Modulation of the higher-order folding of chromatin by deletion of histone H3 and H4 terminal domains.
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.
Krajewski
W A
WA
Department of Biochemistry and Microbiology, University of Victoria, BC, Canada.
Ausió
J
J
D002467:Cell Nucleus / Q000737:chemistry; D002843:Chromatin / Q000737:chemistry*; D004247:DNA / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D004996:Ethidium / Q000494:pharmacology; D006367:HeLa Cells; D006657:Histones / Q000737:chemistry*; D006801:Humans; D007364:Intercalating Agents / Q000494:pharmacology; D008836:Micrococcal Nuclease / Q000378:metabolism; D009690:Nucleic Acid Conformation; D009707:Nucleosomes / Q000737:chemistry; D017510:Protein Folding; D014357:Trypsin / Q000378:metabolism
D002843:Chromatin; D006657:Histones; D007364:Intercalating Agents; D009707:Nucleosomes; D004247:DNA; D008836:Micrococcal Nuclease; D014357:Trypsin; D004996:Ethidium