Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.26.3 (RNase III)
 1,015 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The ribonuclease III Dicer (Dcr1) has been shown to be required for chromosome segregation and gene silencing in Schizosaccharomyces pombe. These effects are thought to be transcriptional, mediated by formation and maintenance of heterochromatin, and guided by small RNAs derived from Dcr1 along a process known as RNA interference. In order to get further insights into the gene regulatory role of Dcr1, we performed comparative analyses of dcr1 knockout and wild-type fission yeast strains. Analysis of part of the soluble proteomes identified eight cellular proteins whose expression is under Dcr1 control, three of which are integral constituents of the glycolysis pathway. Further correlations with their respective mRNA transcript levels are compatible with the existence of a post-transcriptional gene regulatory mechanism involving Dcr1 or a Dcr1 complex. Experiments designed to identify components of Dcr1 complexes unveiled two novel Dcr1 interactors, namely the zinc finger protein Byr3 and the ribosomal protein L12. Consistently enriched in Dcr1 immune complexes, Byr3 and L12 may link Dcr1 to the transcriptional and translational machineries, respectively, and contribute to post-transcriptional gene regulation in fission yeast.
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PMID:Involvement of Dcr1 in post-transcriptional regulation of gene expression in Schizosaccharomyces pombe. 1798 3

Plant microRNAs (miRNAs) are processed by the RNase III-like enzyme DICER-LIKE1 acting in concert with the double-stranded RNA-binding protein HYPONASTIC LEAVES1 and the zinc finger protein SERRATE. Together, they excise a miRNA/miRNA( *) duplex with a 2 nucleotide 3' overhang from the primary miRNA (pri-miRNA) transcript. pri-miRNAs include a partially self-complementary foldback or stem loop, which gives rise to the mature miRNA. In animals, pri-miRNAs are very similar, with a stereotypic position of the miRNA within the foldback. Accordingly, rules for miRNA excision from the precursor are quite simple in animals. In contrast, how miRNA sequences are recognized in the structurally much more diverse foldbacks of plants is unknown. We have performed an extensive in vivo structure-function analysis of Arabidopsis thaliana pri-miRNA 172a (pri-miR172a). A junction of single-stranded and double-stranded RNA 15 nucleotides proximal from the miRNA/miRNA(*) duplex appears to be essential for accurate miR172a processing. This attribute is found in several other but not all plant miRNA foldbacks. In addition, we have identified features of the distal foldback structure important for miR172a processing. Our ability to engineer de novo a functional minimal miRNA precursor highlights that we have discovered several elements both necessary and sufficient for accurate miRNA processing.
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PMID:Structure determinants for accurate processing of miR172a in Arabidopsis thaliana. 2001 54

Mitochondrial mRNA editing in trypanosomatid parasites involves several multiprotein assemblies, including three very similar complexes that contain the key enzymatic editing activities and sediment at ~20S on glycerol gradients. These ~20S editosomes have a common set of 12 proteins, including enzymes for uridylyl (U) removal and addition, 2 RNA ligases, 2 proteins with RNase III-like domains, and 6 proteins with predicted oligonucleotide binding (OB) folds. In addition, each of the 3 distinct ~20S editosomes contains a different RNase III-type endonuclease, 1 of 3 related proteins and, in one case, an additional exonuclease. Here we present a protein-protein interaction map that was obtained through a combination of yeast two-hybrid analysis and subcomplex reconstitution with recombinant protein. This map interlinks ten of the proteins and in several cases localizes the protein region mediating the interaction, which often includes the predicted OB-fold domain. The results indicate that the OB-fold proteins form an extensive protein-protein interaction network that connects the two trimeric subcomplexes that catalyze U removal or addition and RNA ligation. One of these proteins, KREPA6, interacts with the OB-fold zinc finger protein in each subcomplex that interconnects their two catalytic proteins. Another OB-fold protein, KREPA3, appears to link to the putative endonuclease subcomplex. These results reveal a physical organization that underlies the coordination of the various catalytic and substrate binding activities within the ~20S editosomes during the editing process.
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PMID:A protein-protein interaction map of trypanosome ~20S editosomes. 2001 60