Disease relevance of YDR341C

• In the present study, we solved the crystal structure of a typical A20-recognizing ArgRS from Thermus thermophilus at 2.3 A resolution [1].
• The kinetic data revealed that yeast ArgRS could charge E. coli tRNA(Arg), but at a lower efficiency than it charged either the transcribed or native yeast tRNA(Arg) [2].

High impact information on YDR341C

• The crystal structure of arginyl-tRNA synthetase (ArgRS) from Saccharomyces cerevisiae, a class I aminoacyl-tRNA synthetase (aaRS), with L-arginine bound to the active site has been solved at 2.75 A resolution and refined to a crystallographic R-factor of 19.7% [3].
• The guanidinium group forms two salt bridge interactions with two acidic residues, and one H-bond with a tyrosine residue; these three residues are strictly conserved in all ArgRS sequences [3].
• The effects of the substitutions were analyzed in vivo in an ArgRS-knockout strain and in vitro by measuring the aminoacylation efficiencies for two distinct tRNA(Arg) isoacceptors [4].
• Alanine mutagenesis was used to probe all the side chain mediated interactions that occur between tRNA(Arg2)(ICG) and ArgRS [4].
• Thus, ArgRS and tRNA(Arg) can be considered as a kind of ribonucleoprotein, where the tRNA, before being charged, is acting as a cofactor that activates the enzyme [5].

Chemical compound and disease context of YDR341C

• E. coli ArgRS can acylate only its cognate E. coli tRNA [2].
• The 19F nuclear magnetic resonance (NMR) spectra of 4-fluorotryptophan (4-F-Trp)-labeled Escherichia coli arginyl-tRNA synthetase (ArgRS) show that there are distinct conformational changes in the catalytic core and tRNA anticodon stem and loop-binding domain of the enzyme, when arginine and tRNA(Arg) are added to the unliganded enzyme [6].

Biological context of YDR341C

• ArgRS is composed predominantly of alpha-helices and can be divided into five domains, including the class I-specific active site [3].

Analytical, diagnostic and therapeutic context of YDR341C

• The ArgRS structure allows the definition of a new framework for sequence alignments and subclass definition in class I aaRSs [3].

References