Linked Life Data

2987524

Source:http://linkedlifedata.com/resource/pubmed/id/2987524

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1985-7-2
pubmed:abstractText
The phosphoprotein NS of vesicular stomatitis virus which accumulates within the infected cell cytoplasm is phosphorylated at multiple serine and threonine residues (G. M. Clinton and A. S. Huang, Virology 108:510-514, 1981; Hsu et al., J. Virol. 43:104-112, 1982). Using incomplete chemical cleavage at tryptophan residues, we mapped the major phosphorylation sites to the amino-terminal half of the protein. Analysis of phosphate-labeled tryptic peptides suggests that essentially all of the label is within the large trypsin-resistant fragment predicted from the sequence of Gallione et al. (J. Virol. 39:52-529, 1981). A similar result has been obtained for NS protein isolated from the virus particle by C.-H. Hsu and D. W. Kingsbury (J. Biol. Chem., in press). Analysis of phosphodipeptides utilizing the procedures of C. E. Jones and M. O. J. Olson (Int. J. Pept. Protein Res. 16:135-142, 1980) enabled us to detect as many as six distinct phosphate-containing dipeptides. From these studies, together with the known sequence data, we conclude that the major phosphate residues on cytoplasmic NS protein are located in the amino third of the NS molecule and most probably between residues 35 and 106, inclusive. The studies also provide formal chemical proof that NS protein has a structure consistent with a monomer of the sequence of Gallione et al. as modified by J. K. Rose (personal communication). The low electrophoretic mobility of this protein on sodium dodecyl sulfate-polyacrylamide gel electrophoresis is not therefore due to dimerization.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/2987524-204929, http://linkedlifedata.com/resource/pubmed/commentcorrection/2987524-210582, http://linkedlifedata.com/resource/pubmed/commentcorrection/2987524-232181, http://linkedlifedata.com/resource/pubmed/commentcorrection/2987524-29135, http://linkedlifedata.com/resource/pubmed/commentcorrection/2987524-442541, http://linkedlifedata.com/resource/pubmed/commentcorrection/2987524-465478, http://linkedlifedata.com/resource/pubmed/commentcorrection/2987524-6059350, http://linkedlifedata.com/resource/pubmed/commentcorrection/2987524-6162272, http://linkedlifedata.com/resource/pubmed/commentcorrection/2987524-6245261, http://linkedlifedata.com/resource/pubmed/commentcorrection/2987524-6268841, http://linkedlifedata.com/resource/pubmed/commentcorrection/2987524-6283149, http://linkedlifedata.com/resource/pubmed/commentcorrection/2987524-6286990, http://linkedlifedata.com/resource/pubmed/commentcorrection/2987524-6322412, http://linkedlifedata.com/resource/pubmed/commentcorrection/2987524-7461896, http://linkedlifedata.com/resource/pubmed/commentcorrection/2987524-990266
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0022-538X
pubmed:author
pubmed:issnType
Print
pubmed:volume
54
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
697-702
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Phosphorylation sites on phosphoprotein NS of vesicular stomatitis virus.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't