Protein component of the ribozyme ribonuclease P alters substrate recognition by directly contacting precursor tRNA
about
Essential roles of Bdp1, a subunit of RNA polymerase III initiation factor TFIIIB, in transcription and tRNA processing.Archaeal RNase P has multiple protein subunits homologous to eukaryotic nuclear RNase P proteinsStructure of a bacterial ribonuclease P holoenzyme in complex with tRNACrystal structure of the phosphorolytic exoribonuclease RNase PH from Bacillus subtilis and implications for its quaternary structure and tRNA bindingRNase P RNAs from some Archaea are catalytically activeFunctional reconstitution and characterization of Pyrococcus furiosus RNase PRNase P: role of distinct protein cofactors in tRNA substrate recognition and RNA-based catalysis.The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological FunctionsSequence Analysis and Comparative Study of the Protein Subunits of Archaeal RNase PHigh-resolution structure of RNase P protein from Thermotoga maritimaStructure of Mth11/Mth Rpp29, an essential protein subunit of archaeal and eukaryotic RNase PLigand concentration regulates the pathways of coupled protein folding and binding.Genome-wide search for yeast RNase P substrates reveals role in maturation of intron-encoded box C/D small nucleolar RNAs.Interactions among the protein and RNA subunits of Saccharomyces cerevisiae nuclear RNase PFunctional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRPEukaryotic ribonuclease P: a plurality of ribonucleoprotein enzymesThe Bacillus subtilis RNase P holoenzyme contains two RNase P RNA and two RNase P protein subunits.Ribonuclease P: the evolution of an ancient RNA enzyme.Site-specific modification and RNA crosslinking of the RNA-binding domain of PKR.Protein-precursor tRNA contact leads to sequence-specific recognition of 5' leaders by bacterial ribonuclease PBacterial ribonuclease P holoenzyme crosslinking analysis reveals protein interaction sites on the RNA subunitOf proteins and RNA: the RNase P/MRP family.A divalent cation stabilizes the active conformation of the B. subtilis RNase P x pre-tRNA complex: a role for an inner-sphere metal ion in RNase P.Eukaryotic ribonuclease P: increased complexity to cope with the nuclear pre-tRNA pathway.Structure of Pfu Pop5, an archaeal RNase P protein.Multiple binding modes of substrate to the catalytic RNA subunit of RNase P from Escherichia coli.The 3' substrate determinants for the catalytic efficiency of the Bacillus subtilis RNase P holoenzyme suggest autolytic processing of the RNase P RNA in vivo.Specific phosphorothioate substitutions probe the active site of Bacillus subtilis ribonuclease P.Recognition of the 5' leader of pre-tRNA substrates by the active site of ribonuclease P.Ionic interactions between PRNA and P protein in Bacillus subtilis RNase P characterized using a magnetocapture-based assayElucidation of structure-function relationships in the protein subunit of bacterial RNase P using a genetic complementation approachDissecting functional cooperation among protein subunits in archaeal RNase P, a catalytic ribonucleoprotein complex.A real-time fluorescence polarization activity assay to screen for inhibitors of bacterial ribonuclease PEvidence for recycling of external guide sequences during cleavage of bipartite substrates in vitro by reconstituted archaeal RNase P.Cleavage of model substrates by archaeal RNase P: role of protein cofactors in cleavage-site selectionThe L7Ae protein binds to two kink-turns in the Pyrococcus furiosus RNase P RNA.Probing the folding intermediate of Bacillus subtilis RNase P protein by nuclear magnetic resonance.The RNR motif of B. subtilis RNase P protein interacts with both PRNA and pre-tRNA to stabilize an active conformer.Assembly of the complex between archaeal RNase P proteins RPP30 and Pop5Probing the architecture of the B. subtilis RNase P holoenzyme active site by cross-linking and affinity cleavage
P2860
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P2860
Protein component of the ribozyme ribonuclease P alters substrate recognition by directly contacting precursor tRNA
description
1998 nî lūn-bûn
@nan
1998 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Protein component of the riboz ...... ctly contacting precursor tRNA
@ast
Protein component of the riboz ...... ctly contacting precursor tRNA
@en
Protein component of the riboz ...... tly contacting precursor tRNA.
@nl
type
label
Protein component of the riboz ...... ctly contacting precursor tRNA
@ast
Protein component of the riboz ...... ctly contacting precursor tRNA
@en
Protein component of the riboz ...... tly contacting precursor tRNA.
@nl
prefLabel
Protein component of the riboz ...... ctly contacting precursor tRNA
@ast
Protein component of the riboz ...... ctly contacting precursor tRNA
@en
Protein component of the riboz ...... tly contacting precursor tRNA.
@nl
P2093
P2860
P356
P1476
Protein component of the riboz ...... ctly contacting precursor tRNA
@en
P2093
C A Fierke
D W Christianson
S Niranjanakumari
P2860
P304
15212-15217
P356
10.1073/PNAS.95.26.15212
P407
P577
1998-12-01T00:00:00Z