THG1 Antibody

1. Minimal requirements for reverse polymerization and tRNA repair by tRNA(His) guanylyltransferase Thg1 have been presented. PMID: 28901837
2. This study determined the crystal structure of GTP-bound Thg1 from Saccharomyces cerevisiae at the maximum resolution of 3.0 A. PMID: 28623126
3. pyrophosphate removal versus nucleotide addition activities of yeast Thg1 with a set of tRNA(His) substrates PMID: 24548272
4. Study provides the first kinetic insight into the individual steps of the non-Watson-Crick addition of G- to tRNAHis, the known physiological function of Thg1 in yeast. PMID: 22136300
5. tRNA(His) from Thg1p-depleted cells is uncharged, although histidyl tRNA synthetase is active and the 3' end of the tRNA is intact, suggesting that G(-1) is a critical determinant for aminoacylation of tRNA(His) in vivo. PMID: 16135808
6. 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 PMID: 16625026
7. These results suggest that 3'-5' polymerization represents either an uncharacterized role for Thg1 in RNA or DNA repair or metabolism, or it may be a remnant of an earlier catalytic strategy used in nature. PMID: 16731615
8. Thg1 substrate recognition is at least in part mediated by preventing recognition of incorrect substrates for nucleotide addition PMID: 18366186

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KEGG: sce:YGR024C

STRING: 4932.YGR024C