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Modulation of the higher-order folding of chromatin by deletion of histone H3 and H4 terminal domains.


ABSTRACT: The 'tails' of histones H3 and H4 were removed by light in situ trypsin digestion of the nuclei. The alterations in the higher-order folding of chromatin resulting from this treatment were monitored by ethidium bromide titration. We found that DNA-intercalation of ethidium bromide under these conditions exhibited a complex concentration effect that was dependent on the extent of chromatin folding. This most likely reflects the structural transitions of chromatin during its folding as a result of the changes in the nucleosome linker twist [Woodcock, Grigoryev, Horowitz and Whitaker (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 9021-9025]. These results strongly suggest that the H3 and H4 terminal domains play a very important role in chromatin folding. We discuss the molecular basis of this phenomenon and propose a novel generalized model for the higher-order folding of chromatin.

SUBMITTER: Krajewski WA 

PROVIDER: S-EPMC1217363 | BioStudies | 1996-01-01

SECONDARY ACCESSION(S): 10.1042/bj3160395

REPOSITORIES: biostudies

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