Processivity of translation in the eukaryote cell: role of aminoacyl-tRNA synthetases

FEBS Letters
Marc Mirande

Abstract

Several lines of evidence led to the conclusion that mammalian ribosomal protein synthesis is a highly organized biological process in vivo. A wealth of data support the concept according to which tRNA aminoacylation, formation of the ternary complex on EF1A and delivery of aminoacyl-tRNA to the ribosome is a processive mechanism where tRNA is vectorially transferred from one component to another. Polypeptide extensions, referred to as tRBDs (tRNA binding domains), are appended to mammalian and yeast aminoacyl-tRNA synthetases. The involvement of these domains in the capture of deacylated tRNA and in the sequestration of aminoacylated tRNA, suggests that cycling of tRNA in translation is mediated by the processivity of the consecutive steps. The possible origin of the tRBDs is discussed.

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Citations

Oct 4, 2011·The Journal of Biological Chemistry·Elvira Olmedo-VerdIgnacio Luque
Dec 20, 2011·Nucleic Acids Research·Thomas D GrantElizabeth J Grayhack
Dec 21, 2012·Nucleic Acids Research·Mariana Pavon-EternodJonathan W Yewdell
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Jul 21, 2014·Cellular and Molecular Life Sciences : CMLS·Daniel Tarrant, Tobias von der Haar
Mar 26, 2015·International Journal of Molecular Sciences·Svitlana Havrylenko, Marc Mirande
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Jun 21, 2011·The Journal of Biological Chemistry·Svitlana HavrylenkoMarc Mirande
Jul 10, 2020·Nucleic Acids Research·Krishnendu KhanPaul L Fox
Nov 22, 2019·ACS Chemical Biology·Liubov Yakovlieva, Marthe T C Walvoort

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