Title
Contributions of linker histones and histone H3 to chromatin structure: Scanning force microscopy studies on trypsinized fibers
Date Issued
01 January 1998
Access level
open access
Resource Type
journal article
Author(s)
Leuba S.
Zlatanova J.
Van Holde K.
University of Oregon
Publisher(s)
Biophysical Society
Abstract
Little is known about the mechanisms that organize linear arrays of nucleosomes into the three-dimensional structures of extended and condensed chromatin fibers. We have earlier defined, from scanning force microscopy (SFM) and mathematical modeling, a set of simple structural determinants of extended fiber morphology, the critical parameters being the entry-exit angle between consecutive linkers and linker length. Here we study the contributions of the structural domains of the linker histones (LHs) and of the N-terminus of histone H3 to extended fiber morphology by SFM imaging of progressively trypsinized chromatin fibers. We find that cleavage of LH tails is associated with a lengthening of the internucleosomal center-to-center distance, and that the somewhat later cleavage of the N-terminus of histone H3 is associated with a flattening of the fiber. The persistence of the 'zigzag' fiber morphology, even at the latest stages of trypsin digestion, can be attributed to the retention of the globular domain of LH in the fiber.
Start page
2823
End page
2829
Volume
74
Issue
6
Language
English
OCDE Knowledge area
Biofísica
Scopus EID
2-s2.0-0031806540
PubMed ID
Source
Biophysical Journal
ISSN of the container
00063495
Sponsor(s)
This work is supported by National Institutes of Health grants GM50276 to KvH and JZ, GM32543 to CB, and a National Institutes of Health Postdoctoral Fellowship 1F32GM16600 to SHL. Some images from this work can be viewed at .
Sources of information: Directorio de Producción Científica Scopus