Ribosomal proteins EL11 from Escherichia coli and L15 from Saccharomyces cerevisiae bind to the same site in both yeast 26 S and mouse 28 S rRNA.
about
A delayed-early response nuclear gene encoding MRPL12, the mitochondrial homologue to the bacterial translational regulator L7/L12 proteinThe GTPase center protein L12 is required for correct ribosomal stalk assembly but not for Saccharomyces cerevisiae viability.Ribosomal protein S14 of Saccharomyces cerevisiae regulates its expression by binding to RPS14B pre-mRNA and to 18S rRNA.A covariant change of the two highly conserved bases in the GTPase-associated center of 28 S rRNA in silkworms and other moths.Conservation of the S10-spc-alpha locus within otherwise highly plastic genomes provides phylogenetic insight into the genus LeptospiraFunctional substitution of mouse ribosomal protein L27' for yeast ribosomal protein L29 in yeast ribosomes.The 26S rRNA binding ribosomal protein equivalent to bacterial protein L11 is encoded by unspliced duplicated genes in Saccharomyces cerevisiae.The yeast omnipotent suppressor SUP46 encodes a ribosomal protein which is a functional and structural homolog of the Escherichia coli S4 ram protein.Replacement of the L11 binding region within E.coli 23S ribosomal RNA with its homologue from yeast: in vivo and in vitro analysis of hybrid ribosomes altered in the GTPase centre.Chimeric rRNAs containing the GTPase centers of the developmentally regulated ribosomal rRNAs of Plasmodium falciparum are functionally distinctA chemical interference study on the interaction of ribosomal protein L11 from Escherichia coli with RNA molecules containing its binding site from 23S rRNALupus antiribosomal P antisera contain antibodies to a small fragment of 28S rRNA located in the proposed ribosomal GTPase center.The duplicated Saccharomyces cerevisiae gene SSM1 encodes a eucaryotic homolog of the eubacterial and archaebacterial L1 ribosomal proteins.Synthesis of ribosomes in Saccharomyces cerevisiae.The conserved GTPase center and variable region V9 from Saccharomyces cerevisiae 26S rRNA can be replaced by their equivalents from other prokaryotes or eukaryotes without detectable loss of ribosomal function.Detection of a key tertiary interaction in the highly conserved GTPase center of large subunit ribosomal RNA.All three functional domains of the large ribosomal subunit protein L25 are required for both early and late pre-rRNA processing steps in Saccharomyces cerevisiae.Conformational changes induced in the Saccharomyces cerevisiae GTPase-associated rRNA by ribosomal stalk components and a translocation inhibitor.Cooperative assembly of proteins in the ribosomal GTPase centre demonstrated by their interactions with mutant 23S rRNAs.A functional site of the GTPase-associated center within 28S ribosomal RNA probed with an anti-RNA autoantibodyIn vivo assembling of bacterial ribosomal protein L11 into yeast ribosomes makes the particles sensitive to the prokaryotic specific antibiotic thiostrepton.Formation of Tertiary Interactions during rRNA GTPase Center Folding.Structural destabilization of the recombinant thermophilic TthL11 ribosomal protein by a single amino acid substitution.Binding of Mammalian Ribosomal Protein Complex P0·P1·P2 and Protein L12 to the GTPase-associated Domain of 28 S Ribosomal RNA and Effect on the Accessibility to Anti-28 S RNA Autoantibody
P2860
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P2860
Ribosomal proteins EL11 from Escherichia coli and L15 from Saccharomyces cerevisiae bind to the same site in both yeast 26 S and mouse 28 S rRNA.
description
1987 nî lūn-bûn
@nan
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
1987年论文
@zh
1987年论文
@zh-cn
name
Ribosomal proteins EL11 from E ...... east 26 S and mouse 28 S rRNA.
@en
type
label
Ribosomal proteins EL11 from E ...... east 26 S and mouse 28 S rRNA.
@en
prefLabel
Ribosomal proteins EL11 from E ...... east 26 S and mouse 28 S rRNA.
@en
P2093
P1476
Ribosomal proteins EL11 from E ...... east 26 S and mouse 28 S rRNA.
@en
P2093
Ballesta JP
Einerhand SW
de Regt VC
el-Baradi TT
P304
P356
10.1016/0022-2836(87)90494-3
P407
P577
1987-06-01T00:00:00Z