorylation and transcriptional competence of the free cytoplasmic form and the virion form of NS protein of vesicular stomatitis virus (VSV-Indiana/Mudd-Summers) were compared. NS protein is known to exist in two distinct phosphorylated states, NS1 and NS2, that are resolvable by gel electrophoresis. In vitro phosphorylation of virion NS protein by the viral L protein-associated protein kinase resulted in the phosphorylation of both NS1 and NS2. However, in the presence of the N-RNA complex, the NS2 form was preferentially phosphorylated. A cellular protein kinase activity, found in cytoplasmic extracts from VSV-infected or uninfected cells, preferentially phosphorylated NS1, which did not undergo dephosphorylation by cellular phosphatase and also did not convert to NS2. In contrast, the virion or cellular NS2 which had been phosphorylated in vivo or in vitro could be rapidly dephosphorylated by a cellular phosphatase. Cytoplasmic NS protein was found to be fully capable of binding to the virion N-RNA template, and in conjunction with L protein, it participated in synthesis of the leader RNA and five mRNA species of VSV. Moreover, under these conditions, neither cellular phosphatase nor cellular ribonuclease was able to bind to reconstituted nucleocapsids. Binding of cytoplasmic NS to the virion N-RNA template in the presence of L protein resulted in a large and preferential enhancement of NS2 phosphorylation. A protein kinase activity, which phosphorylated NS protein in vitro, was found to be associated with the N-RNA template. This activity appeared to be very tightly bound to N-RNA and exhibited absolute specificity for NS protein of the homologous serotype.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
154
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
259-70
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Phosphoprotein NS of vesicular stomatitis virus: phosphorylated states and transcriptional activities of intracellular and virion forms.
pubmed:publicationType
Journal Article