Ribonuclease V of Escherichia Coli, I. Dependence on Ribosomes and Translocation
Abstract
A new RNase activity, tentatively named RNase V, was found in cell-free extracts of E. coli. This activity requires ribosomes, G and T factors, tRNA, K+ or NH4+, Mg2+, GTP, and a sulfhydryl compound to degrade poly U, poly A, T4 phage mRNA, or E. coli mRNA. RNase V is specific for mRNA; it does not attack ribosomal RNA. It is inhibited by antibiotics that decrease breakdown of mRNA in vivo, such as chloramphenicol and streptomycin, and by such agents as 5‧-β, γ-methylene-guanosine triphosphate, and fusidic acid, which inhibit ribosome-dependent GTPase and translocation of ribosomes along mRNA. The evidence suggests that RNase V is either an integral part of the ribosome or is tightly associated with it, and that it selectively degrades mRNA in intact cells.
- Publication:
-
Proceedings of the National Academy of Science
- Pub Date:
- October 1969
- DOI:
- 10.1073/pnas.64.2.693
- Bibcode:
- 1969PNAS...64..693K