Crystal structure of the phosphorolytic exoribonuclease RNase PH from Bacillus subtilis and implications for its quaternary structure and tRNA binding [PDF]
Protein Science, 2004 AbstractRNase PH is a member of the family of phosphorolytic 3′ → 5′ exoribonucleases that also includes polynucleotide phosphorylase (PNPase). RNase PH is involved in the maturation of tRNA precursors and especially important for removal of nucleotide residues near the CCA acceptor end of the mature tRNAs.
Lene S. Harlow +3 more
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Critical functions and key interactions mediated by the RNase E scaffolding domain in Pseudomonas aeruginosa. [PDF]
PLoS GeneticsThe RNA degradosome is a bacterial multi-protein complex mediating mRNA processing and degradation. In Pseudomonadota, this complex assembles on the C-terminal domain (CTD) of RNase E through short linear motifs (SLiMs) that determine its composition and
Sandra Amandine Marie Geslain +5 more
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Identification of the rph (RNase PH) gene of Bacillus subtilis: evidence for suppression of cold-sensitive mutations in Escherichia coli [PDF]
Journal of Bacteriology, 1992 A shotgun cloning of Bacillus subtilis DNA into pBR322 yielded a 2-kb fragment that suppresses the cold-sensitive defect of the nusA10(Cs) Escherichia coli mutant. The responsible gene encodes an open reading frame that is greater than 50% identical at the amino acid level to the E. coli rph gene, which was formerly called orfE. This B.
M G Craven +6 more
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Protein–Protein Interactions between Human Exosome Components Support the Assembly of RNase PH-type Subunits into a Six-membered PNPase-like Ring [PDF]
Journal of Molecular Biology, 2002 The exosome is a complex of 3'-->5' exoribonucleases, which functions in a variety of cellular processes, all requiring the processing or degradation of RNA. Here we present a model for the assembly of the six human RNase PH-like exosome subunits into a hexameric ring structure.
Reinout Raijmakers +3 more
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Crystal structure of a bacterial tRNA-precursor processing enzyme: RNase PH fromBacillus subtilis [PDF]
Acta Crystallographica Section A Foundations of Crystallography, 2002 Anders Kadziola +3 more
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pH Dependence of the RNase T1 Action on Nucleoside 2′ 3′-Cyclic Phosphates [PDF]
The Journal of Biochemistry, 1970 Shinkichi Irie +3 more
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Structure-guided design of endosomolytic chloroquine-like lipid nanoparticles for mRNA delivery and genome editing [PDF]
Nature CommunicationsDespite remarkable progress in designing RNA delivery systems, endosomal escape remains a recognized challenge for efficient RNA delivery. In this study, we develop a robust mRNA delivery platform termed endosomolytic chloroquine-like optimized lipid ...
Zhen Liu +6 more
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mBio, 2022 The Bacillus subtilis genome encodes four 3′ exoribonucleases: polynucleotide phosphorylase (PNPase), RNase R, RNase PH, and YhaM. Previous work showed that PNPase, encoded by the pnpA gene, is the major 3′ exonuclease involved in mRNA turnover; in a ...
Shivani Chhabra +4 more
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RNase 7 contributes to the cutaneous defense against Enterococcus faecium. [PDF]
PLoS ONE, 2009 BackgroundHuman skin is able to mount a fast response against invading microorganisms by the release of antimicrobial proteins such as the ribonuclease RNase 7. Because RNase 7 exhibits high activity against Enterococcus faecium the aim of this study was
Bente Köten +5 more
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Phylogenetic analyses and characterization of RNase X25 from Drosophila melanogaster suggest a conserved housekeeping role and additional functions for RNase T2 enzymes in protostomes. [PDF]
PLoS ONE, 2014 Ribonucleases belonging to the RNase T2 family are enzymes associated with the secretory pathway that are almost absolutely conserved in all eukaryotes.
Linda Ambrosio +5 more
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