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PMID: 1848320 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Protein phosphatase 2A dephosphorylates simian virus 40 large T antigen specifically at residues involved in regulation of DNA-binding activity.

Journal of virology ·Vol. 65 ·No. 4 ·1991-04-00 ·Pages 2098-101

Scheidtmann KH, Virshup DM, Kelly TJ

Abstract

Treatment of purified simian virus 40 large T antigen (LT) with protein phosphatase 2A stimulates LT-dependent DNA unwinding and replication (D. M. Virshup, M. G. Kauffman, and T. J. Kelly, EMBO J. 8: 3891-3898, 1989). The specificity of the catalytic subunit of protein phosphatase 2A toward LT was investigated by two-dimensional peptide mapping. Increasing amounts of phosphatase sequentially removed the phosphates from serine residues 120, 123, 677, and perhaps 679, residues which have been implicated in regulating the DNA-binding activity of LT.

MeSH Terms
Animals Antigens, Viral, Tumor/immunology Cells, Cultured DNA, Viral/metabolism Electrophoresis, Gel, Two-Dimensional Haplorhini Phosphoprotein Phosphatases/metabolism Phosphorylation Protein Phosphatase 2 Simian virus 40/enzymology,genetics,immunology
Chemicals
Antigens, Viral, Tumor DNA, Viral Phosphoprotein Phosphatases Protein Phosphatase 2
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Scheidtmann K H
Institut für Genetik, Universität Bonn, Federal Republic of Germany.
Virshup D M
Kelly T J
References (30)
30 references, click to expand
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.65.4.2098-2101.1991
Published
1991-04-00
Pages
2098-101
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC240073
Subset
IM
Grants
NCI NIH HHS · CA-16519 · United States
NCI NIH HHS · CA-40414 · United States
External Links
PubMed source DOI: 10.1128/JVI.65.4.2098-2101.1991 PMC Full Text View journal details
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