Mechanism of Ribonuclease III Catalytic Regulation by Serine Phosphorylation. [PDF]
Sci Rep, 2016 AbstractRibonuclease III (RNase III) is a conserved, gene-regulatory bacterial endonuclease that cleaves double-helical structures in diverse coding and noncoding RNAs. RNase III is subject to multiple levels of control, reflective of its global regulatory functions.
Gone S +3 more
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Mechanistic basis for selective Csm6-2 activation by cyclic penta-adenylate in a type III CRISPR-Cas system [PDF]
The EMBO JournalType III CRISPR systems generate cyclic oligoadenylate (cOA, 3 to 6 AMPs) messengers upon detecting viral RNA, activating downstream effectors to defend against viral infection.
Ruyi Shi +4 more
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The production of extracellular proteins is regulated by ribonuclease III via two different pathways in Staphylococcus aureus. [PDF]
PLoS ONE, 2011 Staphylococcus aureus ribonuclease III belongs to the enzyme family known to degrade double-stranded RNAs. It has previously been reported that RNase III cannot influence cell growth but regulates virulence gene expression in S. aureus.
Yu Liu +8 more
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Ribonuclease III mechanisms of double-stranded RNA cleavage. [PDF]
Wiley Interdiscip Rev RNA, 2014 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.
Nicholson AW.
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Ribonuclease III is involved in motility of Escherichia coli [PDF]
Journal of Bacteriology, 1978 Mutants of Escherichia coli deficient in ribonuclease III are nonmotile. All transductants and revertants that regained ribonuclease III also regained motility, and all transductants that remained or became rnc are nonmotile, although only some of the revertants that regained motility also became ribonuclease III+.
D Apirion
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Noncatalytic Assembly of Ribonuclease III with Double-Stranded RNA [PDF]
Structure, 2004 Ribonuclease III (RNase III) represents a family of double-stranded RNA (dsRNA) endonucleases. The simplest bacterial enzyme contains an endonuclease domain (endoND) and a dsRNA binding domain (dsRBD). RNase III can affect RNA structure and gene expression in either of two ways: as a dsRNA-processing enzyme that cleaves dsRNA, or as a dsRNA binding ...
Xinhua Ji, Jianhua Gan, David S Waugh
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Characterization of a chlorella virus PBCV-1 encoded ribonuclease III
Virology, 2003 Sequence analysis of the 330-kb genome of chlorella virus PBCV-1 revealed an open reading frame, A464R, which encodes a protein with 30-35% amino acid identity to ribonuclease III (RNase III) from many bacteria. The a464r gene was cloned and the protein was expressed in Escherichia coli using the chitin-binding intein system.
Irina Calin-Jageman +2 more
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Biocomputational Characterization and Evolutionary Analysis of Bubaline Dicer1 Enzyme [PDF]
Asian-Australasian Journal of Animal Sciences, 2015 Dicer, an ribonuclease type III type endonuclease, is the key enzyme involved in biogenesis of microRNAs (miRNAs) and small interfering RNAs (siRNAs), and thus plays a critical role in RNA interference through post transcriptional regulation of gene ...
Jasdeep Singh +3 more
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Structural characterization of a ribonuclease III processing signal [PDF]
Nucleic Acids Research, 1994 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.
D C, Schweisguth +3 more
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Two tandem RNase III cleavage sites determine betT mRNA stability in response to osmotic stress in Escherichia coli. [PDF]
PLoS ONE, 2014 While identifying genes regulated by ribonuclease III (RNase III) in Escherichia coli, we observed that steady-state levels of betT mRNA, which encodes a transporter mediating the influx of choline, are dependent on cellular concentrations of RNase III ...
Minji Sim +6 more
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