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Aminoacyl-tRNA synthetases: Versatile players in the changing theater of translation

Published online by Cambridge University Press:  07 November 2002

CHRISTOPHER FRANCKLYN
Affiliation:
Department of Biochemistry, University of Vermont, Burlington, Vermont 05405, USA
JOHN J. PERONA
Affiliation:
Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106-9510, USA
JOERN PUETZ
Affiliation:
UPR9002 du Centre National de la Recherche Scientifique, Institut de Biologie Moléculaire et Cellulaire, Strasbourg, 67084 Cedex, France
YA-MING HOU
Affiliation:
Department of Biochemistry, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA
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Abstract

Aminoacyl-tRNA synthetases attach amino acids to the 3′ termini of cognate tRNAs to establish the specificity of protein synthesis. A recent Asilomar conference (California, January 13–18, 2002) discussed new research into the structure–function relationship of these crucial enzymes, as well as a multitude of novel functions, including participation in amino acid biosynthesis, cell cycle control, RNA splicing, and export of tRNAs from nucleus to cytoplasm in eukaryotic cells. Together with the discovery of their role in the cellular synthesis of proteins to incorporate selenocysteine and pyrrolysine, these diverse functions of aminoacyl-tRNA synthetases underscore the flexibility and adaptability of these ancient enzymes and stimulate the development of new concepts and methods for expanding the genetic code.

Type
Research Article
Copyright
2002 RNA Society

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