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Wiley InterScience

FEMS Microbiology Reviews

FEMS Microbiology Reviews

Volume 32 Issue 4, Pages 705 - 721

Published Online: 3 Jun 2008

© 2009 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved



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Aminoacyl-tRNA synthetase complexes: molecular multitasking revealed
Corinne D. Hausmann 1 & Michael Ibba 1,2
  1 Department of Microbiology, The Ohio State University, Columbus, OH, USA; and   2 Ohio State Biochemistry Program, The Ohio State University, Columbus, OH, USA
  Correspondence: Michael Ibba, Department of Microbiology, The Ohio State University, 484 West 12th Avenue, Columbus, OH 43210-1292, USA. Tel.: +614 292 2120; fax: +614 292 8120; e-mail: ibba.1@osu.edu

 Editor: Rafael Giraldo

Copyright © 2008 Federation of European Microbiological Societies Published by Blackwell Publishing Ltd
KEYWORDS
aminoacyl-tRNA synthetase • translation • amino acid

ABSTRACT

The accurate synthesis of proteins, dictated by the corresponding nucleotide sequence encoded in mRNA, is essential for cell growth and survival. Central to this process are the aminoacyl-tRNA synthetases (aaRSs), which provide amino acid substrates for the growing polypeptide chain in the form of aminoacyl-tRNAs. The aaRSs are essential for coupling the correct amino acid and tRNA molecules, but are also known to associate in higher order complexes with proteins involved in processes beyond translation. Multiprotein complexes containing aaRSs are found in all three domains of life playing roles in splicing, apoptosis, viral assembly, and regulation of transcription and translation. An overview of the complexes aaRSs form in all domains of life is presented, demonstrating the extensive network of connections between the translational machinery and cellular components involved in a myriad of essential processes beyond protein synthesis.


Received 29 February 2008; revised 21 April 2008; accepted 24 April 2008.
First published online June 2008.

DIGITAL OBJECT IDENTIFIER (DOI)
10.1111/j.1574-6976.2008.00119.x About DOI

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