A structural gene for sigma factor (rpoD) of DNA-dependent RNA polymerase (RNA nucleotidyltransferase; nucleoside-triphosphate: RNA nucleotidyltransferase, E.C. 2.7.7.6) was mapped precisely by a set of F' factors including those already published (Proc. Natl. Acad. Sci. USA. 74, 1831-1835 (1977)).
Altered chemical properties in three mutants of E. coli RNA polymerase sigma subunit
โ Scribed by Burgess, Richard R. ;Gross, Carol A. ;Walter, William ;Lowe, Peter A.
- Publisher
- Springer
- Year
- 1979
- Tongue
- English
- Weight
- 649 KB
- Volume
- 175
- Category
- Article
- ISSN
- 0026-8925
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โฆ Synopsis
We have analyzed some chemical properties of the sigma subunit of RNA polymerase from the sigma mutants: rpoD1 (Gross et al., 1978), rpoD2 (formerly known as alt-1) (Silverstone et al., 1972; Travers et al., 1978), and rpoD800 (Gross et al., 1979). Each of the three mutants is located at about 66 min on the E. coli genetic map and exhibits an alteration in the enzymatic properties of its sigma subunit. The tryptic peptides and isoelectric focusing behavior were analyzed for mutant and wild type sigma. A single, but different altered lysine tryptic peptide was observed for each mutant. No altered arginine tryptic peptides were observed. The rpoD800 mutant sigma showed an altered isoelectric point. These studies provide chemical evidence that the sigma polypeptide in all three mutants is altered and strongly support the conclusion that the mutations are in the structural gene for sigma.
๐ SIMILAR VOLUMES
A mutant of Escherichia coli K12 is described in which sigma and alpha subunits of the DNA-dependent RNA polymerase (EC 2.7.7.6) are produced at the rates much higher than in the normal strain. The rate of synthesis for sigma subunit was found to be at least 10-times higher, though the rapid degrada