Harshey, R. M. ; Ramakrishnan, T. (1976) Purification and properties of DNA-dependent RNA polymerase from Mycobacterium tuberculosis H37Rv Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 432 (1). pp. 49-59. ISSN 0005-2787
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Official URL: http://dx.doi.org/10.1016/0005-2787(76)90040-X
Related URL: http://dx.doi.org/10.1016/0005-2787(76)90040-X
Abstract
RNA polymerase (nucleosidetriphosphate : RNA nucleotidyltransferase (DNA-dependent), EC 2.7.7.6) was purified approximately 200 fold from Mycobacterium tuberculosis H37Rv cells. The purified enzyme has a molecular weight of about 330 000-350 000 and is composed of four subunits. The subunits β', β and σ have molecular weights different from those of Escherichia coli polymerase; the fourth, α subunit has a similar weight. The purified enzyme is a thousand-fold more sensitive to rifampicin, a potent antitubercular drug, than the E. coli RNA polymerase, probably because of the difference in the β subunits. This, with other data presented in this paper, indicate that the RNA polymerase of M. tuberculosis differs in its properties from that of E. coli.
Item Type: | Article |
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Source: | Copyright of this article belongs to Elsevier Science. |
ID Code: | 49211 |
Deposited On: | 19 Jul 2011 11:54 |
Last Modified: | 19 Jul 2011 11:54 |
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