Molecular network and functional implications of macromolecular tRNA synthetase complex.
Understanding the complex network and multi-functionality of proteins is one of the main objectives of post-genome research. Aminoacyl-tRNA synthetases (ARSs) are the family of enzymes that are essential for cellular protein synthesis and viability that catalyze the attachment of specific amino acids to their cognate tRNAs. However, a lot of evidence has shown that these enzymes are multi-functional proteins that are involved in diverse cellular processes, such as tRNA processing, RNA splicing and trafficking, rRNA synthesis, apoptosis, angiogenesis, and inflammation. In addition, mammalian ARSs form a macromolecular complex with three auxiliary factors or with the elongation factor complex. Although the functional meaning and physiological significance of these complexes are poorly understood, recent data on the molecular interactions among the components for the multi-ARS complex are beginning to provide insights into the structural organization and cellular functions. In this review, the molecular mechanism for the assembly and functional implications of the multi-ARS complex will be discussed.
Han
Jung Min
JM
Imagene Co. Biotechnology Incubating Center, Golden Helix, Seoul National University, San 56-1, Shillim-dong, Kwanak-Gu, Republic of Korea.
Kim
Jin Young
JY
Kim
Sunghoon
S
D000604:Amino Acyl-tRNA Synthetases / Q000737:chemistry / Q000145:classification / Q000502:physiology*; D000818:Animals; D046911:Macromolecular Substances; D008954:Models, Biological; D010445:Peptide Elongation Factors / Q000378:metabolism; D014176:Protein Biosynthesis
D046911:Macromolecular Substances; D010445:Peptide Elongation Factors; D000604:Amino Acyl-tRNA Synthetases