Literature DB >> 23746255

Structural basis of the translational elongation cycle.

Rebecca M Voorhees1, V Ramakrishnan.   

Abstract

The sequential addition of amino acids to a growing polypeptide chain is carried out by the ribosome in a complicated multistep process called the elongation cycle. It involves accurate selection of each aminoacyl tRNA as dictated by the mRNA codon, catalysis of peptide bond formation, and movement of the tRNAs and mRNA through the ribosome. The process requires the GTPase factors elongation factor Tu (EF-Tu) and EF-G. Not surprisingly, large conformational changes in both the ribosome and its tRNA substrates occur throughout protein elongation. Major advances in our understanding of the elongation cycle have been made in the past few years as a result of high-resolution crystal structures that capture various states of the process, as well as biochemical and computational studies.

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Year:  2013        PMID: 23746255     DOI: 10.1146/annurev-biochem-113009-092313

Source DB:  PubMed          Journal:  Annu Rev Biochem        ISSN: 0066-4154            Impact factor:   23.643


  131 in total

1.  Initiation factor 2 stabilizes the ribosome in a semirotated conformation.

Authors:  Clarence Ling; Dmitri N Ermolenko
Journal:  Proc Natl Acad Sci U S A       Date:  2015-12-14       Impact factor: 11.205

Review 2.  Paradigms of ribosome synthesis: Lessons learned from ribosomal proteins.

Authors:  Michael Gamalinda; John L Woolford
Journal:  Translation (Austin)       Date:  2015-02-02

Review 3.  Ribosome-targeting antibiotics and mechanisms of bacterial resistance.

Authors:  Daniel N Wilson
Journal:  Nat Rev Microbiol       Date:  2014-01       Impact factor: 60.633

4.  Structure of the mammalian 80S initiation complex with initiation factor 5B on HCV-IRES RNA.

Authors:  Hiroshi Yamamoto; Anett Unbehaun; Justus Loerke; Elmar Behrmann; Marianne Collier; Jörg Bürger; Thorsten Mielke; Christian M T Spahn
Journal:  Nat Struct Mol Biol       Date:  2014-07-27       Impact factor: 15.369

Review 5.  smFRET studies of the 'encounter' complexes and subsequent intermediate states that regulate the selectivity of ligand binding.

Authors:  Colin D Kinz-Thompson; Ruben L Gonzalez
Journal:  FEBS Lett       Date:  2014-07-24       Impact factor: 4.124

6.  The ribosome can discriminate the chirality of amino acids within its peptidyl-transferase center.

Authors:  Michael T Englander; Joshua L Avins; Rachel C Fleisher; Bo Liu; Philip R Effraim; Jiangning Wang; Klaus Schulten; Thomas S Leyh; Ruben L Gonzalez; Virginia W Cornish
Journal:  Proc Natl Acad Sci U S A       Date:  2015-04-27       Impact factor: 11.205

7.  Near Saturation of Ribosomal L7/L12 Binding Sites with Ternary Complexes in Slowly Growing E. coli.

Authors:  Mainak Mustafi; James C Weisshaar
Journal:  J Mol Biol       Date:  2019-04-30       Impact factor: 5.469

8.  Flipping of the ribosomal A-site adenines provides a basis for tRNA selection.

Authors:  Xiancheng Zeng; Jeetender Chugh; Anette Casiano-Negroni; Hashim M Al-Hashimi; Charles L Brooks
Journal:  J Mol Biol       Date:  2014-05-09       Impact factor: 5.469

9.  Visualizing transient Watson-Crick-like mispairs in DNA and RNA duplexes.

Authors:  Isaac J Kimsey; Katja Petzold; Bharathwaj Sathyamoorthy; Zachary W Stein; Hashim M Al-Hashimi
Journal:  Nature       Date:  2015-03-11       Impact factor: 49.962

Review 10.  Ribosome-based quality control of mRNA and nascent peptides.

Authors:  Carrie L Simms; Erica N Thomas; Hani S Zaher
Journal:  Wiley Interdiscip Rev RNA       Date:  2016-05-18       Impact factor: 9.957

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