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EcoSal Plus

Domain 4:

Synthesis and Processing of Macromolecules

Aminoacyl-tRNA Synthetases in the Bacterial World

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.
  • Authors: Richard Giegé1, and Mathias Springer2
  • Editor: Susan T. Lovett3
    Affiliations: 1: Architecture et Réactivité de l’ARN, Université de Strasbourg, CNRS, IBMC, 67084 Strasbourg, France; 2: Université Paris Diderot, Sorbonne Cité, UPR9073 CNRS, IBPC, 75005 Paris, France; 3: Brandeis University, Waltham, MA
  • Received 27 January 2016 Accepted 22 February 2016 Published 23 May 2016
  • Address correspondence to Richard Giegé [email protected] and Mathias Springer [email protected]
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  • Abstract:

    Aminoacyl-tRNA synthetases (aaRSs) are modular enzymes globally conserved in the three kingdoms of life. All catalyze the same two-step reaction, i.e., the attachment of a proteinogenic amino acid on their cognate tRNAs, thereby mediating the correct expression of the genetic code. In addition, some aaRSs acquired other functions beyond this key role in translation. Genomics and X-ray crystallography have revealed great structural diversity in aaRSs (e.g., in oligomery and modularity, in ranking into two distinct groups each subdivided in 3 subgroups, by additional domains appended on the catalytic modules). AaRSs show huge structural plasticity related to function and limited idiosyncrasies that are kingdom or even species specific (e.g., the presence in many of non discriminating aaRSs compensating for the absence of one or two specific aaRSs, notably AsnRS and/or GlnRS). Diversity, as well, occurs in the mechanisms of aaRS gene regulation that are not conserved in evolution, notably between distant groups such as Gram-positive and Gram-negative . The review focuses on bacterial aaRSs (and their paralogs) and covers their structure, function, regulation, and evolution. Structure/function relationships are emphasized, notably the enzymology of tRNA aminoacylation and the editing mechanisms for correction of activation and charging errors. The huge amount of genomic and structural data that accumulated in last two decades is reviewed, showing how the field moved from essentially reductionist biology towards more global and integrated approaches. Likewise, the alternative functions of aaRSs and those of aaRS paralogs (e.g., during cell wall biogenesis and other metabolic processes in or outside protein synthesis) are reviewed. Since aaRS phylogenies present promiscuous bacterial, archaeal, and eukaryal features, similarities and differences in the properties of aaRSs from the three kingdoms of life are pinpointed throughout the review and distinctive characteristics of bacterium-like synthetases from organelles are outlined.

  • Citation: Giegé R, Springer M. 2016. Aminoacyl-tRNA Synthetases in the Bacterial World, EcoSal Plus 2016; doi:10.1128/ecosalplus.ESP-0002-2016

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This article is an updated version of the following content:


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