L. Reverol et al., PRESENCE OF AN UNUSUALLY HIGH-CONCENTRATION OF AN UBIQUITINATED HISTONE-LIKE PROTEIN IN TRYPANOSOMA-CRUZI, Journal of cellular biochemistry, 66(4), 1997, pp. 433-440
The conjugation of ubiquitin to histones H2A and H2B has been establis
hed in higher eukaryotes and has been related to changes in chromatin
organization. In Trypanosoma cruzi, no condensation of chromatin occur
s during mitosis. In order to determine the presence of histone ubiqui
tination in T. cruzi epimastigotes, histones were extracted from chrom
atin and analyzed by three electrophoretic systems: acid-urea, triton-
acid-urea and sodium-dodecylsulphate polyacrylamide gel. The immunoche
mical detection of ubiquitin-histone conjugates by Western blotting sh
owed a strong reaction with a slow migrating band of M-r 19 kDa. The h
igh percentage of ubiquitin-histone conjugates present in T. cruzi chr
omatin may be related to the inability of this parasite to condense ch
romatin into a 30 nm fiber. (C) 1997 Wiley-Liss, Inc.