Specific cleavage of bacteriophage R17 RNA by an endonuclease isolated from E. coli MRE-600.
- 1 March 1968
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 59 (3), 876-883
- https://doi.org/10.1073/pnas.59.3.876
Abstract
A nuclease purified from a RNase I minus strain of Escherichia coli (MRE-600) specifically cleaves R17 RNA at a site about 1/3[image] of the way in the molecule from the 5[image]-end. The fragment that lacks the 5[image]-end of the original molecule is still able to direct the in-vitro synthesis of the phage RNA synthetase. The results suggest that this 2[beta] fragment has impaired ability to direct synthesis of coat protein. The 1[beta] fragment from the 5[image]-end of the RNA has relatively little template activity but directs synthesis of some coat protein-like material.This publication has 18 references indexed in Scilit:
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