A RNA polymerase with transcriptional activity at 0 degrees C from the Antarctic bacterium Pseudomonas syringae.
A DNA-dependent RNA polymerase was purified from the Antarctic psychrotrophic bacterium Pseudomonas syringae. The RNA polymerase showed a typical eubacterial subunit composition with beta, beta', alpha2 and sigma subunits. The subunits cross-reacted with antibodies raised against holoenzyme and the individual subunits of the RNA polymerase of Escherichia coli. However, the enzyme was considered unique, since unlike the RNA polymerase of mesophilic E. coli it exhibited significant and consistent transcriptional activity (10-15%) even at 0 degrees C. But, similar to the enzyme from the mesophilic bacterium, the RNA polymerase from P. syringae exhibited optimum activity at 37 degrees C. The study also demonstrates that the RNA polymerase of P. syringae could preferentially transcribe the cold-inducible gene cspA of E. coli only at lower temperatures (0-22 degrees C). The polymerase was also observed to be relatively more rifampicin-resistant during transcription at lower temperature.
Uma
S
S
Centre for Cellular and Molecular Biology, Hyderabad, India.
Jadhav
R S
RS
Kumar
G S
GS
Shivaji
S
S
Ray
M K
MK
D000220:Adaptation, Biological; D000595:Amino Acid Sequence; D000864:Antarctic Regions; D001426:Bacterial Proteins / Q000096:biosynthesis; D003080:Cold Temperature; D012321:DNA-Directed RNA Polymerases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D015870:Gene Expression; D008969:Molecular Sequence Data; D019384:Nucleic Acid Synthesis Inhibitors / Q000494:pharmacology; D011487:Protein Conformation; D011549:Pseudomonas / Q000201:enzymology*; D012293:Rifampin / Q000494:pharmacology*; D014158:Transcription, Genetic
D001426:Bacterial Proteins; D019384:Nucleic Acid Synthesis Inhibitors; C062260:cold shock protein CS7.4, Bacteria; D012321:DNA-Directed RNA Polymerases; D012293:Rifampin