A putative DNA binding surface in the globular domain of a linker histone is not essential for specific binding to the nucleosome.
A fundamental step in the assembly of native chromatin is the specific recognition and binding of linker histones to the nucleoprotein subunit known as the nucleosome. A first step in defining this important interaction is the determination of residues within linker histones that are important for the structure-specific recognition of the nucleosome core. By combining in vitro assays for the native binding activity of linker histones and site-directed mutagenesis, we have examined a cluster of basic residues within the globular domain of H1(0), a somatic linker histone variant from Xenopus laevis. We show that these residues, which comprise a putative DNA binding surface within the globular domain, do not play an essential role in the structure-specific binding of a linker histone to the nucleosome.
Hayes
J J
JJ
Department of Biochemistry, University of Rochester Medical Center, Rochester, New York 14642, USA.
Kaplan
R
R
Ura
K
K
Pruss
D
D
Wolffe
A
A
D000818:Animals; D001665:Binding Sites; D004247:DNA / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D008836:Micrococcal Nuclease / Q000378:metabolism; D009707:Nucleosomes / Q000378:metabolism*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000378:metabolism; D013329:Structure-Activity Relationship; D014982:Xenopus laevis
D006657:Histones; D009707:Nucleosomes; D011994:Recombinant Proteins; D004247:DNA; D008836:Micrococcal Nuclease; D010450:Endopeptidases