Properties of the histones and functional aspects of the soluble chromatin of epimastigote Trypanosoma cruzi

被引:14
作者
Schlimme, W [1 ]
Burri, M [1 ]
Betschart, B [1 ]
Hecker, H [1 ]
机构
[1] SWISS TROP INST,CH-4002 BASEL,SWITZERLAND
关键词
Trypanosoma cruzi; epimastigote forms; chromatin; histone H1; dissociation; reconstitution; amino acid analysis;
D O I
10.1016/0001-706X(95)00121-T
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
The amino acid composition of all histones of Trypanosoma cruzi was analyzed, and the terminology of the histones of higher eukaryotes adopted. One chromatin associated protein, previously considered to be a variant of histone H1, could not be clearly identified, and shows features of core histones as well as of histone H1. An improved method for the isolation of intact nuclei and the production of soluble chromatin in T. cruzi was established. The chromatin of T. cruzi is relatively instable and histone H1 is easily lost during experimental manipulations. Histone H1 dissociates completely at a relatively low NaCl concentration of 380 mM, leading to an open nucleosome filament which does not condense. The influence of histone H1 of T. cruzi and of rat liver on the compaction pattern of the chromatin was investigated by homologous and heterologous reconstitution experiments, and analysed by electron microscopy. It could be shown that histone H1 of T. cruzi induces nucleosome filaments of T. cruzi as well as those of rat liver to condense. The same is true for histone H1 of rats. It can be concluded that T. cruzi has a functional histone H1.
引用
收藏
页码:141 / 154
页数:14
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