TsaE from Escherichia coli - protein summary.
tRNA N6-threonylcarbamoyladenosine(37) synthesis protein
Position of modification - modification:
t:37 - t6A
This protein belongs to P-loop ATPases. It binds ATP and displays a weak ATPase activity (produce ADP). This protein tends to oligomerize in vitro. Despite TsaC (YrdC), TsaD (YgjD) and TsaB (YeaZ) are present in all bacteria, TsaE (YjeE) is absent in several unicellular and symbiotic bacteria, suggesting that some bacteria can carry out t6A synthesis in absence of YjeE. However, TsaD, TsaC, TsaE and TsaB are both necessary and sufficient for t6A biosynthesis in vitro.
Biosynthesis of threonylcarbamoyl adenosine (t6A), a universal tRNA nucleoside.
Deutsch C, El Yacoubi B, de Crecy-Lagard V, Iwata-Reuyl D
J Biol Chem
Effects on transcription of mutations in ygjD, yeaZ, and yjeE genes, which are involved in a universal tRNA modification in Escherichia coli.
Hashimoto C, Sakaguchi K, Taniguchi Y, Honda H, Oshima T, Ogasawara N, Kato J
Known bioactive small molecules probe the function of a widely conserved but enigmatic bacterial ATPase, YjeE.
Mangat CS, Brown ED
Conserved P-loop GTPases of unknown function in bacteria: an emerging and vital ensemble in bacterial physiology.
Biochem Cell Biol
Mechanism of N6-threonylcarbamoyladenonsine (t(6)A) biosynthesis: isolation and characterization of the intermediate threonylcarbamoyl-AMP.
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