v-Src enhances phosphorylation at Ser-282 of the rous sarcoma virus integrase

S. R. Mumm, R. Horton, D. P. Grandgenett

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5 Scopus citations

Abstract

The Rous sarcoma virus (RSV) integrase (IN) and the β polypeptide (β) of the reverse transcriptase are posttranslationally modified by phosphorylation on Ser at amino acid position 282 of IN. When IN was immunoprecipitated from RSV (Prague A strain) virions, approximately 30 to 40% of the IN molecules were phosphorylated. When IN was immunoprecipitated from a v-src deletion mutant (ΔMst-A) of RSV or from avian myeloblastosis virus (AMV), the percentage of IN molecules that were phosphorylated was significantly reduced. This reduction in phosphorylation of IN between virions was verified by [35S]Met-[35S]Cys or 32P labeling of IN, followed by immunoprecipitation analysis using antisera directed to the amino or carboxyl terminus of IN. In ΔMst-A or AMV, a nonphosphorylated, slightly truncated (at the carboxyl terminus) polypeptide was the major species of IN. The enhanced phosphorylation of IN does not appear to be a general function of transformed cells, since enhanced phosphorylation was not detected in AMV derived from viremic chickens or from a v-src deletion mutant of RSV propagated in a chemically transformed quail cell line, QT6. From these data, we conclude that v-Src is necessary for efficient phosphorylation of IN and β.

Original languageEnglish
Pages (from-to)1995-1999
Number of pages5
JournalJournal of virology
Volume66
Issue number4
DOIs
StatePublished - 1992

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