PRORP proteins support RNase P activity in both organelles and the nucleus in Arabidopsis
about
Mechanistic and Structural Studies of Protein-Only RNase P Compared to Ribonucleoproteins Reveal the Two Faces of the Same Enzymatic ActivityThe Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological FunctionsMultiple Layers of Stress-Induced Regulation in tRNA BiologyAntibiotics and RNase PTransfer RNA post-transcriptional processing, turnover, and subcellular dynamics in the yeast Saccharomyces cerevisiaeP-class pentatricopeptide repeat proteins are required for efficient 5' end formation of plant mitochondrial transcriptsTranscriptional control of an essential ribozyme in Drosophila reveals an ancient evolutionary divide in animalsMitochondrial ribonuclease P structure provides insight into the evolution of catalytic strategies for precursor-tRNA 5' processingConserved regions of ribonucleoprotein ribonuclease MRP are involved in interactions with its substratetRNA biology in mitochondriaA subcomplex of human mitochondrial RNase P is a bifunctional methyltransferase--extensive moonlighting in mitochondrial tRNA biogenesisStructure of the nuclease subunit of human mitochondrial RNase PPlaying RNase P evolution: swapping the RNA catalyst for a protein reveals functional uniformity of highly divergent enzyme formsThe natural history of transfer RNA and its interactions with the ribosomeUse of chemical modification and mass spectrometry to identify substrate-contacting sites in proteinaceous RNase P, a tRNA processing enzymeRNase P branches out from RNP to protein: organelle-triggered diversification?Systematic study of subcellular localization of Arabidopsis PPR proteins confirms a massive targeting to organelles.Molecular characterization of three PRORP proteins in the moss Physcomitrella patens: nuclear PRORP protein is not essential for moss viability.A real-time fluorescence polarization activity assay to screen for inhibitors of bacterial ribonuclease PThe amyloid-β-SDR5C1(ABAD) interaction does not mediate a specific inhibition of mitochondrial RNase P.Small stable RNA maturation and turnover in Bacillus subtilis.Boosting CRISPR/Cas9 multiplex editing capability with the endogenous tRNA-processing system.Multiple RNA processing defects and impaired chloroplast function in plants deficient in the organellar protein-only RNase P enzyme.Mechanistic Studies Reveal Similar Catalytic Strategies for Phosphodiester Bond Hydrolysis by Protein-only and RNA-dependent Ribonuclease PInfluence of Conformation of M. tuberculosis RNase P Protein Subunit on Its Function.The sRNAome mining revealed existence of unique signature small RNAs derived from 5.8SrRNA from Piper nigrum and other plant lineagesNonsense-mediated mRNA decay in Tetrahymena is EJC independent and requires a protozoa-specific nucleaseNuclear Protein-Only Ribonuclease P2 Structure and Biochemical Characterization Provide Insight into the Conserved Properties of tRNA 5' End Processing Enzymes.Structural insights into protein-only RNase P complexed with tRNA.Differential substrate recognition by isozymes of plant protein-only Ribonuclease PNuclear RNase P of Trypanosoma brucei: a single protein in place of the multicomponent RNA-protein complex.Pentatricopeptide repeats: modular blocks for building RNA-binding proteins.PPR proteins shed a new light on RNase P biology.RNA processing and decay in plastids.The translational apparatus of plastids and its role in plant developmentRNase P-Mediated Sequence-Specific Cleavage of RNA by Engineered External Guide SequencesBiophysical analysis of Arabidopsis protein-only RNase P alone and in complex with tRNA provides a refined model of tRNA binding.Maturation of 5' ends of plant mitochondrial RNAs.Substrate recognition and cleavage-site selection by a single-subunit protein-only RNase P.Comparison of preribosomal RNA processing pathways in yeast, plant and human cells - focus on coordinated action of endo- and exoribonucleases.
P2860
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P2860
PRORP proteins support RNase P activity in both organelles and the nucleus in Arabidopsis
description
2012 nî lūn-bûn
@nan
2012 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
PRORP proteins support RNase P activity in both organelles and the nucleus in Arabidopsis
@ast
PRORP proteins support RNase P activity in both organelles and the nucleus in Arabidopsis
@en
PRORP proteins support RNase P activity in both organelles and the nucleus in Arabidopsis
@nl
type
label
PRORP proteins support RNase P activity in both organelles and the nucleus in Arabidopsis
@ast
PRORP proteins support RNase P activity in both organelles and the nucleus in Arabidopsis
@en
PRORP proteins support RNase P activity in both organelles and the nucleus in Arabidopsis
@nl
prefLabel
PRORP proteins support RNase P activity in both organelles and the nucleus in Arabidopsis
@ast
PRORP proteins support RNase P activity in both organelles and the nucleus in Arabidopsis
@en
PRORP proteins support RNase P activity in both organelles and the nucleus in Arabidopsis
@nl
P2860
P356
P1433
P1476
PRORP proteins support RNase P activity in both organelles and the nucleus in Arabidopsis
@en
P2093
Bernard Gutmann
P2860
P304
P356
10.1101/GAD.189514.112
P577
2012-05-01T00:00:00Z