dc.creatorToro, G. Cecilia
dc.creatorWernstedt, Christer
dc.creatorAreche Medina, Carlos
dc.creatorJaramillo, Nicolás
dc.creatorHellman, Ulf
dc.creatorGalanti Garrone, Norbel
dc.date.accessioned2019-01-29T14:52:18Z
dc.date.available2019-01-29T14:52:18Z
dc.date.created2019-01-29T14:52:18Z
dc.date.issued1992
dc.identifierJournal of Cellular Biochemistry, Volumen 49, Issue 3, 2018, Pages 266-271
dc.identifier10974644
dc.identifier07302312
dc.identifier10.1002/jcb.240490309
dc.identifierhttp://repositorio.uchile.cl/handle/2250/161079
dc.description.abstractTrypanosoma cruzi presents six histones electrophoretically resolved in three gel systems. Indirect evidence shows that one of these histones, name, corresponds to H4 in other species. We present evidence that histones is H4 by sequencing its amino terminal end. The amino terminal of T. cruzi histone H4, unlike that of other H4s examined thus far is not blocked. Moreover, this protein presents two variants. This partial amino acid sequence of T. cruzi histone H4 differs greatly from homologous sequences of human, yeast, or Tetrahymena. Since the conservatism of the core histones (H2A, H2B, H3, and H4) is clearly illustrated by comparative sequence analyses, the data shown here demonstrates that T. cruzi histone H4 is the most divergent reported. Quantitative analysis of the data suggests that the rate of substitutions in the histone H4 amino terminal sequence varies among different lineages. We postulate a slow‐down in the evolutionary rate of histone H4 amino terminal domain in the me
dc.languageen
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
dc.sourceJournal of Cellular Biochemistry
dc.subjectamino terminal domain
dc.subjectchromatin
dc.subjectevolution
dc.subjecthistone H4
dc.subjectmolecular clock
dc.titleExtremely divergent histone H4 sequence from trypanosoma cruzi: Evolutionary implications
dc.typeArtículos de revistas


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