Modomics - A Database of RNA Modifications
Thg1 from Saccharomyces cerevisiae - protein summary.
Position of modification - modification:
t:0 - G
tRNAHis guanylyltransferase, adds a guanosine residue to the 5' end of tRNAHis after transcription and RNase P cleavage. Enzymes from Thg1 family exhibit 3'-to-5' polymerase activity. A crystal structure of Mycobacterium tuberculosis and H. sapiens homologues have been solved (3OTB, 3OTD, 3OTE and 3OTC, respectively).
tRNAHis maturation: an essential yeast protein catalyzes addition of a guanine nucleotide to the 5' end of tRNAHis.
Gu W, Jackman JE, Lohan AJ, Gray MW, Phizicky EM
tRNAHis guanylyltransferase (THG1), a unique 3′-5′ nucleotidyl transferase, shares unexpected structural homology with canonical 5′-3′ DNA polymerases.
Hyde SJ, Eckenroth BE, Smith BA, Eberley WA, Heintz NH, Jackman JE, Doublié S
Proc Natl Acad Sci U S A
Doing it in reverse: 3'-to-5' polymerization by the Thg1 superfamily.
Jackman JE, Gott JM, Gray MW
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