Abstract
The mechanisms responsible for organizing linear arrays of nucleosomes into the three-dimensional structure of chromatin are still largely unknown. In a companion paper (Leuba, S. H., et al. 1998. Biophys. J. 74:2823-2829), we study the contributions of linker histone domains and the N-terminal tail of core histone H3 to extended chromatin fiber structure by scanning force microscopy imaging of mildly trypsinized fibers. Here we complement and extend these studies by scanning force microscopy imaging of selectively reconstituted chromatin fibers, which differ in subtle but distinctive ways in their histone composition. We demonstrate an absolute requirement for the globular domain of the linker histones and a structural redundancy of the tails of linker histones and of histone H3 in determining conformational stability.
MeSH Terms
Animals
Chickens
Chromatin/metabolism,ultrastructure
DNA/chemistry,metabolism,ultrastructure
Erythrocytes/ultrastructure
Histones/chemistry,metabolism,ultrastructure
Microscopy, Atomic Force/methods
Models, Molecular
Nucleosomes/chemistry,metabolism,ultrastructure
Chemicals
Chromatin
Histones
Nucleosomes
DNA
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Leuba S H
Institute of Molecular Biology, University of Oregon, Eugene 97403-1229, USA.
Bustamante C
van Holde K
Zlatanova J
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