PMID: 816387Apr 15, 1976

Purification and properties of DNA-dependent RNA polymerase from Mycobacterium tuberculosis H37RV

Biochimica Et Biophysica Acta
R M Harshey, T Ramakrishnan

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 beta', beta and sigma have molecular weights different from those of Escherichia coli polymerase; the fourth, alpha 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 beta 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.

Citations

Jan 1, 1996·Research in Microbiology·S T Cole
Aug 29, 2007·Antimicrobial Agents and Chemotherapy·Tawanda GumboG L Drusano
Oct 1, 1982·Antimicrobial Agents and Chemotherapy·A JoshiM Chakravorty
Jul 1, 1995·Antimicrobial Agents and Chemotherapy·K FujiiK Hosoe
Feb 24, 2006·Antimicrobial Agents and Chemotherapy·Christopher K MurphyDavid M Rothstein
Mar 19, 2005·Journal of Bacteriology·Sougata Roy, Parthasarathi Ajitkumar
Sep 7, 2001·Annual Review of Microbiology·L G Wayne, C D Sohaskey
Dec 30, 2015·Antimicrobial Agents and Chemotherapy·G L DrusanoWilliam Hope
Mar 23, 2017·Protein Expression and Purification·Omar Herrera-AsmatMaria L Kireeva

Related Concepts

Antitubercular Agents
Antiviral Agents
Enzyme Activation
Alkalescens-Dispar Group
Immunodiffusion Measurement
Magnesium
Manganese
Mycobacterium tuberculosis H37Rv
Tubocin
Transcriptase

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