Modomics - A Database of RNA Modifications
TsaC from Escherichia coli - protein summary.
tRNA N6-threonylcarbamoyladenosine(37) synthesis protein
Position of modification - modification:
t:37 - t6A
TsaC, the bacterial ortholog of eukaryal and archaeal Sua5, is an ATPase (produces AMP) that binds A37-containing tRNA, but not threonine. Together with 3 other proteins (TsaD=YgjD, TsaB=YeaZ and TsaE=YjeE), ATP, threonine and bicarbonate as cofactors, they catalyze the in vitro formation of t6A (threonyl-carbamoylation) at position 37 of all bacterial tRNA decoding ANN codons (ile, Met, Thr, Lys, Asn, Ser and Arg). However the detailed stepwise mechanism of t6A formation is still not known (March 2012).
The structure of the yrdC gene product from Escherichia coli reveals a new fold and suggests a role in RNA binding.
Teplova M, Tereshko V, Sanishvili R, Joachimiak A, Bushueva T, Anderson WF, Egli M
The universal YrdC/Sua5 family is required for the formation of threonylcarbamoyladenosine in tRNA.
El Yacoubi B, Lyons B, Cruz Y, Reddy R, Nordin B, Agnelli F, Williamson JR, Schimmel P, Swairjo MA, de Crecy-Lagard V
Nucleic Acids Res
YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase.
Harris KA, Jones V, Bilbille Y, Swairjo MA, Agris PF
Biosynthesis of threonylcarbamoyl adenosine (t6A), a universal tRNA nucleoside.
Deutsch C, El Yacoubi B, de Crecy-Lagard V, Iwata-Reuyl D
J Biol Chem
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