Characterization of a HMG2-like protein from Schistosoma mansoni.
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.
Fantappié
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Departamento de Bioquímica Médica ICB/CCS, Universidade Federal do Rio de Janeiro, Cidade Universitária, Brasil.
Rumjanek
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D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis*; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D004277:DNA, Single-Stranded / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006031:Glycosylation; D015801:Helminth Proteins / Q000737:chemistry* / Q000378:metabolism; D006868:Hydrolysis; D008297:Male; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry* / Q000378:metabolism; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D012550:Schistosoma mansoni / Q000737:chemistry* / Q000235:genetics; D017386:Sequence Homology, Amino Acid
D000596:Amino Acids; D002241:Carbohydrates; D004277:DNA, Single-Stranded; D015801:Helminth Proteins; D009687:Nuclear Proteins