Sequence preference of mouse H1(0) and H1t.
Histone H1 proteins bind to DNA and are important in formation and maintenance of chromatin structure. Little is known about differences among variant H1 histones in their interactions with DNA. We examined the effects of histones H1(0) and H1t on thermal denaturation of several DNA species. One of the DNA molecules was a 214-base-pair fragment from the plasmid pBR322, which contains an AT-rich and a GC-rich region. Both H1(0) and H1t bound preferentially to one region of the DNA fragment, a region that is relatively GC-rich. This result indicates that histones H1(0) and H1t are not totally nonspecific but rather bind with some sequence preference to DNA. This conclusion was supported by studies of other DNA species, including two 92-base-pair fragments derived from the two regions of the 214-mer, and several synthetic homocopolymers of DNA. Data obtained with the homocopolymers suggested that the binding preference was not simple preference for GC base pairs. The binding of the two H1 variants was not identical: there appear to be differences in binding site sizes, affinities, and sequence selectivities between H1t and H1(0).
Wellman
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SE
Department of Pharmacology and Toxicology, University of Mississippi Medical Center, Jackson 39216-4505, USA. swellman@pharmacology.umsmed.edu
Song
Y
Y
Mamoon
N M
NM
D000818:Animals; D001482:Base Composition; D020029:Base Pairing; D001483:Base Sequence; D001665:Binding Sites; D004268:DNA-Binding Proteins / Q000737:chemistry*; D004926:Escherichia coli; D006657:Histones / Q000737:chemistry*; D051379:Mice; D008956:Models, Chemical; D009691:Nucleic Acid Denaturation; D009838:Oligodeoxyribonucleotides / Q000737:chemistry; D011119:Polynucleotides / Q000737:chemistry
D004268:DNA-Binding Proteins; D006657:Histones; D009838:Oligodeoxyribonucleotides; D011119:Polynucleotides; C024063:nuclear protein H1(0)