Vibrio harveyi RNA polymerase: purification and resolution from gyrase A.
RNA polymerase was purified from Vibrio harveyi and found to contain polypeptides (beta, beta', alpha and sigma) closely corresponding to those of the Escherichia coli enzyme. In vitro transcription studies using V. harveyi and E. coli RNA polymerase demonstrated that the purified V. harveyi RNA polymerase is functional and that the two enzymes have the same promoter specificity. Chromatography through a monoQ column was required to remove a 100-kilodalton protein that was present in large amounts and copurified with the RNA polymerase. N-terminal amino acid sequencing showed that the first 18 amino acids of the 100-kilodalton protein shares 78% sequence identity with the A subunit of gyrase or topoisomerase II. The abundance of the gyrase A protein is unprecedented and may be linked to bioluminescence.
Swartzman
E
E
Department of Biochemistry, McGill University, Montréal, Que., Canada.
Meighen
E A
EA
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000302:isolation & purification*; D004250:DNA Topoisomerases, Type II / Q000235:genetics / Q000302:isolation & purification*; D012321:DNA-Directed RNA Polymerases / Q000235:genetics / Q000302:isolation & purification*; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial; D008163:Luminescent Measurements; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D014158:Transcription, Genetic; D014733:Vibrio / Q000201:enzymology* / Q000235:genetics
D001426:Bacterial Proteins; D012321:DNA-Directed RNA Polymerases; D004250:DNA Topoisomerases, Type II