Linked Life Data

2991232

Source:http://linkedlifedata.com/resource/pubmed/id/2991232

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1985-8-28
pubmed:abstractText
The NS protein of vesicular stomatitis virus is an auxiliary protein in the virus core (nucleocapsid) that plays a role in virus-specific RNA synthesis. NS exhibits a variety of phosphorylated forms, and the degree of phosphorylation correlates with the rate of RNA synthesis. However, chymotryptic peptide mapping has indicated that all forms of NS share a common cluster of phosphorylated residues. To locate these residues in the primary structure of the molecule, we performed a series of residue-specific chemical and enzymatic cleavages and separated radiophosphate-labeled peptides by gel electrophoresis. The data indicate that the constitutively phosphorylated sites in NS molecules reside in the amino-terminal region of the molecule, between residues 35 and 78. The previously reported resistance of the phosphoamino acids in this region to dephosphorylation by exogenous phosphatase suggests that this domain is embedded within the tertiary structure of the molecule or involved in quaternary interactions. In contrast, the amino acid residues that are phosphorylated secondarily, making NS more active in RNA synthesis, reside in more exposed regions of the molecule.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
260
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8990-5
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Constitutively phosphorylated residues in the NS protein of vesicular stomatitis virus.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't