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
Mechanism of action of RNase T. I. Identification of residues required for catalysis, substrate binding, and dimerization.
Yuhong Zuo,Murray P. Deutscher +1 more
TL;DR: Analysis of Escherichia coli RNase T found three conserved Exo motifs that included four invariant acidic residues that probably form the RNaseT catalytic center in a manner similar to that found in other DEDD exonucleases.
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Escherichia coli rna gene encoding RNase I: cloning, overexpression, subcellular distribution of the enzyme, and use of an rna deletion to identify additional RNases.
TL;DR: In this article, the cloning and overexpression of the Escherichia coli rna gene encoding RNase I were described, and the rna clone was used to identify a deletion strain totally lacking the Rna gene.
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A Novel Mechanism for Ribonuclease Regulation TRANSFER-MESSENGER RNA (tmRNA) AND ITS ASSOCIATED PROTEIN SmpB REGULATE THE STABILITY OF RNase R
TL;DR: A previously unknown regulatory process in which the stability of an RNase is determined by its interaction with an RNA and an RNA-associated protein is defined.
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How RNase R Degrades Structured RNA: ROLE OF THE HELICASE ACTIVITY AND THE S1 DOMAIN *
TL;DR: A detailed model is developed that explains how RNase R digests structured RNA and how this differs from its action on single-stranded RNA.
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Reactions at the 3′ Terminus of Transfer Ribonucleic Acid: IV. EXTENTS OF NORMAL AND ANOMALOUS NUCLEOTIDE INCORPORATION CATALYZED BY TRANSFER RIBONUCLEIC ACID NUCLEOTIDYLTRANSFERASE
TL;DR: Evidence is presented that apparently homogeneous preparations of tRNA nucleotidyltransferase contain a poly(C) polymerase activity which utilized as substrates intact tRNA, rRNA, and tRNAs without complete termini, suggesting that contamination of the enzyme preparation was probably not involved.