PMID: 6169371Sep 28, 1981Paper

Template-binding site of AMV reverse transcriptase and inactivation of the enzyme by N-ethylmaleimide

Biochimica Et Biophysica Acta
V K Parnaik, M R Das

Abstract

N-Ethylmaleimide, a sulfhydryl-specific reagent, strongly inhibits AMV reverse transcriptase by specifically interfering with the template-binding site of the enzyme. However, the kinetics of inhibition differ widely with the composition and structure of the templates employed. The copying of templates with multiple 3'-hydroxyl termini appeared to be more susceptible to N-ethylmaleimide treatment, suggesting that the reagent may interfere with initiation of DNA synthesis. The ability of a template bound to enzyme prior to N-ethylmaleimide treatment to protect against inactivation of copying of other templates also, implies a common binding site for the different templates. Template exchange experiments demonstrated competition between activated calf thymus DNA and rAn . dT12--18 for binding to the enzyme. Thus, templates varying widely in composition and conformation appear to bind at a common site on reverse transcriptase. The experimental data also show suggestive evidence for small but finite differences in the requirements for optimal binding for templates of different structures.

References

Dec 1, 1970·Proceedings of the National Academy of Sciences of the United States of America·E ScolnickG J Todaro
Jul 1, 1971·Proceedings of the National Academy of Sciences of the United States of America·D Baltimore, D Smoler
Aug 20, 1971·Biochemical and Biophysical Research Communications·A SchlabachA Weissbach
May 1, 1967·The British Journal of Psychiatry : the Journal of Mental Science·J MarconiL Moya
Sep 30, 1980·Biochemical and Biophysical Research Communications·M J ModakE Gillerman

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