Publikation: Simian‐virus‐40 large‐T‐antigen‐catalyzed DNA and RNA unwinding reactions
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Simian virus 40 large T antigen is a helicase separating the complementary strands of double-stranded DNA in the presence of hydrolyzable ATP and of double-stranded RNA in the presence of non-ATP nucleotides (GTP, CTP or UTP). We have constructed partially single-stranded nucleic acid substrates consisting of RNA or DNA strands hydrogen bonded to either RNA or DNA complements. We found that ATP is utilized as a cofactor for the T-antigen-catalyzed unwinding reaction when the substrates contain overhanging single-stranded DNA, regardless of whether the double-stranded region is DNA or hybrid DNA · RNA. Conversely, non-ATP nucleotides are used when the overhanging single strand is RNA. Based on these and additional findings, we propose that the bound nucleic acid induces a conformational change in T antigen resulting in a proper orientation of both nucleic acid and nucleotide relative to the active center of the ATPase/helicase domain of the enzyme. The implications of our conclusion for the roles which T antigen may play in vivo are discussed.
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SCHEFFNER, Martin, Rolf KNIPPERS, Hans STAHL, 1991. Simian‐virus‐40 large‐T‐antigen‐catalyzed DNA and RNA unwinding reactions. In: European Journal of Biochemistry. 1991, 195(1), pp. 49-54. ISSN 0014-2956. eISSN 1432-1033. Available under: doi: 10.1111/j.1432-1033.1991.tb15674.xBibTex
@article{Scheffner1991Simia-42732, year={1991}, doi={10.1111/j.1432-1033.1991.tb15674.x}, title={Simian‐virus‐40 large‐T‐antigen‐catalyzed DNA and RNA unwinding reactions}, number={1}, volume={195}, issn={0014-2956}, journal={European Journal of Biochemistry}, pages={49--54}, author={Scheffner, Martin and Knippers, Rolf and Stahl, Hans} }
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