scholarly journals The dissociation of σ-factor from ribonucleic acid polymerase

1977 ◽  
Vol 163 (1) ◽  
pp. 177-179 ◽  
Author(s):  
A M Campbell ◽  
P A Lowe
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Ribonucleic Acid ◽  
Sigma Factor ◽  
Association Constant ◽  
Absolute Concentration ◽  
The Core ◽  
Core Enzyme ◽  
Σ Factor ◽  
The Absolute

The sigma-factor of Escherichia coli RNA polymerase was shown to dissociate from the core enzyme as a function of absolute concentration. The association constant is in the range 10(6)-10(8) litre/mol. This implies that the amount of holoenzyme, core enzyme and sigma-factor in RNA polymerase assays may vary according to the absolute concentration of the enzyme.

scholarly journals Crl Facilitates RNA Polymerase Holoenzyme Formation

2006 ◽  
Vol 188 (22) ◽  
pp. 7966-7970 ◽  
Author(s):  
Tamas Gaal ◽  
Mark J. Mandel ◽  
Thomas J. Silhavy ◽  
Richard L. Gourse
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Stationary Phase ◽  
Mechanism Of Action ◽  
Sigma Factor ◽  
Transcriptional Coactivator ◽  
Transcription System ◽  
The Core ◽  
Core Enzyme ◽  
Rna Polymerase Holoenzyme

ABSTRACT The Escherichia coli Crl protein has been described as a transcriptional coactivator for the stationary-phase sigma factor σS. In a transcription system with highly purified components, we demonstrate that Crl affects transcription not only by the EσS RNA polymerase holoenzyme but also by Eσ70 and Eσ32. Crl increased transcription dramatically but only when the σ concentration was low and when Crl was added to σ prior to assembly with the core enzyme. Our results suggest that Crl facilitates holoenzyme formation, the first positive regulator identified with this mechanism of action.

scholarly journals The interaction between σS , the stationary phase σ factor, and the core enzyme of Escherichia coli RNA polymerase

2002 ◽  
Vol 7 (3) ◽  
pp. 233-247 ◽  
Author(s):  
Frédéric Colland ◽  
Nobuyuki Fujita ◽  
Akira Ishihama ◽  
Annie Kolb
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Stationary Phase ◽  
The Core ◽  
Core Enzyme ◽  
Σ Factor

Salt-dependent binding of Escherichia coli RNA polymerase to DNA and specific transcription by the core enzyme and holoenzyme

Biochemistry ◽  
1987 ◽  
Vol 26 (12) ◽  
pp. 3322-3330 ◽  
Author(s):  
Annemarie R. Wheeler ◽  
A. Young M. Woody ◽  
Robert W. Woody
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
The Core ◽  
Core Enzyme

scholarly journals Mass Spectrometry of Escherichia coli RNA Polymerase: Interactions of the Core Enzyme with σ70 and Rsd Protein

Structure ◽  
2004 ◽  
Vol 12 (2) ◽  
pp. 269-275 ◽  
Author(s):  
Leopold L. Ilag ◽  
Lars F. Westblade ◽  
Caroline Deshayes ◽  
Annie Kolb ◽  
Stephen J.W. Busby ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Escherichia Coli ◽  
Rna Polymerase ◽  
The Core ◽  
Core Enzyme

scholarly journals 1H n.m.r. of the DNA-dependent RNA polymerase from Escherichia coli

1982 ◽  
Vol 207 (1) ◽  
pp. 175-177 ◽  
Author(s):  
Lucian Cellai ◽  
Annalaura Segre ◽  
Hermann Heumann
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Ionic Strength ◽  
Rna Polymerase ◽  
The Other ◽  
Basic Amino Acids ◽  
The Core ◽  
Core Enzyme

The1H n.m.r. study of the DNA-dependent RNA polymerase from Escherichia coli has revealed that the holoenzyme (ββ′α2σ) displays two mobile regions: one, observable also in the core enzyme (ββ′α2), is characterized by basic amino acids and its appearance and form depend on ionic strength; the other, specific to the holoenzyme, is characterized by threonine residues and its appearance does not depend on ionic strength.

scholarly journals Interaction of sigma factor σN with Escherichia coli RNA polymerase core enzyme

2000 ◽  
Vol 352 (2) ◽  
pp. 539 ◽  
Author(s):  
David J. SCOTT ◽  
Anna L. FERGUSON ◽  
Maria-Trinidad GALLEGOS ◽  
Melinda PITT ◽  
Martin BUCK ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Sigma Factor ◽  
Core Enzyme

Spatial arrangement of σ-factor and core enzyme of Escherichia coli RNA polymerase

1991 ◽  
Vol 219 (4) ◽  
pp. 747-755 ◽  
Author(s):  
Hermann Lederer ◽  
Kell Mortensen ◽  
Roland P. May ◽  
Gisela Baer ◽  
Henry L. Crespi ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Spatial Arrangement ◽  
Core Enzyme ◽  
Σ Factor

scholarly journals Mapping of the Rsd Contact Site on the Sigma 70 Subunit of Escherichia coli RNA Polymerase

2001 ◽  
Vol 183 (9) ◽  
pp. 2952-2956 ◽  
Author(s):  
Miki Jishage ◽  
Dipak Dasgupta ◽  
Akira Ishihama
Keyword(s):  
Escherichia Coli ◽  
Transcription Factors ◽  
Complex Formation ◽  
Rna Polymerase ◽  
Sigma Factor ◽  
Cleavage Sites ◽  
Contact Site ◽  
Core Enzyme ◽  
Recognition Helix ◽  
Sigma 70

ABSTRACT Rsd (regulator of sigma D) is an anti-sigma factor for theEscherichia coli RNA polymerase ς70 subunit. The contact site of Rsd on ς70 was analyzed after mapping of the contact-dependent cleavage sites by Rsd-tethered iron-p-bromoacetamidobenzyl EDTA and by analysis of the complex formation between Ala-substituted ς70 and Rsd. Results indicate that the Rsd contact site is located downstream of the promoter −35 recognition helix-turn-helix motif within region 4, overlapping with the regions involved in interaction with both core enzyme and ς70 contact transcription factors.

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