CHARACTERIZATION OF A HMG2-LIKE PROTEIN FROM SCHISTOSOMA-MANSONI

被引：6

作者：

FANTAPPIE, MR

RUMJANEK, FD

机构：

[1] Departamento de Bioquímica Médica ICB/CCS, Universidade Federal do Rio de Janeiro, Cidade Universitária, Ilha do Fundão, CP 68041, CEP 21910, Rio de Janeiro R.J.

来源：

PARASITOLOGY | 1994年 / 108卷

关键词：

SCHISTOSOMA MANSONI; HMG PROTEINS; DNA BINDING;

D O I：

10.1017/S0031182000078501

中图分类号：

R38 [医学寄生虫学]; Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ; 100103 ;

摘要：

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 P-32 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.

引用

页码：43 / 50

页数：8

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