Literature DB >> 16194295

Translation initiation: structures, mechanisms and evolution.

Assen Marintchev1, Gerhard Wagner.   

Abstract

Translation, the process of mRNA-encoded protein synthesis, requires a complex apparatus, composed of the ribosome, tRNAs and additional protein factors, including aminoacyl tRNA synthetases. The ribosome provides the platform for proper assembly of mRNA, tRNAs and protein factors and carries the peptidyl-transferase activity. It consists of small and large subunits. The ribosomes are ribonucleoprotein particles with a ribosomal RNA core, to which multiple ribosomal proteins are bound. The sequence and structure of ribosomal RNAs, tRNAs, some of the ribosomal proteins and some of the additional protein factors are conserved in all kingdoms, underlying the common origin of the translation apparatus. Translation can be subdivided into several steps: initiation, elongation, termination and recycling. Of these, initiation is the most complex and the most divergent among the different kingdoms of life. A great amount of new structural, biochemical and genetic information on translation initiation has been accumulated in recent years, which led to the realization that initiation also shows a great degree of conservation throughout evolution. In this review, we summarize the available structural and functional data on translation initiation in the context of evolution, drawing parallels between eubacteria, archaea, and eukaryotes. We will start with an overview of the ribosome structure and of translation in general, placing emphasis on factors and processes with relevance to initiation. The major steps in initiation and the factors involved will be described, followed by discussion of the structure and function of the individual initiation factors throughout evolution. We will conclude with a summary of the available information on the kinetic and thermodynamic aspects of translation initiation.

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Year:  2004        PMID: 16194295     DOI: 10.1017/S0033583505004026

Source DB:  PubMed          Journal:  Q Rev Biophys        ISSN: 0033-5835            Impact factor:   5.318


  107 in total

1.  Structural dynamics of bacterial translation initiation factor IF2.

Authors:  Hans Wienk; Evgeny Tishchenko; Riccardo Belardinelli; Simona Tomaselli; Ramachandra Dongre; Roberto Spurio; Gert E Folkers; Claudio O Gualerzi; Rolf Boelens
Journal:  J Biol Chem       Date:  2012-02-03       Impact factor: 5.157

2.  Plant cap-binding complexes eukaryotic initiation factors eIF4F and eIFISO4F: molecular specificity of subunit binding.

Authors:  Laura K Mayberry; M Leah Allen; Kelley R Nitka; Lara Campbell; Patricia A Murphy; Karen S Browning
Journal:  J Biol Chem       Date:  2011-09-30       Impact factor: 5.157

3.  Multifactorial determinants of protein expression in prokaryotic open reading frames.

Authors:  Malin Allert; J Colin Cox; Homme W Hellinga
Journal:  J Mol Biol       Date:  2010-08-18       Impact factor: 5.469

Review 4.  The role of the poly(A) binding protein in the assembly of the Cap-binding complex during translation initiation in plants.

Authors:  Daniel R Gallie
Journal:  Translation (Austin)       Date:  2014-10-30

5.  eIF5B employs a novel domain release mechanism to catalyze ribosomal subunit joining.

Authors:  Bernhard Kuhle; Ralf Ficner
Journal:  EMBO J       Date:  2014-03-31       Impact factor: 11.598

6.  The 3' cap-independent translation element of Barley yellow dwarf virus binds eIF4F via the eIF4G subunit to initiate translation.

Authors:  Krzysztof Treder; Elizabeth L Pettit Kneller; Edwards M Allen; Zhaohui Wang; Karen S Browning; W Allen Miller
Journal:  RNA       Date:  2007-11-19       Impact factor: 4.942

7.  A model for the origin of protein synthesis as coreplicational scanning of nascent RNA.

Authors:  Alexander V Yakhnin
Journal:  Orig Life Evol Biosph       Date:  2007-09-20       Impact factor: 1.950

8.  Many nonuniversal archaeal ribosomal proteins are found in conserved gene clusters.

Authors:  Jiachen Wang; Indrani Dasgupta; George E Fox
Journal:  Archaea       Date:  2009-04-28       Impact factor: 3.273

9.  Backbone resonance assignment of the HEAT1-domain of the human eukaryotic translation initiation factor 4GI.

Authors:  Sabine R Akabayov; Gerhard Wagner
Journal:  Biomol NMR Assign       Date:  2013-01-17       Impact factor: 0.746

10.  Role of oxygen consumption in hypoxia protection by translation factor depletion.

Authors:  Barbara Scott; Chun-Ling Sun; Xianrong Mao; Cong Yu; Bhupinder P S Vohra; Jeffrey Milbrandt; C Michael Crowder
Journal:  J Exp Biol       Date:  2013-03-26       Impact factor: 3.312

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