Affiliation:
1. Department of Molecular Biology, Division of Biological Sciences, Albert Einstein College of Medicine, Bronx, New York 10461
Abstract
Deoxyribonucleic acid-dependent ribonucleic acid (RNA) polymerase (EC 2.7.7.6) was purified from the dimorphic bacterium
Caulobacter crescentus
at three stages in development. Enzyme from pure populations of stalked cells, as well as populations enriched in swarmer and predivisional cells, appeared identical in subunit structure and template requirements. The molecular weights of the enzyme subunits were 165,000, 155,000, 101,000, and 44,000, respectively. By analogy with RNA polymerase from other bacterial sources, they are considered to be components of the
C. crescentus
holoenzyme, β′, β, σ, and α, respectively. The
C. crescentus
enzyme appeared similar to the
Pseudomonas aeruginosa
enzyme and unlike the
Escherichia coli
enzyme with respect to subunit molecular weights and failure to separate into core and sigma components upon phosphocellulose chromatography. In addition, the effects of ionic strength on the time course of polymerization varied both with the sources of bacterial polymerase and bacteriophage DNA.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
31 articles.
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