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J. Biol. Chem., Vol. 275, Issue 42, 32383-32386, October 20, 2000

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ACCELERATED PUBLICATION
Structural and Genomic Correlates of Hyperthermostability^*

From the ^§ Architecture et Fonction des Macromolécules Biologiques, CNRS UPR9039, and the ^¶ Information Génétique et Structurale, CNRS UMR 1889, 31 chemin Joseph Aiguier, 13402 Marseille cedex 20, France

While most organisms grow at temperatures ranging between 20 and 50 °C, many archaea and a few bacteria have been found capable of withstanding temperatures close to 100 °C, or beyond, such as Pyrococcus or Aquifex. Here we report the results of two independent large scale unbiased approaches to identify global protein properties correlating with an extreme thermophile lifestyle. First, we performed a comparative proteome analyses using 30 complete genome sequences from the three kingdoms. A large difference between the proportions of charged versus polar (noncharged) amino acids was found to be a signature of all hyperthermophilic organisms. Second, we analyzed the water accessible surfaces of 189 protein structures belonging to mesophiles or hyperthermophiles. We found that the surfaces of hyperthermophilic proteins exhibited the shift already observed at the genomic level, i.e. a proportion of solvent accessible charged residues strongly increased at the expense of polar residues. The biophysical requirements for the presence of charged residues at the protein surface, allowing protein stabilization through ion bonds, is therefore clearly imprinted and detectable in all genome sequences available to date.

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