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F-10 nuclear binding proteins of Schistosoma mansoni: structural and functional features

Published online by Cambridge University Press:  06 April 2009

A. L. M. Giannini
Affiliation:
Departamento de Bioquímica Médica ICB/CCS, Universidade Federal do Rio de Janeiro, Cidade Universitária - Ilha do Fund´o, CP 68041 CEP 21941-590, Rio de Janeiro RJ, Brasil
E. C. Caride
Affiliation:
Departamento de Bioquímica Médica ICB/CCS, Universidade Federal do Rio de Janeiro, Cidade Universitária - Ilha do Fund´o, CP 68041 CEP 21941-590, Rio de Janeiro RJ, Brasil
V. M. Martin Braga
Affiliation:
Departamento de Bioquímica Médica ICB/CCS, Universidade Federal do Rio de Janeiro, Cidade Universitária - Ilha do Fund´o, CP 68041 CEP 21941-590, Rio de Janeiro RJ, Brasil
F. D. Rumjanek
Affiliation:
Departamento de Bioquímica Médica ICB/CCS, Universidade Federal do Rio de Janeiro, Cidade Universitária - Ilha do Fund´o, CP 68041 CEP 21941-590, Rio de Janeiro RJ, Brasil

Summary

By incubating total protein extracts of Schistosoma mansoni with 3H-17-β-estradiol and 20-hydroxyecdysone, steroid binding proteins were detected in both male and female worms. The interaction of nuclear proteins with a restriction fragment of the gender and stage-specific gene F-10 was investigated using the ‘band-shift’ technique. Male and female nuclear proteins bound in a distinct way to the fragment of this gene containing putative regulatory consensus motifs. Among the nuclear proteins, only those rich in cysteine residues bound to DNA. In vitro incubation of live worms with the oestrogen antagonist Tamoxifen, altered the pattern of the DNA binding proteins, producing in females a profile similar to that obtained with male worm protein extracts. This effect of Tamoxifen could not be correlated to inhibition of protein biosynthesis. These results suggest that the regulation of transcription of the F-10 gene might involve steroid receptors.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1995

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