The final step of tRNA splicing in Saccharomyces cerevisiae (Baker's yeast) requires 2'-phosphotransferase (Tpt1) to transfer the 2'-phosphate from
ligated tRNA to NAD, producing mature tRNA and ADP ribose-1' '-2' '-cyclic phosphate. Yeast and Mus musculus (Mouse) Tpt1 protein and bacterial KptA protein can catalyze the conversion of the
generated intermediate to both product and the original substrate, these enzymes
likely use the same reaction mechanism. Step 1 of this reaction is strikingly similar to the
ADP-ribosylation of proteins catalyzed by a number of bacterial toxins.
KptA, a functional Tpt1
protein homologue from Escherichia coli is strikingly similar to yeast Tpt1 in its kinetic parameters, although
E. coli is not known to have a 2'-phosphorylated RNA substrate [1,2].
Spinelli SL, Kierzek R, Turner DH, Phizicky EM.
Transient ADP-ribosylation of a 2'-phosphate implicated in its removal from ligated tRNA during splicing in yeast.
J. Biol. Chem. 274 2637-44 1999
[PubMed: 9915792] http://dx.doi.org/10.1074/jbc.274.5.2637
2.
Steiger MA, Kierzek R, Turner DH, Phizicky EM.
Substrate recognition by a yeast 2'-phosphotransferase involved in tRNA splicing and by its Escherichia coli homolog.
Biochemistry 40 14098-105 2001
[PubMed: 11705403] http://dx.doi.org/10.1021/bi011388t
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