PMID: 2120186Oct 1, 1990Paper

Purification and partial characterization of the DNA-dependent RNA polymerase from Rickettsia prowazekii

Journal of Bacteriology
H F Ding, H H Winkler

Abstract

The DNA-dependent RNA polymerase was purified from Rickettsia prowazekii, an obligate intracellular bacterial parasite. Because of limitation of available rickettsiae, the classical methods for isolation of the enzyme from other procaryotes were modified to purify RNA polymerase from small quantities of cells (25 mg of protein). The subunit composition of the rickettsial RNA polymerase was typical of a eubacterial RNA polymerase. R. prowazekii had beta' (148,000 daltons), beta (142,000 daltons), sigma (85,000 daltons), and alpha (34,500 daltons) subunits as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The appropriate subunits of the rickettsial RNA polymerase bound to polyclonal antisera against Escherichia coli core polymerase and E. coli sigma 70 subunit in Western blots (immunoblots). The enzyme activity was dependent on all four ribonucleoside triphosphates, Mg2+, and a DNA template. Optimal activity occurred in the presence of 10 mM MgCl2 and 50 mM NaCl. Interestingly, in striking contrast to E. coli, approximately 74% of the rickettsial RNA polymerase activity was associated with the rickettsial cell membrane at a low salt concentration (50 mM NaCl) and dissociated from the membrane at a high s...Continue Reading

References

Sep 1, 1987·Infection and Immunity·H H Winkler
Aug 1, 1987·Journal of Bacteriology·D O WoodD C Krause
Jan 1, 1986·Advances in Biophysics·A Ishihama
Jun 27, 1973·Nature: New Biology·A Travers, R Buckland
Jan 1, 1982·Annual Review of Microbiology·E Weiss

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Citations

Mar 1, 1996·Journal of Bacteriology·H Pang, H H Winkler
Nov 1, 1995·Journal of Bacteriology·L P Aniskovitch, H H Winkler
Dec 24, 2003·Analytical Biochemistry·Peter KuhlmanAshley Galant

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