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
semanticscholar +5 more sources
pH Dependence of the RNase T1 Action on Nucleoside 2′ 3′-Cyclic Phosphates [PDF]
The Journal of Biochemistry, 1970 Shinkichi Irie +3 more
semanticscholar +5 more sources
Sinorhizobium meliloti RNase III: Catalytic Features and Impact on Symbiosis
Frontiers in Genetics, 2018 Members of the ribonuclease (RNase) III family of enzymes are metal-dependent double-strand specific endoribonucleases. They are ubiquitously found and eukaryotic RNase III-like enzymes include Dicer and Drosha, involved in RNA processing and RNA ...
Margarida Saramago +4 more
doaj +2 more sources
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
doaj +2 more sources
Identification of the Acidification Mechanism of the Optimal pH for RNase He1
Biological and Pharmaceutical Bulletin, 2023 Ribonuclease (RNase) He1 is a small ribonuclease belonging to the RNase T1 family. Most of the RNase T1 family members are active at neutral pH, except for RNase Ms, U2, and He1, which function at an acidic pH. We crystallized and analyzed the structure of RNase He1 and elucidated how the acidic amino residues of the α1β3- (He1:26-33) and β67-loops ...
Katsuki Takebe +7 more
openalex +4 more sources
Implication of RNases PH in Turnover of M1 RNA [PDF]
Bulletin of the Korean Chemical Society, 2010 Figure 1. Effects on sequestration of C5 protein on M1 RNA stability in endoribonuclease-deficient cells. Total cellular RNA was isolated from strains GW10 (wild type), GW11 (rng‒), and GW20 (rne) containing plasmids at the indicated times after the rifampicin treatment. Each RNA sample (30 μg) was fractionated on a 5% polyacrylamide gel containing 7 M
Yool Kim +4 more
openalex +5 more sources
pH-Sensitive carboxymethyl chitosan-modified cationic liposomes for sorafenib and siRNA co-delivery
International Journal of Nanomedicine, 2015 Yao Yao, Zhihui Su, Yanchao Liang, Na Zhang School of Pharmaceutical Sciences, Shandong University, Jinan, Shandong, People’s Republic of China Abstract: Combination of chemotherapeutic drug and small interfering RNA (siRNA) can affect multiple ...
Yao Y, Su ZH, Liang YC, Zhang N
doaj +2 more sources
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
openalex +3 more sources
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
doaj +1 more source
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
doaj +1 more source