Role of the extra G-C pair at the end of the acceptor stem of tRNA(His) in aminoacylation.
about
tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerasesA central pseudoknotted three-way junction imposes tRNA-like mimicry and the orientation of three 5' upstream pseudoknots in the 3' terminus of tobacco mosaic virus RNA.Recognition nucleotides for human phenylalanyl-tRNA synthetaseTFAM detects co-evolution of tRNA identity rules with lateral transfer of histidyl-tRNA synthetaseStructural basis of reverse nucleotide polymerizationCrystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylatetRNAHis maturation: an essential yeast protein catalyzes addition of a guanine nucleotide to the 5' end of tRNAHisEvolutionary conservation of a functionally important backbone phosphate group critical for aminoacylation of histidine tRNAs.Histidyl-tRNA synthetaseResected RNA pseudoknots and their recognition by histidyl-tRNA synthetasetRNA recognition of tRNA-guanine transglycosylase from a hyperthermophilic archaeon, Pyrococcus horikoshii.Template-dependent 3'-5' nucleotide addition is a shared feature of tRNAHis guanylyltransferase enzymes from multiple domains of lifeSelenocysteine inserting tRNAs: an overview.The requirement for the highly conserved G-1 residue of Saccharomyces cerevisiae tRNAHis can be circumvented by overexpression of tRNAHis and its synthetase.Enzymatic aminoacylation of an eight-base-pair microhelix with histidine.Nucleotides that determine Escherichia coli tRNA(Arg) and tRNA(Lys) acceptor identities revealed by analyses of mutant opal and amber suppressor tRNAs.The tRNA specificity of Thermus thermophilus EF-Tu.Depletion of Saccharomyces cerevisiae tRNA(His) guanylyltransferase Thg1p leads to uncharged tRNAHis with additional m(5)C.Biosynthesis of archaeosine, a novel derivative of 7-deazaguanosine specific to archaeal tRNA, proceeds via a pathway involving base replacement on the tRNA polynucleotide chain.3'-5' tRNAHis guanylyltransferase in bacteria.Crystal structure of a reverse polymerase.RNA editing of larch mitochondrial tRNA(His) precursors is a prerequisite for processingBiosynthesis of Histidine.Role of acceptor stem conformation in tRNAVal recognition by its cognate synthetase.tRNA 5'-end repair activities of tRNAHis guanylyltransferase (Thg1)-like proteins from Bacteria and Archaea.Change of tRNA identity leads to a divergent orthogonal histidyl-tRNA synthetase/tRNAHis pairA histidine accepting tRNA-like fold at the 3'-end of satellite tobacco mosaic virus RNA.Efficient mischarging of a viral tRNA-like structure and aminoacylation of a minihelix containing a pseudoknot: histidinylation of turnip yellow mosaic virus RNA.Suppression of amber codons in Caulobacter crescentus by the orthogonal Escherichia coli histidyl-tRNA synthetase/tRNAHis pairLife without post-transcriptional addition of G-1: two alternatives for tRNAHis identity in EukaryaStructural basis for recognition of G-1-containing tRNA by histidyl-tRNA synthetase.Small RNA helices as substrates for aminoacylation and their relationship to charging of transfer RNAs.tRNAHis-guanylyltransferase establishes tRNAHis identityLoss of a universal tRNA featureDoing it in reverse: 3'-to-5' polymerization by the Thg1 superfamily.RNA damage in biological conflicts and the diversity of responding RNA repair systems5'-Terminal nucleotide variations in human cytoplasmic tRNAHisGUG and its 5'-halves.A genomically modified Escherichia coli strain carrying an orthogonal E. coli histidyl-tRNA synthetase•tRNAHis pair.Absence of a universal element for tRNAHis identity in Acanthamoeba castellanii.Template-dependent nucleotide addition in the reverse (3'-5') direction by Thg1-like protein.
P2860
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P2860
Role of the extra G-C pair at the end of the acceptor stem of tRNA(His) in aminoacylation.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
Role of the extra G-C pair at ...... f tRNA(His) in aminoacylation.
@ast
Role of the extra G-C pair at ...... f tRNA(His) in aminoacylation.
@en
type
label
Role of the extra G-C pair at ...... f tRNA(His) in aminoacylation.
@ast
Role of the extra G-C pair at ...... f tRNA(His) in aminoacylation.
@en
prefLabel
Role of the extra G-C pair at ...... f tRNA(His) in aminoacylation.
@ast
Role of the extra G-C pair at ...... f tRNA(His) in aminoacylation.
@en
P2093
P2860
P356
P1476
Role of the extra G-C pair at ...... f tRNA(His) in aminoacylation.
@en
P2093
P2860
P304
P356
10.1093/NAR/17.19.7855
P407
P577
1989-10-01T00:00:00Z