M
Murray P. Deutscher
Researcher at University of Miami
Publications - 184
Citations - 11738
Murray P. Deutscher is an academic researcher from University of Miami. The author has contributed to research in topics: RNase P & RNase PH. The author has an hindex of 60, co-authored 184 publications receiving 11193 citations. Previous affiliations of Murray P. Deutscher include University of Connecticut Health Center & National Institute for Medical Research.
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Journal ArticleDOI
Nuclear protein synthesis: A re-evaluation
TL;DR: It is shown that isolated Chinese hamster ovary and HeLa cell nuclei are essentially inactive for translation, and that the earlier results were most likely due to cytoplasmic contamination.
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Reversible acetylation on Lys501 regulates the activity of RNase II
TL;DR: It is shown that one residue, Lys501, is acetylated in RNase II, and this modification affects binding of the substrate and thus decreases the catalytic activity of RN enzyme II, indicating that acetylation can regulate the activity of a bacterial ribonuclease.
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Reactions at the 3' terminus of transfer ribonucleic acid. 3. Catalytic properties of two purified rabbit liver transfer ribonucleic acid nucleotidyl transferases.
TL;DR: Although many of the properties of the two enzymes are quite similar, significant differences do exist, suggesting that both enzymes probably acted on the same tRNA population.
Journal ArticleDOI
Characterization of Escherichia coli RNase PH.
K O Kelly,Murray P. Deutscher +1 more
TL;DR: The OrfE protein has both the degradative and synthetic activities of RNase PH, and the equilibrium constant for RNasePH is near unity, suggesting that at the phosphate concentration present in vivo, the enzyme would participate in RNA degradation.
Journal ArticleDOI
Reactions at the 3′ Terminus of Transfer Ribonucleic Acid: II. PURIFICATION AND PHYSICAL AND CHEMICAL PROPERTIES OF RABBIT LIVER TRANSFER RIBONUCLEIC ACID NUCLEOTIDYLTRANSFERASE
TL;DR: Evidence is presented which suggests that the molecular weight change of tRNA nucleotidyltransferase was due to removal of bound tRNA, and the formation of a tight complex between the purified enzyme and tRNA was also demonstrated.