Mitochondrial ribonuclease P structure provides insight into the evolution of catalytic strategies for precursor-tRNA 5' processing
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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 FunctionsStructure of a PLS-class Pentatricopeptide Repeat Protein Provides Insights into Mechanism of RNA RecognitionStructural basis for the modular recognition of single-stranded RNA by PPR proteinsStructural basis for RNA recognition by a dimeric PPR-protein complexAn artificial PPR scaffold for programmable RNA recognitionThe design and structural characterization of a synthetic pentatricopeptide repeat proteinThe Pet309 pentatricopeptide repeat motifs mediate efficient binding to the mitochondrial COX1 transcript in yeast.Structure of the nuclease subunit of human mitochondrial RNase PUse of chemical modification and mass spectrometry to identify substrate-contacting sites in proteinaceous RNase P, a tRNA processing enzymeRedefining the structural motifs that determine RNA binding and RNA editing by pentatricopeptide repeat proteins in land plants.The Schizosaccharomyces pombe PPR protein Ppr10 associates with a novel protein Mpa1 and acts as a mitochondrial translational activator.The pentatricopeptide repeat protein MTSF2 stabilizes a nad1 precursor transcript and defines the 3΄ end of its 5΄-half intron.Comprehensive classification of the PIN domain-like superfamilyElucidation of the RNA recognition code for pentatricopeptide repeat proteins involved in organelle RNA editing in plants.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.Uses of phage display in agriculture: sequence analysis and comparative modeling of late embryogenesis abundant client proteins suggest protein-nucleic acid binding functionality.Auto-inhibitory Mechanism of the Human Mitochondrial RNase P Protein Complex.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.Cleavage of Model Substrates by Arabidopsis thaliana PRORP1 Reveals New Insights into Its Substrate RequirementsNuclear 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.De-coding and re-coding RNA recognition by PUF and PPR repeat proteins.Differential substrate recognition by isozymes of plant protein-only Ribonuclease PStructural basis for specific single-stranded RNA recognition by designer pentatricopeptide repeat proteinsPentatricopeptide repeats: modular blocks for building RNA-binding proteins.PPR proteins shed a new light on RNase P biology.Yeast PPR proteins, watchdogs of mitochondrial gene expression.Small RNAs reveal two target sites of the RNA-maturation factor Mbb1 in the chloroplast of ChlamydomonasHuman pentatricopeptide proteins: only a few and what do they do?Nucleic acid catalysis: metals, nucleobases, and other cofactors.Structural mechanisms of RNA recognition: sequence-specific and non-specific RNA-binding proteins and the Cas9-RNA-DNA complex.Engineering reprogrammable RNA-binding proteins for study and manipulation of the transcriptome.Biophysical analysis of Arabidopsis protein-only RNase P alone and in complex with tRNA provides a refined model of tRNA binding.Substrate recognition and cleavage-site selection by a single-subunit protein-only RNase P.Structural conservation of the PIN domain active site across all domains of life.Crystallization and crystallographic analysis of an Arabidopsis nuclear proteinaceous RNase P.Function of PPR proteins in plastid gene expression.
P2860
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P2860
Mitochondrial ribonuclease P structure provides insight into the evolution of catalytic strategies for precursor-tRNA 5' processing
description
2012 nî lūn-bûn
@nan
2012 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հոտեմբերին 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
Mitochondrial ribonuclease P s ...... r precursor-tRNA 5' processing
@ast
Mitochondrial ribonuclease P s ...... r precursor-tRNA 5' processing
@en
Mitochondrial ribonuclease P s ...... r precursor-tRNA 5' processing
@nl
type
label
Mitochondrial ribonuclease P s ...... r precursor-tRNA 5' processing
@ast
Mitochondrial ribonuclease P s ...... r precursor-tRNA 5' processing
@en
Mitochondrial ribonuclease P s ...... r precursor-tRNA 5' processing
@nl
prefLabel
Mitochondrial ribonuclease P s ...... r precursor-tRNA 5' processing
@ast
Mitochondrial ribonuclease P s ...... r precursor-tRNA 5' processing
@en
Mitochondrial ribonuclease P s ...... r precursor-tRNA 5' processing
@nl
P2093
P2860
P3181
P356
P1476
Mitochondrial ribonuclease P s ...... r precursor-tRNA 5' processing
@en
P2093
Carol A Fierke
Michael J Howard
Wan Hsin Lim
P2860
P304
16149-16154
P3181
P356
10.1073/PNAS.1209062109
P407
P577
2012-09-18T00:00:00Z