Molecular network and functional implications of macromolecular tRNA synthetase complex

Research output: Journal Publications and Reviews (RGC: 21, 22, 62)62_Review of books or of software (or similar publications/items)peer-review

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Detail(s)

Original languageEnglish
Pages (from-to)985-993
Journal / PublicationBiochemical and Biophysical Research Communications
Volume303
Issue number4
Publication statusPublished - 18 Apr 2003
Externally publishedYes

Abstract

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. © 2003 Elsevier Science (USA). All rights reserved.

Research Area(s)

  • Aminoacyl-tRNA synthetase, Complex, Elongation factor, Network, Protein synthesis, Protein-protein interaction, Review