Comments:

Tad2 is part of the functional heterodimeric deaminase Tad2/3. At variance with other dimeric ADAT2/3 deaminases, T. brucei Tad2/3 contains only one functional zinc ion, out of the two per dimeric enzyme. The C-terminal end of subunit tbTad2 plays a critical role in tRNA binding, while subunit Tad3 contributes to catalysis - it is not simply a structural component. This tRNA A:I editing enzyme plays a role in both A:I editing in position 34 and C:U editing in position 32 in vivo. In vitro, this A-to-I tRNA deaminase catalyzes also C-to-U deamination of DNA. The A34-to-I34 deamination reaction was tested with T. brucei tRNA-Thr as substrate. However, as other eukaryotic heterodimeric Tad2/3 it also works on other naturally occurring A34-containing tRNA (Alfonzo J. , unpublished data).

Protein sequence:

Publications:

Title	Authors	Journal	Details	PubMed Id	DOI
A-to-I and C-to-U editing within transfer RNAs.	Su AA, Randau L	Biochemistry (Mosc)	[details]	22022967	-
Determinants of tRNA editing and modification: Avoiding conundrums, affecting function.	Paris Z, Fleming IM, Alfonzo JD	Semin Cell Dev Biol	[details]	22024020	-
A single zinc ion is sufficient for an active Trypanosoma brucei tRNA editing deaminase.	Spears JL, Rubio MA, Gaston KW, Wywial E, Strikoudis A, Bujnicki JM, Papavasiliou FN, Alfonzo JD	J Biol Chem	[details]	21507956	-
The C-terminal end of the Trypanosoma brucei editing deaminase plays a critical role in tRNA binding.	Ragone FL, Spears JL, Wohlgamuth-Benedum JM, Kreel N, Papavasiliou FN, Alfonzo JD	RNA	[details]	21602302	-
An adenosine-to-inosine tRNA-editing enzyme that can perform C-to-U deamination of DNA.	Rubio MA, Pastar I, Gaston KW, Ragone FL, Janzen CJ, Cross GA, Papavasiliou FN, Alfonzo JD	Proc Natl Acad Sci U S A	[details]	17483465	-

Links:

_TriTrypDB_

_GeneDB_

_Wikipedia - Deamination_

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