Characterization of a unique protein component of yeast RNase MRP: an RNA-binding protein with a zinc-cluster domain.
about
hPop1: an autoantigenic protein subunit shared by the human RNase P and RNase MRP ribonucleoproteinsAutoantigenic properties of some protein subunits of catalytically active complexes of human ribonuclease PRNA-protein interactions in the human RNase MRP ribonucleoprotein complex.Phylogenetic analysis of the structure of RNase MRP RNA in yeastsDifferential association of protein subunits with the human RNase MRP and RNase P complexesPurification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRPRNase MRP cleaves the CLB2 mRNA to promote cell cycle progression: novel method of mRNA degradationEukaryotic ribonucleases P/MRP: the crystal structure of the P3 domainhPop5, a protein subunit of the human RNase MRP and RNase P endoribonucleases.Interactions between subunits of Saccharomyces cerevisiae RNase MRP support a conserved eukaryotic RNase P/MRP architecture.Genome-wide search for yeast RNase P substrates reveals role in maturation of intron-encoded box C/D small nucleolar RNAs.Conserved regions of ribonucleoprotein ribonuclease MRP are involved in interactions with its substrateGlobal identification of new substrates for the yeast endoribonuclease, RNase mitochondrial RNA processing (MRP)Dbp3p, a putative RNA helicase in Saccharomyces cerevisiae, is required for efficient pre-rRNA processing predominantly at site A3.Gar1p binds to the small nucleolar RNAs snR10 and snR30 in vitro through a nontypical RNA binding element.Mutagenesis of SNM1, which encodes a protein component of the yeast RNase MRP, reveals a role for this ribonucleoprotein endoribonuclease in plasmid segregation.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 enzymesStreptavidin aptamers: affinity tags for the study of RNAs and ribonucleoproteinsProtein trans-acting factors involved in ribosome biogenesis in Saccharomyces cerevisiaeRibonuclease P: the evolution of an ancient RNA enzyme.Crystallization and preliminary X-ray diffraction analysis of the P3 RNA domain of yeast ribonuclease MRP in a complex with RNase P/MRP protein components Pop6 and Pop7.Comparison of mitochondrial and nucleolar RNase MRP reveals identical RNA components with distinct enzymatic activities and protein componentsLithium toxicity in yeast is due to the inhibition of RNA processing enzymes.Of proteins and RNA: the RNase P/MRP family.Eukaryotic ribonuclease P: increased complexity to cope with the nuclear pre-tRNA pathway.GAMETOPHYTE DEFECTIVE 1, a putative subunit of RNases P/MRP, is essential for female gametogenesis and male competence in Arabidopsis.Functional equivalence of hairpins in the RNA subunits of RNase MRP and RNase P in Saccharomyces cerevisiaeAn active precursor in assembly of yeast nuclear ribonuclease P.Characterization of conserved sequence elements in eukaryotic RNase P RNA reveals roles in holoenzyme assembly and tRNA processingRNase MRP cleaves pre-tRNASer-Met in the tRNA maturation pathway.A functional dominant mutation in Schizosaccharomyces pombe RNase MRP RNA affects nuclear RNA processing and requires the mitochondrial-associated nuclear mutation ptp1-1 for viabilitySpecific binding of a Pop6/Pop7 heterodimer to the P3 stem of the yeast RNase MRP and RNase P RNAsA specialized processing body that is temporally and asymmetrically regulated during the cell cycle in Saccharomyces cerevisiaeFootprinting analysis demonstrates extensive similarity between eukaryotic RNase P and RNase MRP holoenzymes.Identification of a functional core in the RNA component of RNase MRP of budding yeastsRNase P: increased versatility through protein complexity?Inventory and analysis of the protein subunits of the ribonucleases P and MRP provides further evidence of homology between the yeast and human enzymes.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
Characterization of a unique protein component of yeast RNase MRP: an RNA-binding protein with a zinc-cluster domain.
description
1994 nî lūn-bûn
@nan
1994 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Characterization of a unique p ...... in with a zinc-cluster domain.
@ast
Characterization of a unique p ...... in with a zinc-cluster domain.
@en
Characterization of a unique p ...... in with a zinc-cluster domain.
@nl
type
label
Characterization of a unique p ...... in with a zinc-cluster domain.
@ast
Characterization of a unique p ...... in with a zinc-cluster domain.
@en
Characterization of a unique p ...... in with a zinc-cluster domain.
@nl
prefLabel
Characterization of a unique p ...... in with a zinc-cluster domain.
@ast
Characterization of a unique p ...... in with a zinc-cluster domain.
@en
Characterization of a unique p ...... in with a zinc-cluster domain.
@nl
P2860
P356
P1433
P1476
Characterization of a unique p ...... in with a zinc-cluster domain.
@en
P2093
D A Clayton
M E Schmitt
P2860
P304
P356
10.1101/GAD.8.21.2617
P407
P577
1994-11-01T00:00:00Z