Premium
Structural and functional consequences of mutating a proteobacteria‐specific surface residue in the catalytic domain of Escherichia coli GluRS
Author(s) -
Dasgupta Saumya,
Manna Debasis,
Basu Gautam
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.05.006
Subject(s) - escherichia coli , transfer rna , mutant , biology , escherichia , enzyme , biochemistry , genetics , chemistry , rna , gene
Nucleotides whose mutations seriously affect glutamylation efficiency are experimentally known for Escherichia coli tRNA Glu . However, not much is known about functional hotspots on the complementary enzyme, glutamyl‐tRNA synthetase (GluRS). From structural and functional studies on an Arg266Leu mutant of E. coli GluRS, we demonstrate that Arg266 is essential for efficient glutamylation of tRNA Glu . Consistent with this result, we found that Arg266 is a conserved signature of proteobacterial GluRS. In contrast, most non‐proteobacterial GluRS contain Leu, and never Arg, at this position. Our results imply a unique strategy of glutamylation of tRNA Glu in proteobacteria under phylum‐specific evolutionary compulsions.