Results 231 to 240 of about 6,830 (257)
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Arabidopsis mRNA decay landscape shaped by XRN 5'-3' exoribonucleases.
The Plant Journal, 20235'-3' exoribonucleases (XRNs) play crucial roles in the control of RNA processing, quality, and quantity in eukaryotes. Although genome-wide profiling of RNA decay fragments is now feasible, how XRNs shape the plant mRNA degradome remains elusive.
Wan-Yin Han +5 more
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Decay of Piwi-Interacting RNAs in Human Cells Is Primarily Mediated by 5' to 3' Exoribonucleases.
ACS Chemical Biology, 2022Piwi-interacting RNAs (piRNAs) are a group of small noncoding RNA molecules that regulate the activity of transposons and control gene expression. The cellular concentration of RNAs is generally maintained by their rates of biogenesis and degradation ...
Sumirtha Balaratnam +3 more
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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
Virginia Folsom +2 more
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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.
Kazuei Igarashi +4 more
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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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Drosophila 5′ → 3′-Exoribonuclease Pacman
2001Publisher Summary This chapter concentrates on the methods used to express a Drosophila recombinat 5′ → 3′-exoribonuclease, purify the protein, and analyze its activity in vitro . Analysis of early development in Drosophila has shown that RNA localization, control of translation, and mRNA stability are intimately linked.
Sarah F. Newbury +2 more
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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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Cooperation of Endo- and Exoribonucleases in Chloroplast mRNA Turnover
2004Chloroplasts were acquired by eukaryotic cells through endosymbiosis and have retained their own gene expression machinery. One hallmark of chloroplast gene regulation is the predominance of posttranscriptional control, which is exerted both at the gene-specific and global levels.
Thomas J. Bollenbach +2 more
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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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Function and Characterization of Poly(A)-Specific 3´ Exoribonucleases
1997Poly(A) tails are commonly found at the 3´ end of various classes of RNA (reviewed in Brawerman 1981; Manley 1995b). They are evolutionarily widespread and appear on RNAs of several different organisms. In mammalian cells almost all mRNAs end with an approximately 200-adenosine-residue-long poly(A) tail.
Jonas Åström, Anders Virtanen
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