Thermophiles like hot T

Ryan Lieph, Felipe A. Veloso, David S. Holmes

Resultado de la investigación: Contribución a una revistaEstudio breverevisión exhaustiva

7 Citas (Scopus)

Resumen

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.

Idioma originalInglés
Páginas (desde-hasta)423-426
Número de páginas4
PublicaciónTrends in Microbiology
Volumen14
N.º10
DOI
EstadoPublicada - oct 2006

Áreas temáticas de ASJC Scopus

  • Microbiología
  • Microbiología (médica)
  • Enfermedades infecciosas
  • Virología

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