Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Identification of critical residues for G-1 addition and substrate recognition by tRNA(His) guanylyltransferase.

Biochemistry - 22 Apr 2008

Jackman Jane E, Phizicky Eric M

Abstract excerpt

The yeast tRNA(His) guanylyltransferase (Thg1) is an essential enzyme in yeast. Thg1 adds a single G residue to the 5' end of tRNA(His) (G(-1)), which serves as a crucial determinant for aminoacylation of tRNA(His). Thg1 is the only known gene product that catalyzes the 3'-5' addition of a single nucleotide via a normal phosphodiester bond, and since there is no identifiable sequence similarity between Thg1 and...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alanine
Share to Kinetics
Share to Nucleotidyltransferases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Phosphorylation

Share to Saccharomyces cerevisiae

Share to Sequence Alignment

Share to Sequence Homology, Amino Acid

Share to Substrate Specificity

Source

Identifiers

PMID: 18366186
DOI: 10.1021/bi702517q

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of critical residues for G-1 addition and substrate recognition by tRNA(His) guanylyltransferase.PMID 18366186Read ↗

tRNAHis 5-methylcytidine levels increase in response to several growth arrest conditions in Saccharomyces cerevisiae.Semantic proximity Read ↗

Template-dependent nucleotide addition in the reverse (3'-5') direction by Thg1-like protein.Semantic proximity Read ↗

Structural basis for recognition of G-1-containing tRNA by histidyl-tRNA synthetase.Semantic proximity Read ↗

Minimal requirements for reverse polymerization and tRNA repair by tRNAHis guanylyltransferase.Semantic proximity Read ↗

Hypomodified tRNA in evolutionarily distant yeasts can trigger rapid tRNA decay to activate the general amino acid control response, but with different consequencesSemantic proximity Read ↗

Molecular basis for t6A modification in human mitochondria.Semantic proximity Read ↗

The yeast rapid tRNA decay pathway primarily monitors the structural integrity of the acceptor and T-stems of mature tRNA.Semantic proximity Read ↗

Initiator tRNA lacking 1-methyladenosine is unexpectedly targeted by the rapid tRNA decay pathway in evolutionarily distant yeast speciesSemantic proximity Read ↗

tRNA m <sup>1</sup> G9 modification depends on substrate-specific RNA conformational changes induced by the methyltransferase Trm10Semantic proximity Read ↗

Two proteins that form a complex are required for 7-methylguanosine modification of yeast tRNA.Semantic proximity Read ↗

The Enzymatic Paradox of Yeast Arginyl-tRNA Synthetase: Exclusive Arginine Transfer Controlled by a Flexible Mechanism of tRNA Recognition.Semantic proximity Read ↗

Guanine nucleotide pool imbalance impairs multiple steps of protein synthesis and disrupts GCN4 translational control in Saccharomyces cerevisiae.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.