tRNAHis guanylyltransferase adds G-1 to the 5' end of tRNAHis by recognition of the anticodon, one of several features unexpectedly shared with tRNA synthetases.
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tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerasesDeterminants of tRNA editing and modification: avoiding conundrums, affecting functionStructural basis of reverse nucleotide polymerizationtRNA biology charges to the frontPresence of a classical RRM-fold palm domain in Thg1-type 3'- 5'nucleic acid polymerases and the origin of the GGDEF and CRISPR polymerase domainsTemplate-dependent 3'-5' nucleotide addition is a shared feature of tRNAHis guanylyltransferase enzymes from multiple domains of lifeThe requirement for the highly conserved G-1 residue of Saccharomyces cerevisiae tRNAHis can be circumvented by overexpression of tRNAHis and its synthetase.Unification of Cas protein families and a simple scenario for the origin and evolution of CRISPR-Cas systems3'-5' tRNAHis guanylyltransferase in bacteria.Mitochondrial tRNA 5'-editing in Dictyostelium discoideum and Polysphondylium pallidumPlant mitochondria use two pathways for the biogenesis of tRNAHisCrystal structure of a reverse polymerase.tRNAHis guanylyltransferase catalyzes a 3'-5' polymerization reaction that is distinct from G-1 additiontRNA 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 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.tRNAHis-guanylyltransferase establishes tRNAHis identityAbsence of a universal element for tRNAHis identity in Acanthamoeba castellanii.Template-dependent nucleotide addition in the reverse (3'-5') direction by Thg1-like protein.Identification of distinct biological functions for four 3'-5' RNA polymerases.Do all modifications benefit all tRNAs?Saccharomyces cerevisiae Thg1 uses 5'-pyrophosphate removal to control addition of nucleotides to tRNA(His.).Kinetic analysis of 3'-5' nucleotide addition catalyzed by eukaryotic tRNA(His) guanylyltransferase.Unexpected expansion of tRNA substrate recognition by the yeast m1G9 methyltransferase Trm10.In vitro substrate specificities of 3'-5' polymerases correlate with biological outcomes of tRNA 5'-editing reactions.A role for tRNA(His) guanylyltransferase (Thg1)-like proteins from Dictyostelium discoideum in mitochondrial 5'-tRNA editing.A mutation in the THG1L gene in a family with cerebellar ataxia and developmental delay.S. cerevisiae Trm140 has two recognition modes for 3-methylcytidine modification of the anticodon loop of tRNA substrates.Minimal requirements for reverse polymerization and tRNA repair by tRNAHis guanylyltransferase.Human BCDIN3D Is a Cytoplasmic tRNA-Specific 5'-Monophosphate Methyltransferase
P2860
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P2860
tRNAHis guanylyltransferase adds G-1 to the 5' end of tRNAHis by recognition of the anticodon, one of several features unexpectedly shared with tRNA synthetases.
description
2006 nî lūn-bûn
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2006年の論文
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name
tRNAHis guanylyltransferase ad ...... shared with tRNA synthetases.
@en
tRNAHis guanylyltransferase ad ...... shared with tRNA synthetases.
@nl
type
label
tRNAHis guanylyltransferase ad ...... shared with tRNA synthetases.
@en
tRNAHis guanylyltransferase ad ...... shared with tRNA synthetases.
@nl
prefLabel
tRNAHis guanylyltransferase ad ...... shared with tRNA synthetases.
@en
tRNAHis guanylyltransferase ad ...... shared with tRNA synthetases.
@nl
P2860
P356
P1433
P1476
tRNAHis guanylyltransferase ad ...... y shared with tRNA synthetases
@en
P2093
Eric M Phizicky
P2860
P304
P356
10.1261/RNA.54706
P407
P577
2006-04-19T00:00:00Z