Showing papers by "Murray P. Deutscher published in 1981"

TL;DR: Study of the mode of action of RNase D indicates that it is an exonuclease which initiates hydrolysis at the 3'-terminus and removes 5'-mononucleotides in a random fashion, and the relation of these properties to its possible role as a processing nuclease is discussed.

TL;DR: RNase D, a putative tRNa processing nuclease, has been purified about 1,000-fold from extracts of Escherichia coli to apparent homogeneity, as judged by acrylamide gel electrophoresis under nondenaturing and denaturing conditions and by gel electrofocusing.

TL;DR: Preliminary analysis indicates that the factor in infected cell extracts responsible for the conversion is a heat-labile, relatively low-molecular weight protein, and that RNase D is modified by association with this phage-specific component.