Autor: |
Gragerov, A. I., Kocherginskaya, S. A., Larionov, O. A., Kalyaeva, E. S., Nikiforov, V. G. |
Zdroj: |
Molecular and General Genetics MGG; November 1980, Vol. 180 Issue: 2 p399-403, 5p |
Abstrakt: |
RNA polymerases with a cold-sensitive activity were purified from seven mutants of Escherichia coli. Subunit reconstitution experiments have shown that RNA polymerases from three mutants (RpoB262, RpoB264, and RpoB264) owed their cold sensitivity to alterations in the ß-subunit. Three mutants (RpoC3, RpoC263, and RpoC267) were shown to be defective in the ß' subunit and one (RpoBC266) in bot ß and ß' subunits. Two mutations (rpoC3 and rpoC263) reduced the level of RNA polymerase reconstitution. RNA polymerases from RpoC3 and RpoBC266 mutants are defective in RNA chain elongation at 6°C, while all the other mutants are defective in RNA polymerase-promoter interaction. Most mutant RNA polymerases differ from the wild-type enzyme in transcription selectivity. The results obtained in this study indicate that both ß and ß' subunits are involved in RNA chain elongation and promoter binding and selection. |
Databáze: |
Supplemental Index |
Externí odkaz: |
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