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RNA unwinding activity of SV40 large T antigen

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1989

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Stahl, Hans

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https://doi.org/10.1016/0092-8674(89)90334-6
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Cell. 1989, 57(6), pp. 955-963. ISSN 0092-8674. eISSN 1097-4172. Available under: doi: 10.1016/0092-8674(89)90334-6

Zusammenfassung

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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570 Biowissenschaften, Biologie

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ISO 690SCHEFFNER, Martin, Rolf KNIPPERS, Hans STAHL, 1989. RNA unwinding activity of SV40 large T antigen. In: Cell. 1989, 57(6), pp. 955-963. ISSN 0092-8674. eISSN 1097-4172. Available under: doi: 10.1016/0092-8674(89)90334-6
BibTex
@article{Scheffner1989-06unwin-42736,
  year={1989},
  doi={10.1016/0092-8674(89)90334-6},
  title={RNA unwinding activity of SV40 large T antigen},
  number={6},
  volume={57},
  issn={0092-8674},
  journal={Cell},
  pages={955--963},
  author={Scheffner, Martin and Knippers, Rolf and Stahl, Hans}
}
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    <dcterms:abstract xml:lang="eng">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.</dcterms:abstract>
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