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Linker histone tails and N-tails of histone H3 are redundant: Scanning force microscopy studies of reconstituted fibers
Author(s): Leuba SH, Bustamante C, van Holde K, Zlatanova J
Source: BIOPHYSICAL JOURNAL    Volume: 74    Issue: 6    Pages: 2830-2839    Published: JUN 1998  
Times Cited: 51     References: 34     
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 at. 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.
Document Type: Article
Language: English
Reprint Address: Zlatanova, J (reprint author), Oregon State Univ, Dept Biochem & Biophys, Corvallis, OR 97331 USA
Addresses:
1. Oregon State Univ, Dept Biochem & Biophys, Corvallis, OR 97331 USA
2. Univ Oregon, Inst Mol Biol, Eugene, OR 97403 USA
3. Univ Oregon, Dept Chem, Eugene, OR 97403 USA
4. Univ Oregon, Howard Hughes Med Inst, Eugene, OR 97403 USA
5. Bulgarian Acad Sci, Inst Genet, BU-1113 Sofia, Bulgaria
Publisher: BIOPHYSICAL SOCIETY, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3998 USA
Subject Category: Biophysics
IDS Number: ZT214
ISSN: 0006-3495
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