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SANTOS, A.S. Structure and function: evolution of the protein Glutathione S Transferase D1 in the species of the cluster Drosophila buzzatii (group Drosophila repleta). 2018. 78f. Dissertação (Mestrado em Ciência). Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, 2018. The cluster Drosophila buzzatii (group D. repleta) is constituted by seven cryptic species, with larval development occurring exclusively in tissues of decomposing cacti. Cacti are composed of several chemical compounds, which include toxic substances (alkaloids, steroids and phenols) for insects. In the cactophilic species Drosophila mojavensis and D. buzzatii, the GSTD1 gene, from the Glutathione S-transferases family, is overexpressed in larvae submitted to toxic substrates. GSTD1 is indicated with detoxification function, being important target of selection and necessary in the adaptation process in Drosophila species. In the present work, complete coding regions of the GSTD1 gene were isolated from the seven species of the D. buzzatii cluster with the objective of understanding the evolution in DNA sequences and phenotypes (proteins), with analysis of the structure and function of the GSTD1 protein in the process detoxification, among the species of the cluster. 630 bp of the GSTD1 gene was sequenced for each species and the primary structure of the protein, composed of 209 amino acids, was inferred "In silico". In the Bayesian phylogenetic inferences with the GSTD1 gene, monophyly of the cluster is indicated, with the formation of the first grouping between D. buzzatii and D. koepferae, the second composed by D. antonietae and D. serido and finally, a grouping between D. gouveai, D. borborema and D. seriema. Signs of positive selection on DNA sequences result in changes in amino acid residues at positions 39, 133, 136 and 209, with changes in the chemical structure of the GSTD1 protein among the species in the cluster. We obtained seven models of the GSTD1 protein, performed with homology modeling, one for each species of the D. buzzatii cluster. In the molecular docking between the GSTD1 proteins with the mescaline ligand, it was observed that the proteins of D. seriema, D. gouveai and D. koepferae presented better chemical interactions with the ligand and lower energy expenditure. Interestingly, the mescaline linker was positioned between two GSH (glutathione reductase) regions, in D. seriema, D. gouveai and D. koepferae. The evolution of the GSTD1 gene among D. buzzatii cluster species involves positive selection signals in DNA sequences with chemical changes in amino acid residues at the G-sites and in the internal structure of the GSTD1 protein, as well as the ability of the GSH binding site to recognize the alkaloid compound. Key-words: Drosophila. Cactaceae. GSTD1 protein. GSH site. detoxification. adaptation.

Estrutura e função: evolução da proteína Glutationa S - Transferase D1 nas espécies do cluster Drosophila buzzatii (grupo Drosophila repleta)