Mutants That Affect Recoding

Part of the Nucleic Acids and Molecular Biology book series (NUCLEIC, volume 24)


Fast, accurate translation is a hallmark of protein synthesis. However, recoding systems subvert the normal decoding mechanisms to redefine codons or shift translation into alternate reading frames. Genetic analyses in yeast and bacteria have enhanced our understanding of non-standard decoding and of normal decoding processes. Recent crystallographic efforts have provided unprecedented insights into the mechanisms underlying translation and the selection of cognate tRNAs. Ribosomal components and factors involved in decoding have also been identified genetically, through selections for mutants that alter the fidelity of protein synthesis, or impact upon various recoding phenomena. The availability of high-resolution structures of ribosomal complexes together with advances in biochemistry now allow the effects of many of these mutant components to be explained in molecular terms.


Ribosomal Protein Closed Conformation Peptide Bond Formation Peptidyltransferase Center Translational Fidelity 



Work in the authors’ laboratories was supported by grants GM058859 and AI064307 from the National Institutes of Health (to J.D.D.) and MCB0745025 from the National Science Foundation (to M.OC.).


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© Springer Science+Business Media, LLC 2010

Authors and Affiliations

  1. 1.Department of Cell Biology and Molecular Genetics, 2135 Microbiology BuildingUniversity of MarylandCollege ParkUSA
  2. 2.School of Biological SciencesUniversity of Missouri-Kansas CityKansas CityUSA

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