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

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Scheidtmann, KH; Virshup, DM; Kelly, TJ

Published Date

  • April 1991

Published In

Volume / Issue

  • 65 / 4

Start / End Page

  • 2098 - 2101

PubMed ID

  • 1848320

Pubmed Central ID

  • 1848320

International Standard Serial Number (ISSN)

  • 0022-538X

Language

  • eng

Conference Location

  • United States