Literature DB >> 25874843

Mechanisms of ribosome rescue in bacteria.

Kenneth C Keiler1.   

Abstract

Ribosomes that stall during translation need to be rescued to ensure that the protein synthesis capacity of the cell is maintained. Stalling arises when ribosomes become trapped at the 3' end of an mRNA, which occurs when a codon is unavailable, as this leads to the arrest of elongation or termination. In addition, various factors can induce ribosome stalling in the middle of an mRNA, including the presence of specific amino acid sequence motifs in the nascent polypeptide. Almost all bacteria use a mechanism known as trans-translation to rescue stalled ribosomes, and some species also have other rescue mechanisms that are mediated either by the alternative ribosome-rescue factor A (ArfA) or ArfB. In this Review, I summarize the recent studies that have demonstrated the conditions that trigger ribosome stalling, the pathways that bacteria use to rescue stalled ribosomes and the physiological effects of these processes.

Mesh:

Year:  2015        PMID: 25874843     DOI: 10.1038/nrmicro3438

Source DB:  PubMed          Journal:  Nat Rev Microbiol        ISSN: 1740-1526            Impact factor:   60.633


  132 in total

1.  SsrA-mediated peptide tagging caused by rare codons and tRNA scarcity.

Authors:  E D Roche; R T Sauer
Journal:  EMBO J       Date:  1999-08-16       Impact factor: 11.598

2.  The ribosomal exit tunnel functions as a discriminating gate.

Authors:  Hitoshi Nakatogawa; Koreaki Ito
Journal:  Cell       Date:  2002-03-08       Impact factor: 41.582

3.  Reduced action of polypeptide release factors induces mRNA cleavage and tmRNA tagging at stop codons in Escherichia coli.

Authors:  Xia Li; Teruaki Yokota; Koichi Ito; Yoshikazu Nakamura; Hiroji Aiba
Journal:  Mol Microbiol       Date:  2007-01       Impact factor: 3.501

Review 4.  The tmRNA system for translational surveillance and ribosome rescue.

Authors:  Sean D Moore; Robert T Sauer
Journal:  Annu Rev Biochem       Date:  2007       Impact factor: 23.643

5.  Translation elongation factor EF-P alleviates ribosome stalling at polyproline stretches.

Authors:  Susanne Ude; Jürgen Lassak; Agata L Starosta; Tobias Kraxenberger; Daniel N Wilson; Kirsten Jung
Journal:  Science       Date:  2012-12-13       Impact factor: 47.728

6.  Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA.

Authors:  Susanne K Christensen; Kim Pedersen; Flemming G Hansen; Kenn Gerdes
Journal:  J Mol Biol       Date:  2003-09-26       Impact factor: 5.469

7.  Proline residues at the C terminus of nascent chains induce SsrA tagging during translation termination.

Authors:  Christopher S Hayes; Baundauna Bose; Robert T Sauer
Journal:  J Biol Chem       Date:  2002-07-08       Impact factor: 5.157

8.  Diverse bacterial genomes encode an operon of two genes, one of which is an unusual class-I release factor that potentially recognizes atypical mRNA signals other than normal stop codons.

Authors:  Pavel V Baranov; Bente Vestergaard; Thomas Hamelryck; Raymond F Gesteland; Jens Nyborg; John F Atkins
Journal:  Biol Direct       Date:  2006-09-13       Impact factor: 4.540

9.  Comprehensive identification of essential Staphylococcus aureus genes using Transposon-Mediated Differential Hybridisation (TMDH).

Authors:  Roy R Chaudhuri; Andrew G Allen; Paul J Owen; Gil Shalom; Karl Stone; Marcus Harrison; Timothy A Burgis; Michael Lockyer; Jorge Garcia-Lara; Simon J Foster; Stephen J Pleasance; Sarah E Peters; Duncan J Maskell; Ian G Charles
Journal:  BMC Genomics       Date:  2009-07-01       Impact factor: 3.969

10.  Formation of the first peptide bond: the structure of EF-P bound to the 70S ribosome.

Authors:  Gregor Blaha; Robin E Stanley; Thomas A Steitz
Journal:  Science       Date:  2009-08-21       Impact factor: 47.728

View more
  79 in total

Review 1.  Non-canonical roles of tRNAs and tRNA mimics in bacterial cell biology.

Authors:  Assaf Katz; Sara Elgamal; Andrei Rajkovic; Michael Ibba
Journal:  Mol Microbiol       Date:  2016-06-28       Impact factor: 3.501

2.  Cut in translation: ribosome-dependent mRNA decay.

Authors:  David Lalaouna; Eric Massé
Journal:  EMBO J       Date:  2017-04-10       Impact factor: 11.598

3.  Mechanistic insights into the alternative translation termination by ArfA and RF2.

Authors:  Chengying Ma; Daisuke Kurita; Ningning Li; Yan Chen; Hyouta Himeno; Ning Gao
Journal:  Nature       Date:  2016-12-01       Impact factor: 49.962

4.  Structural basis for ArfA-RF2-mediated translation termination on mRNAs lacking stop codons.

Authors:  Paul Huter; Claudia Müller; Bertrand Beckert; Stefan Arenz; Otto Berninghausen; Roland Beckmann; Daniel N Wilson
Journal:  Nature       Date:  2016-12-01       Impact factor: 49.962

5.  How a circularized tmRNA moves through the ribosome.

Authors:  Christopher D Rae; Yuliya Gordiyenko; V Ramakrishnan
Journal:  Science       Date:  2019-02-15       Impact factor: 47.728

6.  Structural basis of co-translational quality control by ArfA and RF2 bound to ribosome.

Authors:  Fuxing Zeng; Yanbo Chen; Jonathan Remis; Mrinal Shekhar; James C Phillips; Emad Tajkhorshid; Hong Jin
Journal:  Nature       Date:  2017-01-11       Impact factor: 49.962

Review 7.  Ribosomal frameshifting and transcriptional slippage: From genetic steganography and cryptography to adventitious use.

Authors:  John F Atkins; Gary Loughran; Pramod R Bhatt; Andrew E Firth; Pavel V Baranov
Journal:  Nucleic Acids Res       Date:  2016-07-19       Impact factor: 16.971

Review 8.  Regulated Proteolysis in Bacteria: Caulobacter.

Authors:  Kamal Kishore Joshi; Peter Chien
Journal:  Annu Rev Genet       Date:  2016-10-13       Impact factor: 16.830

Review 9.  CRISPR Tools To Control Gene Expression in Bacteria.

Authors:  Antoine Vigouroux; David Bikard
Journal:  Microbiol Mol Biol Rev       Date:  2020-04-01       Impact factor: 11.056

10.  Multistep substrate binding and engagement by the AAA+ ClpXP protease.

Authors:  Reuben A Saunders; Benjamin M Stinson; Tania A Baker; Robert T Sauer
Journal:  Proc Natl Acad Sci U S A       Date:  2020-10-26       Impact factor: 11.205

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.