Abstract
Highly purified rho termination factor from Escherichia coli catalyzes an RNA-dependent hydrolysis of ribonucleoside triphosphates to nucleoside diphosphates and inorganic phosphate. In the presence of poly(C), a specific activity of 100 μmole of ATP hydrolyzed per min/mg has been measured. The phosphohydrolase activity appears to be associated with the protein responsible for termination of RNA synthesis, but a functional relationship between the two activities is not yet evident. Hydrolysis of nucleoside triphosphates occurs in the absence of termination and without any extensive degradation of RNA.
Dates
Type | When |
---|---|
Created | 19 years, 2 months ago (May 31, 2006, 2:55 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 10:26 a.m.) |
Indexed | 1 week ago (Aug. 19, 2025, 6:40 a.m.) |
Issued | 51 years, 3 months ago (May 1, 1974) |
Published | 51 years, 3 months ago (May 1, 1974) |
Published Online | 51 years, 3 months ago (May 1, 1974) |
Published Print | 51 years, 3 months ago (May 1, 1974) |
@article{Lowery_Goldhammer_1974, title={An RNA-Dependent Nucleoside Triphosphate Phosphohydrolase (ATPase) Associated with Rho Termination Factor}, volume={71}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.71.5.2003}, DOI={10.1073/pnas.71.5.2003}, number={5}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Lowery-Goldhammer, Carolyn and Richardson, John P.}, year={1974}, month=may, pages={2003–2007} }