V. Anantharaman et al., TRAM, a predicted RNA-binding domain, common to tRNA uracil methylation and adenine thiolation enzymes, FEMS MICROB, 197(2), 2001, pp. 215-221
A previously undetected conserved domain is identified in two distinct clas
ses of tRNA-modifying enzymes, namely uridine methylases of the TRM2 family
and enzymes of the MiaB family that are involved in 2-methylthioadenine fo
rmation. This domain, for which the acronym TRAM is proposed after TRM2 and
MiaB, is predicted to bind tRNA and deliver the RNA-modifying enzymatic do
mains to their targets. In addition to the two families of RNA-modifying en
zymes. the TRAM domain is present in several other proteins associated with
the translation machinery and in a family of small, uncharacterized archae
al proteins that are predicted to have a role in the regulation of tRNA mod
ification or translation. Secondary structure prediction indicates that the
TRAM domain adopts a simple beta -barrel fold. In addition. sequence analy
sis of the MiaB family enzymes showed that they share the predicted catalyt
ic site with biotin and lipoate synthases and probably employ the same mech
anism for sulfur insertion into their respective substrate. (C) 2001 Publis
hed by Elsevier Science B.V. on behalf of the Federation of European Microb
iological Societies.