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Presence of an unusually high concentration of an ubiquitinated histone‐like protein in Trypanosoma cruzi
Author(s) -
Reverol Lorena,
Chirinos Mayel,
Henriquez Diana A.
Publication year - 1997
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(19970915)66:4<433::aid-jcb2>3.0.co;2-m
Subject(s) - chromatin , histone , histone h2b , histone h1 , ubiquitin , acetylation , histone h2a , microbiology and biotechnology , biochemistry , chemistry , biology , dna , gene
The conjugation of ubiquitin to histones H2A and H2B has been established in higher eukaryotes and has been related to changes in chromatin organization. In Trypanosoma cruzi, no condensation of chromatin occurs during mitosis. In order to determine the presence of histone ubiquitination in T. cruzi epimastigotes, histones were extracted from chromatin and analyzed by three electrophoretic systems: acid‐urea, triton‐acid‐urea and sodium‐dodecyl‐sulphate polyacrylamide gel. The immunochemical detection of ubiquitin‐histone conjugates by Western blotting showed a strong reaction with a slow migrating band of M r 19 kDa. The high percentage of ubiquitin‐histone conjugates present in T. cruzi chromatin may be related to the inability of this parasite to condense chromatin into a 30 nm fiber. J. Cell. Biochem. 66:433–440, 1997. © 1997 Wiley‐Liss, Inc.