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PMID: 2153233 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Simian virus 40 large T antigen induces or activates a protein kinase which phosphorylates the transformation-associated protein p53.

Journal of virology ·Vol. 64 ·No. 2 ·1990-02-00 ·Pages 672-9

Scheidtmann KH, Haber A

Abstract

The cellular phosphoprotein p53 is presumably involved in simian virus 40 (SV40)-induced transformation. We have monitored changes in the state of phosphorylation of p53 from normal versus SV40-infected or -transformed cells. In normal cells, p 53 was hardly phosphorylated. Upon infection or transformation, a quantitative and qualitative increase in p53 phosphorylation was observed as revealed by two-dimensional phosphopeptide analysis. This increase was dependent on a functional large T antigen. In rat cells, enhanced phosphorylation of p53 resulted in conversion to a second, electrophoretically distinct form. In cells transformed with transformation-defective mutants, phosphorylation of p53 was reduced and conversion to form 2 was inefficient. These data suggest (i) that SV40 large T antigen induces or activates a protein kinase, one substrate of which is p53, (ii) that transformation-defective mutants are impaired in kinase induction, and (iii) that either a certain phosphorylation state of p53 or the SV40-induced kinase is critical for efficient transformation.

MeSH Terms
Animals Antigens, Polyomavirus Transforming Cell Line Cell Transformation, Viral Electrophoresis, Gel, Two-Dimensional Electrophoresis, Polyacrylamide Gel Kinetics Nuclear Proteins/metabolism Oncogene Proteins/isolation & purification,metabolism Peptide Fragments/isolation & purification Phosphopeptides/isolation & purification Phosphoproteins/isolation & purification,metabolism Phosphoric Monoester Hydrolases Phosphorylation Protein Kinases/biosynthesis,metabolism Simian virus 40/genetics,immunology Tumor Suppressor Protein p53
Chemicals
Antigens, Polyomavirus Transforming Nuclear Proteins Oncogene Proteins Peptide Fragments Phosphopeptides Phosphoproteins Tumor Suppressor Protein p53 Protein Kinases Phosphoric Monoester Hydrolases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Scheidtmann K H
Institut für Immunbiologie, Universität Freiburg, Federal Republic of Germany.
Haber A
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.64.2.672-679.1990
Published
1990-02-00
Pages
672-9
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC249159
Subset
IM
External Links
PubMed source DOI: 10.1128/JVI.64.2.672-679.1990 PMC Full Text View journal details
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