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Characterization of a HMG2-like protein from Schistosoma mansoni

Published online by Cambridge University Press:  06 April 2009

M. R. Fantappié  and
F. D. Rumjanek
M. R. Fantappié
Affiliation:
Departamento de Bioquímica Médico ICB/CCS, Universidade Federal do Rio de Janeiro, Cidade Universitária, Ilha do Fundão, CP 68041, CEP 21910, Rio de Janeiro R.J., Brasil
F. D. Rumjanek
Affiliation:
Departamento de Bioquímica Médico ICB/CCS, Universidade Federal do Rio de Janeiro, Cidade Universitária, Ilha do Fundão, CP 68041, CEP 21910, Rio de Janeiro R.J., Brasil
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Summary

An HMG2-like protein was purified from nuclear extracts of adult Schistosoma mansoni. Investigation of the amino acid composition of the schistosome HMG2-like protein showed that glutamic acid, glycine, aspartic acid and lysine were the most abundant. Carbohydrate analysis showed that the HMG2-like protein presented a low degree of glycosylation, galactose or glucose being the major monosaccharide constituent. Incubation of live schistosomes with 32P followed by isolation of nuclear proteins showed that the HMG-2 like protein could be phosphorylated. Partial sequence analysis of cyanogen bromide peptides revealed the occurrence of a phosphorylation consensus motif. The schistosome HMG2-like protein was found to bind preferentially to single-stranded DNA. The results suggest that the major non-histone S. mansoni nuclear protein belongs to the HMG family.

Keywords

Schistosoma mansoniHMG proteinsDNA binding
Type
Research Article
Information
Parasitology , Volume 108 , Issue 1 , January 1994 , pp. 43 - 50
Copyright
Copyright © Cambridge University Press 1994

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