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RNA unwinding activity of SV40 large T antigen

Authors
Journal
Cell
0092-8674
Publisher
Elsevier
Publication Date
Volume
57
Issue
6
Identifiers
DOI: 10.1016/0092-8674(89)90334-6
Disciplines
  • Biology

Abstract

Abstract Large T antigen, the regulatory protein encoded by simian virus 40, has DNA helicase activity and unwinds double-stranded DNA at the expense of ATP. T antigen also functions as an RNA helicase separating duplex regions in partially double-stranded RNA substrates. Surprisingly, T antigen RNA helicase activity requires UTP, CTP, or GTP as a cofactor, whereas ATP is an inefficient energy source for the RNA unwinding reaction. Accordingly, T antigen has both an intrinsic non-ATP NTPase activity that is stimulated by single-stranded RNA and an ATPase activity stimulated by single-stranded DNA. Thus, it appears that the bound nucleotide determines whether T antigen acts as an RNA helicase or as a DNA helicase.

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