Interaction between Escherichia coli RNA polymerase and its substrates, the nucleoside triphosphates, was studied by gel-filtration and dialysis-rate-measurement techniques. 2. The holoenzyme bound variable amounts of ATP and GTP. There was no correlation between substrate-binding ability and enzyme activity of different enzyme preparations. 3. The core enzyme bound a maximum of 0.1 mol of ATP/mol of enzyme. The dissociation constant of this interaction was of the order of 1 × 10(-5)M. The core enzyme did not bind GTP. 4. A protein of mol.wt. 60000, which was eluted in the first fraction during phosphocellulose column chromatography of the holoenzyme, bound appreciable amounts of ATP. The dissociation constant of this interaction was of the order of 3 × 10(-5)-5 × 10(-6)M. 5. Evidence presented shows that this protein, and not the sigma factor, is responsible for the observed variation in the ATP-binding ability of the holoenzyme.
Skip Nav Destination
Article navigation
January 1976
-
Cover Image
Cover Image
- PDF Icon PDF LinkFront Matter
- PDF Icon PDF LinkTable of Contents
- PDF Icon PDF LinkAdvertising
Research Article|
January 01 1976
Substrate-binding ability of Escherichia coli ribonucleic acid polymerase in relation to its protein composition
A Rognes;
A Rognes
1Department of Biochemistry, University of Bergen, 5000 Bergen, Norway
Search for other works by this author on:
K A Abraham
K A Abraham
1Department of Biochemistry, University of Bergen, 5000 Bergen, Norway
Search for other works by this author on:
Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 1976 London: The Biochemical Society
1976
Biochem J (1976) 153 (1): 55–62.
Citation
A Rognes, K A Abraham; Substrate-binding ability of Escherichia coli ribonucleic acid polymerase in relation to its protein composition. Biochem J 1 January 1976; 153 (1): 55–62. doi: https://doi.org/10.1042/bj1530055
Download citation file:
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Could not validate captcha. Please try again.
Biochemical Society Member Sign in
Sign InSign in via your Institution
Sign in via your InstitutionGet Access To This Article
4
Views