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

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.

journal_name

J Virol

journal_title

Journal of virology

authors

Scheidtmann KH,Virshup DM,Kelly TJ

doi

10.1128/JVI.65.4.2098-2101.1991

subject

Has Abstract

pub_date

1991-04-01 00:00:00

pages

2098-101

issue

4

eissn

0022-538X

issn

1098-5514

journal_volume

65

pub_type

杂志文章