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

Karl Heinz Scheidtmann, David M. Virshup, Thomas Kelly

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)2098-2101
Number of pages4
JournalJournal of Virology
Volume65
Issue number4
StatePublished - 1991
Externally publishedYes

Fingerprint

Simian virus 40
Protein Phosphatase 2
phosphoprotein phosphatase
Viral Tumor Antigens
antigens
DNA
peptide mapping
Phosphoserine
Peptide Mapping
protein subunits
DNA Replication
Phosphoric Monoester Hydrolases
serine
Catalytic Domain
phosphates

ASJC Scopus subject areas

  • Immunology

Cite this

Protein phosphatase 2A dephosphorylates simian virus 40 large T antigen specifically at residues involved in regulation of DNA-binding activity. / Scheidtmann, Karl Heinz; Virshup, David M.; Kelly, Thomas.

In: Journal of Virology, Vol. 65, No. 4, 1991, p. 2098-2101.

Research output: Contribution to journalArticle

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