The heat of sublimation of carbon

Kern, David M.

doi:10.1021/ed033p272

Cited by 11 publications

(2 citation statements)

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“…Preliminary functional assays showed indeed activation of Glu by YadB and inability of this protein to aminoacylate tRNA Glu (22). These first assays, however, revealed the unexpected property of YadB to activate Glu in the absence of tRNA, in contrast to canonical GluRSs that require tRNA Glu for this step (37). The comparative kinetic data obtained with wild-type YadB and GluRS (Table 1) fully confirm those obtained with His-tagged YadB (22).…”

Section: Resultssupporting

confidence: 60%

An aminoacyl-tRNA synthetase-like protein encoded by the Escherichia coli yadB gene glutamylates specifically tRNA ^Asp

Dubois

Blaise

Becker

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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The product of the Escherichia coli yadB gene is homologous to the N-terminal part of bacterial glutamyl-tRNA synthetases (GluRSs), including the Rossmann fold with the acceptor-binding domain and the stem-contact fold. This GluRS-like protein, which lacks the anticodon-binding domain, does not use tRNA Glu as substrate in vitro nor in vivo, but aminoacylates tRNA Asp with glutamate. The yadB gene is expressed in wild-type E. coli as an operon with the dksA gene, which encodes a protein involved in the general stress response by means of its action at the translational level. The fate of the glutamylated tRNA Asp is not known, but its incapacity to bind elongation factor Tu suggests that it is not involved in ribosomal protein synthesis. Genes homologous to yadB are present only in bacteria, mostly in Proteobacteria. Sequence alignments and phylogenetic analyses show that the YadB proteins form a distinct monophyletic group related to the bacterial and organellar GluRSs (␣-type GlxRSs superfamily) with ubiquitous function as suggested by the similar functional properties of the YadB homologue from Neisseria meningitidis.glutamyl-tRNA synthetase ͉ misacylation ͉ evolution

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Section: Resultssupporting

confidence: 60%