Linker histone tails and N-tails of histone H3 are redundant: scanning force microscopy studies of reconstituted fibers.
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.
Leuba
S H
SH
Institute of Molecular Biology, University of Oregon, Eugene 97403-1229, USA.
Bustamante
C
C
van Holde
K
K
Zlatanova
J
J
D000818:Animals; D002645:Chickens; D002843:Chromatin / Q000378:metabolism / Q000648:ultrastructure*; D004247:DNA / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D004912:Erythrocytes / Q000648:ultrastructure; D006657:Histones / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure*; D018625:Microscopy, Atomic Force / Q000379:methods; D008958:Models, Molecular; D009707:Nucleosomes / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure
D002843:Chromatin; D006657:Histones; D009707:Nucleosomes; D004247:DNA