title: Thermophiles like hot T.
abstract: A plethora of mechanisms confer protein stability in thermophilic microorganisms and, recently, it was suggested that these mechanisms might be divided along evolutionary lines. Here, a multi-genome comparison shows that there is a statistically significant increase in the proportion of NTN codons correlated with increasing optimal growth temperature for both Bacteria and Archaea. NTN encodes exclusively non-polar, hydrophobic amino acids and indicates a common underlying use of hydrophobicity for stabilizing proteins in Bacteria and Archaea that transcends evolutionary origins. However, some microorganisms do not follow this trend, suggesting that alternate mechanisms (e.g. intracellular electrolytes) might be used for protein stabilization. These studies highlight the usefulness of large-scale comparative genomics to uncover novel relationships that are not immediately obvious from protein structure studies alone.
authors.affiliation: Center for Bioinformatics and Genome Biology, Millennium Institute of Fundamental and Applied Biology, Life Science Foundation and Andrés Bello University, Av. Zanartu 1482, Santiago, Chile.
authors.forename: Ryan
authors.initials: R
authors.lastname: Lieph
authors.forename: Felipe A
authors.initials: FA
authors.lastname: Veloso
authors.forename: David S
authors.initials: DS
authors.lastname: Holmes
mesh_terms: D000595:Amino Acid Sequence; D001105:Archaea / Q000145:classification / Q000235:genetics* / Q000378:metabolism; D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001419:Bacteria / Q000145:classification / Q000235:genetics* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D003062:Codon / Q000235:genetics*; D016680:Genome, Bacterial; D006358:Hot Temperature; D057927:Hydrophobic and Hydrophilic Interactions
chemical_list: D019843:Archaeal Proteins; D001426:Bacterial Proteins; D003062:Codon