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Aminoacyl‐tRNA synthetase–interacting multifunctional proteins (AIMPs): A triad for cellular homeostasis
Author(s) -
Park Sang Gyu,
Choi EungChil,
Kim Sunghoon
Publication year - 2010
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.324
Subject(s) - aminoacyl trna synthetase , transfer rna , translation (biology) , biology , biochemistry , cofactor , enzyme , genetic code , microbiology and biotechnology , chemistry , rna , amino acid , gene , messenger rna
Aminoacyl‐tRNA synthetases (ARSs) are highly conserved for efficient and precise translation of genetic codes. In higher eukaryotic systems, several different ARSs including glutamyl‐prolyl‐, isoelucyl‐, leucyl‐, methionyl‐, glutaminyl‐, lysyl‐, arginyl‐, and aspartyl‐tRNA synthetase form a macromolecular protein complex with three nonenzymatic cofactors (AIMP1/p43, AIMP2/p38, and AIMP3/p18). Although the structure and functional implications for this complex formation are not completely understood, rapidly accumulating evidences suggest that this complex would work as a molecular hub linked to the multiple signaling pathways that involve the components of enzymes and cofactors. In this article, the roles of three nonenzymatic components of the multi‐tRNA synthetase complex in the assembly of the components and in cell regulation are addressed. © 2010 IUBMB IUBMB Life, 62(4): 296–302, 2010