title: Linker DNA bending induced by the core histones of chromatin.
abstract: We have previously reported that ionic conditions that stabilize the folding of long chromatin into 30-nm filaments cause linker DNA to bend, bringing the two nucleosomes of a dinucleosome into contact [Yao, J., Lowary, P. T., & Widom, J. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 7603-7607]. Dinucleosomes are studied because they allow the unambiguous detection of linker DNA bending through measurement of their nucleosome-nucleosome distance. Because of the large resistance of DNA to bending, the observed compaction must be facilitated by the histones. We have now tested the role of histone H1 (and its variant, H5) in this process. We find that dinucleosomes from which the H1 and H5 have been removed are able to compact to the same extent as native dinucleosomes; the transition is shifted to higher salt concentrations. We conclude that histone H1 is not essential for compacting the chromatin filament. However, H1 contributes to the free energy of compaction, and so it may select a single, ordered, compact state (the 30-nm filament, in long chromatin) from a family of compact states which are possible in its absence.
authors.affiliation: Department of Chemistry, University of Illinois, Urbana 61801.
authors.forename: J
authors.initials: J
authors.lastname: Yao
authors.forename: P T
authors.initials: PT
authors.lastname: Lowary
authors.forename: J
authors.initials: J
authors.lastname: Widom
mesh_terms: D000818:Animals; D002645:Chickens; D002843:Chromatin / Q000737:chemistry* / Q000302:isolation & purification; D004247:DNA / Q000737:chemistry*; D006657:Histones / Q000235:genetics*; D009690:Nucleic Acid Conformation; D009707:Nucleosomes / Q000737:chemistry; D013816:Thermodynamics
chemical_list: D002843:Chromatin; D006657:Histones; D009707:Nucleosomes; D004247:DNA