Work

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

Year: 1991

Type: article

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.

Source: Journal of Virology

DOI: 10.1128/jvi.65.4.2098-2101.1991

Authors: K H Scheidtmann, D M Virshup, T J Kelly

Institution: University of Bonn

Language: English

Topic: Polyomavirus and related diseases

Subfield: Oncology

Field: Medicine

Domain: Health Sciences

Open Access status: green

Funders: National Institutes of Health, National Cancer Institute

Awards: G1823966086, G1890337441, Program on Molecular and Cellular Mechanisms of Tumorigenesis