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PMID: 6092915 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Functional domains of the pp60v-src protein as revealed by analysis of temperature-sensitive Rous sarcoma virus mutants.

Molecular and cellular biology ·Vol. 4 ·No. 8 ·1984-08-00 ·Pages 1508-14

Stoker AW, Enrietto PJ, Wyke JA

Abstract

Four temperature-sensitive (ts) Rous sarcoma virus src gene mutants with lesions in different parts of the gene represent three classes of alteration in pp60src. These classes are composed of mutants with (i) heat-labile protein kinase activities both in vitro and in vivo (tsLA27 and tsLA29), (ii) heat-labile kinases in vivo but not in vitro (tsLA33), and (iii) neither in vivo nor in vitro heat-labile kinases (tsLA32). The latter class indicates the existence of structural or functional pp60src domains that are required for transformation but do not grossly affect tyrosine kinase activity.

MeSH Terms
Amino Acids/analysis Animals Avian Sarcoma Viruses/enzymology,genetics Chick Embryo Mutation Oncogene Protein pp60(v-src) Phosphorylation Protein Kinases/genetics Temperature Viral Proteins/genetics,metabolism
Chemicals
Amino Acids Viral Proteins Protein Kinases Oncogene Protein pp60(v-src)
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Stoker A W
Enrietto P J
Wyke J A
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60 references, click to expand
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/mcb.4.8.1508-1514.1984
Published
1984-08-00
Pages
1508-14
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC368941
Subset
IM
Grants
NCI NIH HHS · 5F 32 CA-06674-02 · United States
External Links
PubMed source DOI: 10.1128/mcb.4.8.1508-1514.1984 PMC Full Text View journal details
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