Título: Genetic code redundancy and its influence on the encoded polypeptides
Autores: Spencer, Paige S
Barral, Jose M.; The University of Texas Medical Branch
Fecha: 2012-03-20
Publicador: Computacional and structural biotechnology journal
Fuente:
Tipo: info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Peer-reviewed Article
Tema: No aplica
Descripción: The genetic code is said to be redundant in that the same amino acid residue can be encoded by multiple, so-called synonymous, codons. If all properties of synonymous codons were entirely equivalent, one would expect that they would be equally distributed along protein coding sequences. However, many studies over the last three decades have demonstrated that their distribution is not entirely random. It has been postulated that certain codons may be translated by the ribosome faster than others and thus their non-random distribution dictates how fast the ribosome moves along particular segments of the mRNA. The reasons behind such segmental variability in the rates of protein synthesis, and thus polypeptide emergence from the ribosome, have been explored by theoretical and experimental approaches. Predictions of the relative rates at which particular codons are translated and their impact on the nascent chain have not arrived at unequivocal conclusions. This is probably due, at least in part, to variation in the basis for classification of codons as “fast” or “slow”, as well as variability in the number and types of genes and proteins analyzed. Recent methodological advances have allowed nucleotide-resolution studies of ribosome residency times in entire transcriptomes, which confirm the non-uniform movement of ribosomes along mRNAs and shed light on the actual determinants of rate control. Moreover, experiments have begun to emerge that systematically examine the influence of variations in ribosomal movement and the fate of the emerging polypeptide chain.
Idioma: Inglés

Artículos similares:

Systems biology and metabolic engineering of Arthrospira cell factories por Klanchui, Amornpan,Vorapreeda, Tayvich,Vongsangnak, Wanwipa,Kannapho, Chiraphan,Cheevadhanarak, Supapon,Meechai, Asawin
The Role of INDY in Metabolic Regulation por Willmes, Diana M; Charité University School of Medicine Berlin,Birkenfeld, Andreas L; Charité University School of Medicine Berlin
Structure-based Methods for Computational Protein Functional Site Prediction por KC, Dukka B; North Carolina A&T State University
The Biochemistry of Vitreoscilla hemoglobin por Stark, Benjamin C.; Illinois Institute of Technology,Dikshit, Kanak L.; Institute of Microbial Technology,Pagilla, Krishna R.; Illinois Institute of Technology
Computer-Aided Protein Directed Evolution: a Review of Web Servers, Databases and other Computational Tools for Protein Engineering por Verma, Rajni; Jacobs University Bremen,Schwaneberg, Ulrich; RWTH Aachen University,Roccatano, Danilo; Jacobs University Bremen
A method to predict edge strands in beta-sheets from protein sequences por Guilloux, Antonin,Caudron, Bernard,Jestin, Jean-Luc
MD simulation studies to investigate iso-energetic conformational behaviour of modified nucleosides m2G and m22G present in tRNA por Bavi, Rohit S,Sambhare, Susmit B,Sonawane, Kailas D; Structural Bioinformatics Unit, Department of Biochemistry, Shivaji University, Kolhapur 416 004, Maharashtra (M.S.), India.
Metabolomics in the identification of biomarkers of dietary intake por O’Gorman, Aoife,Gibbons, Helena,Brennan, Lorraine
10