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

K. H. Scheidtmann, D. M. Virshup, T. J. Kelly

Research output: Contribution to journalArticlepeer-review

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
DOIs
StatePublished - 1991
Externally publishedYes

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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