Structural disorder in expanding the functionome of aminoacyl-tRNA synthetases.
Over the past decade, aminoacyl-tRNA synthetases (AARSs) have emerged as a new class of regulatory proteins with widespread functions beyond their classic role in protein synthesis. The functional expansion concurs with the incorporation of new domains and motifs to AARSs and coincides with the emergence of the multi-synthetase complex (MSC) during the course of eukaryotic evolution. Notably, the new domains in AARSs are often found to be structurally disordered or to be linked to the enzyme cores via unstructured linkers. We performed bioinformatic analysis and classified the 20 human cytoplasmic AARSs into three groups based on their propensities for structural disorder. The analysis also suggests that, while the assembly of the MSC mainly involves ordered structural domains, structurally disordered regions play an important role in activating and expanding the regulatory functions of AARSs.
Departments of Chemical Physiology and Cell and Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. Electronic address: xlyang@scripps.edu.
Xiang-Lei
XL
Yang
D000604:Amino Acyl-tRNA Synthetases / Q000737:chemistry* / Q000145:classification / Q000378:metabolism; D019295:Computational Biology; D003593:Cytoplasm / Q000378:metabolism; D006801:Humans; D054730:Protein Interaction Domains and Motifs; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism
D021122:Protein Subunits; D000604:Amino Acyl-tRNA Synthetases