| Processo: | 01/07539-5 |
| Modalidade de apoio: | Auxílio à Pesquisa - Regular |
| Data de Início da vigência: | 01 de outubro de 2001 |
| Data de Término da vigência: | 30 de junho de 2009 |
| Área do conhecimento: | Ciências Biológicas - Bioquímica |
| Pesquisador responsável: | Luis Eduardo Soares Netto |
| Beneficiário: | Luis Eduardo Soares Netto |
| Instituição Sede: | Instituto de Biociências (IB). Universidade de São Paulo (USP). São Paulo , SP, Brasil |
| Município da Instituição Sede: | São Paulo |
| Bolsa(s) vinculada(s): | 06/01359-9 - Suporte tecnico para producao de proteinas recombinantes em larga escala.,
BP.TT 02/06675-5 - Suporte técnico para produção de proteínas puras em grande escala, BP.TT |
| Assunto(s): | Expressão gênica Purificação de proteínas |
| Palavra(s)-Chave do Pesquisador: | Gene Expression | Protein Purification | Structure |
Resumo
I am interested in the study of a class of antioxidant enzymes named peroxiredoxins. The peroxiredoxin active site is very conserved and contain a cysteine residue. Many peroxiredoxins were associated with physiological processes. The relationship between these physiological processes and the antioxidant activity of peroxiredoxin is unknown. The role of peroxiredoxins in yeast cells has been studied because it is a model for studying higher eucaryotes that is very amenable to genetic manipulations. One point that has attract our attention is the great number of peroxidd - decomposing enzymes in eucaryotic cells. Among various of those enzymes, five peroxiredoxins isoforms were identified in yeast. Each enzyme may have a particular role in a specific place and/our situation. Alternatively, these proteins may possess different substrate specificities. For some peroxiredoxins it was shown that thioredoxin is the reductant substrate but for others the thiol substrate is still unknown. It would be interesting the determination of the structure of the thioredoxin binding domain of these peroxidases. We have already cloned the genes, overexpressed and purified the recombinant proteins for three peroxiredoxins isoforms. The determination of cTPx I, cTPx II and mTPx I tertiary structure may reveal more details about mechanistic aspects of thioredoxin - peroxiredoxin interactíon. (AU)
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