Results 131 to 140 of about 3,047 (148)
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Escherichiacoli mutants deficient in exoribonucleases
Biochemical and Biophysical Research Communications, 1976Abstract Strain S296, isolated by screening 2000 colonies after nitrosoguanidine mutagenesis, yields extracts with less than 1% of wild-type RNase activity against ( 3 H) poly(U). Unlike other E. coli strains, S296 grows with a doubling time of about 2 hr., both in nutrient broth and in minimal medium, and at 30°, 37° and 42°. The strain retains
N, Nikolaev, V, Folsom, D, Schlessinger
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A microsomal exoribonuclease from rat liver
Biochimica et Biophysica Acta (BBA) - Enzymology, 1979A exoribonuclease has been purified from the microsomes of rat liver. The enzyme had an apparent molecular weight of 80 000-83 000 and produced, via a processive mechanism, 5'-AMP as the only product from poly(A). The degradation was found to proceed in the 3' to 5' direction.
H, Kumagai +4 more
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Structures of 5′–3′ Exoribonucleases
20125'-3' Exoribonucleases (XRNs) have important functions in RNA processing, RNA turnover and decay, RNA interference, RNA polymerase transcription, and other cellular processes. Their sequences share two highly conserved regions, CR1 and CR2. The cytoplasmic Xrn1 and the nuclear Xrn2/Rat1 are found in yeast and animals, and XRNs are found in most other ...
Jeong Ho, Chang +2 more
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2011
The 5′-3′ exoribonucleases have important functions in RNA processing, RNA degradation, RNA interference, transcription, and other cellular processes. The Xrn1 and Xrn2/Rat1 family of enzymes are the best characterized 5′-3′ exoribonucleases, and there has been significant recent progress in the understanding of their structure and function. Especially,
Jeong Ho Chang, Song Xiang, Liang Tong
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The 5′-3′ exoribonucleases have important functions in RNA processing, RNA degradation, RNA interference, transcription, and other cellular processes. The Xrn1 and Xrn2/Rat1 family of enzymes are the best characterized 5′-3′ exoribonucleases, and there has been significant recent progress in the understanding of their structure and function. Especially,
Jeong Ho Chang, Song Xiang, Liang Tong
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2001
Publisher Summary The detection, purification, and partial characterization of 5′-exoribonuclease 1 (Xrn1) from Saccharomyces cerevisiae as a 160-kDa RNase was reported in 1980 and 1985. The enzyme is a processive exonuclease hydrolyzing RNA from the 5′ end with the production of 5′-mononucleofides.
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Publisher Summary The detection, purification, and partial characterization of 5′-exoribonuclease 1 (Xrn1) from Saccharomyces cerevisiae as a 160-kDa RNase was reported in 1980 and 1985. The enzyme is a processive exonuclease hydrolyzing RNA from the 5′ end with the production of 5′-mononucleofides.
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A cytoplasmic exoribonuclease from HeLa cells
Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1977An exoribonuclease has been purified from the cytoplasm of HeLa cells. The enzyme produces 5'-AMP as the only product from poly(A). The degradation proceeds in a 3' to 5' direction, and a 3'-OH terminus is required. In addition to poly(A), the enzyme degrades other synthetic homopolymers as well as natural messenger, and ribosomal RNAs.
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An exoribonuclease in bovine brain
Brain Research, 1975An exonuclease which degrades RNA to yield 3′-mononucleotides has been purified 300-fold from an acetone powder of bovine brain white matter. The enzyme preparation does not contain detectable quantities of RNase A, DNase, 2′,3′-cyclic phosphodiesterase, 5′-nucleotidase, and acid and alkaline phosphatase activities and requires sulfhydryl compounds for
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Structural basis of exoribonuclease-mediated mRNA transcription termination
NatureEfficient termination is required for robust gene transcription. Eukaryotic organisms use a conserved exoribonuclease-mediated mechanism to terminate the mRNA transcription by RNA polymerase II (Pol II)1-5. Here we report two cryogenic electron microscopy structures of Saccharomyces cerevisiae Pol II pre-termination transcription complexes bound to the
Yuan Zeng +3 more
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Exoribonucleases and their multiple roles in RNA metabolism
2000In recent years there has been a dramatic shift in our thinking about ribonucleases (RNases). Although they were once considered to be nonspecific, degradative enzymes, it is now clear that RNases play a central role in every aspect of cellular RNA metabolism, including decay of mRNA, conversion of RNA precursors to their mature forms, and end-turnover
M P, Deutscher, Z, Li
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Exoribonuclease Activity of Purified Reverse Transcriptase Preparations from Retroviruses
The Journal of Biochemistry, 1989Highly purified and commercially available preparations of reverse transcriptases from retroviruses contain a 3' to 5' exoribonuclease activity capable of hydrolyzing synthetic homopolyribonucleotides having a 3'-OH end. The exoribonuclease activity of reverse transcriptase preparations from Rous associated virus-2 was further characterized.
Y, Kikuchi +3 more
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