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Recognition Sites around the Catalytic Centre of DNA-dependent RNA Polymerase

Nature volume 227, pages 57–59 (1970)Cite this article

Abstract

WE have been studying the structure of enzymes of nucleic acid metabolism by amino-acid sequence analysis and affinity labelling techniques and hope in this way to discover specific enzyme inhibitors. We report here the inhibition of purified DNA-dependent RNA polyrnerase from Escherichia coli by the nucleoside analogues, β-D-ribosyl-6-methyl-thiopurine (MMPR, methylthioinosine) and its periodate oxidation product (MMPR-OP), and by β-D-arabinosyl-6-mercaptopurine (Ara-6MP). We also report a lack of inhibition by the arabinosides of cytosine (Ara-C) and adenine (Ara-A). The results lead us to propose a tentative stochastic model for the catalytic centre of DNA-dependent RNA polyinerase from E. coli B.

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Authors and Affiliations

  1. Departments of Biophysical Sciences and Biology, University of Houston, Houston, Texas, 77004

    T. C. SPOOR, F. PERSICO, J. EVANS & A. P. KIMBALL

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  1. T. C. SPOOR
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  2. F. PERSICO
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  3. J. EVANS
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  4. A. P. KIMBALL
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SPOOR, T., PERSICO, F., EVANS, J. et al. Recognition Sites around the Catalytic Centre of DNA-dependent RNA Polymerase. Nature 227, 57–59 (1970). https://doi.org/10.1038/227057b0

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  • DOI: https://doi.org/10.1038/227057b0

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