Ruler-based mechanisms of ribonuclease III enzymes
نویسندگان
چکیده
منابع مشابه
Ribonuclease revisited: structural insights into ribonuclease III family enzymes.
Ribonuclease III (RNase III) enzymes occur ubiquitously in biology and are responsible for processing RNA precursors into functional RNAs that participate in protein synthesis, RNA interference and a range of other cellular activities. Members of the RNase III enzyme family, including Escherichia coli RNase III, Rnt1, Dicer and Drosha, share the ability to recognize and cleave double-stranded R...
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Double-stranded(ds) RNA has diverse roles in gene expression and regulation, host defense, and genome surveillance in bacterial and eukaryotic cells. A central aspect of dsRNA function is its selective recognition and cleavage by members of the ribonuclease III (RNase III) family of divalent-metal-ion-dependent phosphodiesterases. The processing of dsRNA by RNase III family members is an essent...
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Ribonuclease P (RNase P) is an essential endonuclease that acts early in the tRNA biogenesis pathway. This enzyme catalyzes cleavage of the leader sequence of precursor tRNAs (pre-tRNAs), generating the mature 5' end of tRNAs. RNase P activities have been identified in Bacteria, Archaea, and Eucarya, as well as organelles. Most forms of RNase P are ribonucleoproteins, i.e., they consist of an e...
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The structure of a ribonuclease III processing signal from bacteriophage T7 was examined by NMR spectroscopy, optical melting, and chemical and enzymatic modification. A 41 nucleotide variant of the T7 R1.1 processing signal has two Watson-Crick base-paired helices separated by an internal loop, consistent with its predicted secondary structure. The internal loop is neither rigidly structured n...
متن کاملPurification and properties of ribonuclease III from Escherichia coli.
A nuclease with specificity for double-stranded RNA (RNase III) has been found in extracts of Escherichia coli. It remains within osmotically shocked cells attached to the ribosomes. It sediments with the ribosomes in less than 0.20 M NH&l, but is detached at higher concentrations. A purification is described which utilizes this property. The free enzyme, after diethylaminoethyl Sephadex and ca...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations and Advances
سال: 2017
ISSN: 2053-2733
DOI: 10.1107/s0108767317099949