PL EN


Preferences help
enabled [disable] Abstract
Number of results
2003 | 44 | 2 | 235-261
Article title

Internal correspondence analysis of codon and amino-acid usage in thermophilic bacteria

Title variants
Languages of publication
EN
Abstracts
EN
Starting from two datasets of codon usage in coding sequences from mesophilic and thermophilic bacteria, we used internal correspondence analysis to study the variability of codon usage within and between species, and within and between amino acids. The first dataset included 18,958,458 codons from 58,482 coding sequences from completely sequenced genomes of 25 species, along with 6,793,581 dinucleotides from 21,876 intergenic spaces. The second dataset, with partially sequenced genomes, included 97,095,873 codons from 293 bacterial species. Results were consistent between the two datasets. The trend for the amino-acid composition of thermophilic proteins was found to be under the control of a pressure at the nucleic acid level, not a selection at the protein level. This effect was not present in intergenic spaces, ruling out a pressure at the DNA level. The pattern at the mRNA level was more complex than a simple purine enrichment of the sense strand of coding sequences. Outliers in the partial genome dataset introduced a note of caution about the interpretation of temperature as the direct determinant of the trend observed in thermophiles. The surprising lack of selection on the amino-acid content of thermophilic proteins suggests that the amino-acid repertoire was set up in a hot environment.
Discipline
Publisher

Year
Volume
44
Issue
2
Pages
235-261
Physical description
Contributors
author
author
References
Document Type
ARTICLE
Publication order reference
J.R. Lobry, Laboratoire de Biometrie, Biologie Evolutive, Centre National de la Recherche Scientifique -UMR-5558, Universite Claude Bernard - LYON I, 43 Bd 11/11/1918, F-69622 Villeurbanne Cedex, France
Identifiers
YADDA identifier
bwmeta1.element.element-from-psjc-c9f67d73-82ad-3d2f-a616-ef5fcbe0cda3
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.