PROTEIN PHOSPHATASE-2A DEPHOSPHORYLATES SIMIAN VIRUS-40 LARGE T-ANTIGEN SPECIFICALLY AT RESIDUES INVOLVED IN REGULATION OF DNA-BINDING ACTIVITY

被引：50

作者：

SCHEIDTMANN, KH ^{[1
]}

VIRSHUP, DM ^{[1
]}

KELLY, TJ ^{[1
]}

机构：

[1] JOHNS HOPKINS UNIV,SCH MED,DEPT MOLEC BIOL & GENET,BALTIMORE,MD 21205

来源：

JOURNAL OF VIROLOGY | 1991年 / 65卷 / 04期

关键词：

D O I：

10.1128/JVI.65.4.2098-2101.1991

中图分类号：

Q93 [微生物学];

学科分类号：

071005 [微生物学]; 100705 [微生物与生化药学];

摘要：

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.

引用

页码：2098 / 2101

页数：4

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