文摘
Histone H1 proteins bind to DNA and are important in formation and maintenance of chromatinstructure. Little is known about differences among variant H1 histones in their interactions with DNA.We examined the effects of histones H10 and H1t on thermal denaturation of several DNA species. Oneof the DNA molecules was a 214-base-pair fragment from the plasmid pBR322, which contains an AT-rich and a GC-rich region. Both H10 and H1t bound preferentially to one region of the DNA fragment,a region that is relatively GC-rich. This result indicates that histones H10 and H1t are not totally nonspecificbut rather bind with some sequence preference to DNA. This conclusion was supported by studies ofother 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 thatthe binding preference was not simple preference for GC base pairs. The binding of the two H1 variantswas not identical: there appear to be differences in binding site sizes, affinities, and sequence selectivitiesbetween H1t and H10.