Snyder-Theilen feline sarcoma virus P85 contains a single phosphotyrosine acceptor site recognized by its associated protein kinase.

Abstract:

:Cells nonproductively transformed by a variant of the Snyder-Theilen strain of feline sarcoma virus (FeSV) expressed an 85,000-dalton polyprotein (P85) with associated tyrosine-specific protein kinase activity. We identified within this polyprotein a single tyrosine acceptor site for its enzyme activity. This acceptor site, as well as two serine phosphorylation sites localized with the p12 structural component of Snyder-Theilen FeSv P85, was phosphorylated in cells nonproductively transformed by Snyder-Theilen FeSv. In contrast, infection by Snyder-Theilen FeSV transformation-defective mutants resulted in phosphorylation only of the two serine acceptor sites, indicating phosphorylation of the tyrosine acceptor site to be transformation specific. In addition, we describe in vitro labeling conditions, using unfractionated cell extracts, which resulted in preferential phosphorylation of the single Snyder-Theilen FeSV tyrosine-specific acceptor site.

journal_name

J Virol

journal_title

Journal of virology

authors

Blomberg J,Van de Ven WJ,Reynolds FH Jr,Nalewaik RP,Stephenson JR

doi

10.1128/JVI.38.3.886-894.1981

subject

Has Abstract

pub_date

1981-06-01 00:00:00

pages

886-94

issue

3

eissn

0022-538X

issn

1098-5514

journal_volume

38

pub_type

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