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PMID: 9635737 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Linker histone tails and N-tails of histone H3 are redundant: scanning force microscopy studies of reconstituted fibers.

Biophysical journal ·Vol. 74 ·No. 6 ·1998-06-00 ·Pages 2830-9

Leuba SH, Bustamante C, van Holde K, Zlatanova J

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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Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
Published
1998-06-00
Pages
2830-9
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1299624
Subset
IM
Grants
NIGMS NIH HHS · 1F32GM16600 · United States
NIGMS NIH HHS · GM32543 · United States
NIGMS NIH HHS · GM50276 · United States
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