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Structure and Dynamics of the Human Multi-tRNA Synthetase Complex.
Kim, Myung Hee; Kang, Beom Sik.
Afiliación
  • Kim MH; Infection and Immunity Research Laboratory, Metabolic Regulation Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, South Korea. mhk8n@kribb.re.kr.
  • Kang BS; School of Life Sciences, Kyungpook National University, Daegu, South Korea. bskang2@knu.ac.kr.
Subcell Biochem ; 99: 199-233, 2022.
Article en En | MEDLINE | ID: mdl-36151377
ABSTRACT
Aminoacyl-tRNA synthetases (ARSs) are essential enzymes that ligate amino acids to their cognate tRNAs during protein synthesis. A growing body of scientific evidence acknowledges that ubiquitously expressed ARSs act as crossover mediators of biological processes, such as immunity and metabolism, beyond translation. In particular, a cytoplasmic multi-tRNA synthetase complex (MSC), which consists of eight ARSs and three ARS-interacting multifunctional proteins in humans, is recognized to be a central player that controls the complexity of biological systems. Although the role of the MSC in biological processes including protein synthesis is still unclear, maintaining the structural integrity of MSC is essential for life. This chapter deals with current knowledge on the structural aspects of the human MSC and its protein components. The main focus is on the regulatory functions of MSC beyond its catalytic activity.
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Aminoacil-ARNt Sintetasas Límite: Humans Idioma: En Revista: Subcell Biochem Año: 2022 Tipo del documento: Article País de afiliación: Corea del Sur

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Aminoacil-ARNt Sintetasas Límite: Humans Idioma: En Revista: Subcell Biochem Año: 2022 Tipo del documento: Article País de afiliación: Corea del Sur