Conserved amino acids in each subunit of the heteroligomeric tRNA m1A58 Mtase from Saccharomyces cerevisiae contribute to tRNA binding.
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Bioinformatics analysis suggests base modifications of tRNAs and miRNAs in Arabidopsis thalianaTrmt61B is a methyltransferase responsible for 1-methyladenosine at position 58 of human mitochondrial tRNAsMethylated nucleosides in tRNA and tRNA methyltransferasesMechanism of activation of methyltransferases involved in translation by the Trm112 'hub' proteinYeast Trm7 interacts with distinct proteins for critical modifications of the tRNAPhe anticodon loop.Crystal structure of the two-subunit tRNA m(1)A58 methyltransferase TRM6-TRM61 from Saccharomyces cerevisiae.Structural comparison of tRNA m(1)A58 methyltransferases revealed different molecular strategies to maintain their oligomeric architecture under extreme conditionsMeta-analysis of small RNA-sequencing errors reveals ubiquitous post-transcriptional RNA modifications.Crystallization and preliminary X-ray diffraction crystallographic study of tRNA m(1)A58 methyltransferase from Saccharomyces cerevisiae.Diversity in mechanism and function of tRNA methyltransferases.Crystal Structure of the Human tRNA m(1)A58 Methyltransferase-tRNA(3)(Lys) Complex: Refolding of Substrate tRNA Allows Access to the Methylation Target.Stereochemical mechanisms of tRNA methyltransferases.Two-subunit enzymes involved in eukaryotic post-transcriptional tRNA modification.Identification and modeling of a phosphatase-like domain in a tRNA 2'-O-ribosyl phosphate transferase Rit1p.The emerging biology of RNA post-transcriptional modifications.Identification of tRNA nucleoside modification genes critical for stress response and development in rice and Arabidopsis.Binding synergy as an essential step for tRNA editing and modification enzyme codependence in Trypanosoma brucei.
P2860
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P2860
Conserved amino acids in each subunit of the heteroligomeric tRNA m1A58 Mtase from Saccharomyces cerevisiae contribute to tRNA binding.
description
2007 nî lūn-bûn
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name
Conserved amino acids in each ...... ae contribute to tRNA binding.
@en
Conserved amino acids in each ...... ae contribute to tRNA binding.
@nl
type
label
Conserved amino acids in each ...... ae contribute to tRNA binding.
@en
Conserved amino acids in each ...... ae contribute to tRNA binding.
@nl
prefLabel
Conserved amino acids in each ...... ae contribute to tRNA binding.
@en
Conserved amino acids in each ...... ae contribute to tRNA binding.
@nl
P2093
P2860
P356
P1476
Conserved amino acids in each ...... ae contribute to tRNA binding.
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P2093
Daniel S Sem
James T Anderson
Sarah G Ozanick
P2860
P304
P356
10.1093/NAR/GKM574
P407
P577
2007-10-10T00:00:00Z