TRAM, a predicted RNA-binding domain, common to tRNA uracil methylation and adenine thiolation enzymes

Citation
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
Citations number
27
Categorie Soggetti
Microbiology
Journal title
FEMS MICROBIOLOGY LETTERS
ISSN journal
03781097 → ACNP
Volume
197
Issue
2
Year of publication
2001
Pages
215 - 221
Database
ISI
SICI code
0378-1097(20010413)197:2<215:TAPRDC>2.0.ZU;2-M
Abstract
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.