Mutations in the sigma subunit of E. coli RNA polymerase which affect positive control of transcription

1985 ◽  
Vol 199 (1) ◽  
pp. 7-13 ◽  
Author(s):  
James C. Hu ◽  
Carol A. Gross
Keyword(s):  
Rna Polymerase ◽  
Positive Control ◽  
E Coli ◽  
Sigma Subunit

scholarly journals Substitutions in Bacteriophage T4 AsiA andEscherichia coli ς70 That Suppress T4motA Activation Mutations

2001 ◽  
Vol 183 (7) ◽  
pp. 2289-2297 ◽  
Author(s):  
Marco P. Cicero ◽  
Meghan M. Sharp ◽  
Carol A. Gross ◽  
Kenneth N. Kreuzer
Keyword(s):  
Rna Polymerase ◽  
Burst Size ◽  
Bacteriophage T4 ◽  
In Vitro Transcription ◽  
Positive Control ◽  
Plaque Morphology ◽  
Mutant Proteins ◽  
E Coli

ABSTRACT Bacteriophage T4 middle-mode transcription requires two phage-encoded proteins, the MotA transcription factor and AsiA coactivator, along with Escherichia coli RNA polymerase holoenzyme containing the ς70 subunit. AmotA positive control (pc) mutant, motA-pc1, was used to select for suppressor mutations that alter other proteins in the transcription complex. Separate genetic selections isolated two AsiA mutants (S22F and Q51E) and five ς70 mutants (Y571C, Y571H, D570N, L595P, and S604P). All seven suppressor mutants gave partial suppressor phenotypes in vivo as judged by plaque morphology and burst size measurements. The S22F mutant AsiA protein and glutathione S-transferase fusions of the five mutant ς70 proteins were purified. All of these mutant proteins allowed normal levels of in vitro transcription when tested with wild-type MotA protein, but they failed to suppress the mutant MotA-pc1 protein in the same assay. The ς70 substitutions affected the 4.2 region, which binds the −35 sequence of E. coli promoters. In the presence of E. coli RNA polymerase without T4 proteins, the L595P and S604P substitutions greatly decreased transcription from standard E. colipromoters. This defect could not be explained solely by a disruption in −35 recognition since similar results were obtained with extended −10 promoters. The generalized transcriptional defect of these two mutants correlated with a defect in binding to core RNA polymerase, as judged by immunoprecipitation analysis. The L595P mutant, which was the most defective for in vitro transcription, failed to support E. coli growth.

The Kinetics of Sigma Subunit Directed Promoter Recognition by E. coli RNA Polymerase

1999 ◽  
Vol 285 (3) ◽  
pp. 955-964 ◽  
Author(s):  
Malcolm Buckle ◽  
Iain K. Pemberton ◽  
Marie-Ange Jacquet ◽  
Henri Buc
Keyword(s):  
Rna Polymerase ◽  
E Coli ◽  
Promoter Recognition ◽  
Sigma Subunit ◽  
Kinetics Of

A new mutation rpoD800, affecting the sigma subunit of E. coli RNA polymerase is allelic to two other sigma mutants

1980 ◽  
Vol 177 (2) ◽  
pp. 277-282 ◽  
Author(s):  
Hope Liebke ◽  
Carol Gross ◽  
William Walter ◽  
Richard Burgess
Keyword(s):  
Rna Polymerase ◽  
New Mutation ◽  
E Coli ◽  
Sigma Subunit

The operen that encodes the sigma subunit of RNA polymerase also encodes ribosomal protein S21 and DNA primase in E. coli K12

Cell ◽  
1983 ◽  
Vol 32 (2) ◽  
pp. 335-349 ◽  
Author(s):  
Zachary F. Burton ◽  
Carol A. Gross ◽  
Kathleen K. Watanabe ◽  
Richard R. Burgess
Keyword(s):  
Rna Polymerase ◽  
Ribosomal Protein ◽  
E Coli ◽  
Dna Primase ◽  
Sigma Subunit

Transcription from a heat-inducible promoter causes heat shock regulation of the sigma subunit of E. coli RNA polymerase

Cell ◽  
1984 ◽  
Vol 38 (2) ◽  
pp. 371-381 ◽  
Author(s):  
Wayne E. Taylor ◽  
David B. Straus ◽  
Alan D. Grossman ◽  
Zachary F. Burton ◽  
Carol A. Gross ◽  
...  
Keyword(s):  
Heat Shock ◽  
Rna Polymerase ◽  
Inducible Promoter ◽  
E Coli ◽  
Sigma Subunit

Altered chemical properties in three mutants of E. coli RNA polymerase sigma subunit

1979 ◽  
Vol 175 (3) ◽  
pp. 251-257 ◽  
Author(s):  
Richard R. Burgess ◽  
Carol A. Gross ◽  
William Walter ◽  
Peter A. Lowe
Keyword(s):  
Rna Polymerase ◽  
Chemical Properties ◽  
E Coli ◽  
Sigma Subunit

Mutations in the Lon gene of E. coli K12 phenotypically suppress a mutation in the sigma subunit of RNA polymerase

Cell ◽  
1983 ◽  
Vol 32 (1) ◽  
pp. 151-159 ◽  
Author(s):  
Alan D. Grossman ◽  
Richard R. Burgess ◽  
William Walter ◽  
Carol A. Gross
Keyword(s):  
Rna Polymerase ◽  
E Coli ◽  
Sigma Subunit

RNA polymerase: Preparation and structural analysis of helical polymers

1984 ◽  
Vol 42 ◽  
pp. 152-153
Author(s):  
E. Loren Buhle ◽  
Pamela Rew ◽  
Ueli Aebi
Keyword(s):  
Structural Analysis ◽  
Rna Polymerase ◽  
Molecular Level ◽  
X Ray Diffraction ◽  
Helical Polymers ◽  
X Ray ◽  
E Coli ◽  
The Past ◽  
Ordered Arrays ◽  
Low Ionic Strength

While DNA-dependent RNA polymerase represents one of the key enzymes involved in transcription and ultimately in gene expression in procaryotic and eucaryotic cells, little progress has been made towards elucidation of its 3-D structure at the molecular level over the past few years. This is mainly because to date no 3-D crystals suitable for X-ray diffraction analysis have been obtained with this rather large (MW ~500 kd) multi-subunit (α2ββ'ζ). As an alternative, we have been trying to form ordered arrays of RNA polymerase from E. coli suitable for structural analysis in the electron microscope combined with image processing. Here we report about helical polymers induced from holoenzyme (α2ββ'ζ) at low ionic strength with 5-7 mM MnCl2 (see Fig. 1a). The presence of the ζ-subunit (MW 86 kd) is required to form these polymers, since the core enzyme (α2ββ') does fail to assemble into such structures under these conditions.

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