A comparison of proteins from Pyrococcus furiosus and Pyrococcus abyssi: barophily in the physicochemical properties of amino acids and in the genetic code.

A comparison is made between orthologous proteins from a nonbarophile (Pyrococcus furiosus) and a barophile (Pyrococcus abyssi) organism. The pattern of asymmetries in the amino acid substitution process identifies the amino acids arginine, serine, glycine, valine and aspartic acid as those having the most barophilic behaviour, and tyrosine and glutamine as the least barophilic. The construction of a hydrostatic pressure asymmetry index (PAI) which orders the amino acids from the most barophilic to the least barophilic makes it possible to visualise the amino acid properties that best explain barophily. The polarity of amino acids is positively correlated to the PAI values, i.e., on average, the more polar amino acids possess a higher PAI value, that is to say they are more barophilic. Moreover, the "size" of amino acids (molecular weight) is negatively correlated to the PAI value, that is to say that, on average, high PAI values are associated to "small" amino acids which are therefore more barophilic than "larger" ones. These two amino acid properties are the same ones that are known for having been important in affecting the origin of genetic code organisation. All the above, as well as the significant and positive correlation between the number of codons attributed to the amino acids in the genetic code and the PAI values, seem to favour the hypothesis that genetic code structuring took place under high hydrostatic pressure.