RESUMO
One of the main characteristics of prokaryotic genomes is the ratio in which guanine-cytosine bases are used in their DNA sequences. This is known as the genomic GC content and varies widely, from values below 20% to values greater than 74%. It has been demonstrated that the genomic GC content varies in accordance with the phylogenetic distribution of organisms and influences the amino acid composition of their corresponding proteomes. This bias is particularly important for amino acids that are coded by GC content-rich codons such as alanine, glycine, and proline, as well as amino acids that are coded by AT-rich codons, such as lysine, asparagine, and isoleucine. In our study, we extend these results by considering the effect of the genomic GC content on the secondary structure of proteins. On a set of 192 representative prokaryotic genomes and proteome sequences, we identified through a bioinformatic study that the composition of the secondary structures of the proteomes varies in relation to the genomic GC content; random coils increase as the genomic GC content increases, while alpha-helices and beta-sheets present an inverse relationship. In addition, we found that the tendency of an amino acid to form part of a secondary structure of proteins is not ubiquitous, as previously expected, but varies according to the genomic GC content. Finally, we discovered that for some specific groups of orthologous proteins, the GC content of genes biases the composition of secondary structures of the proteins for which they code.