Binding of protein uH2A and histone H2A to DNA.
The binding properties of protein uH2A and histone H2A to DNA were investigated by filter binding assays. Both proteins revealed similar affinity for native and denatured DNA. Competition with increasing amounts of repetitive and nonrepetitive DNA has shown that protein uH2A binds selectively to nonrepetitive sequences. When poly d(A-T) was used as a competitor, uH2A bound to this polynucleotide with much greater affinity than histone H2A. These findings suggest a selective binding to regulatory A-T rich intergenic sequences in native DNA.
Kirdar
B
B
Biology Department, Bogazici University, Bebek, Istanbul.
Dalay
N
N
Bermek
E
E
D000818:Animals; D002417:Cattle; D002843:Chromatin / Q000378:metabolism; D004247:DNA / Q000378:metabolism*; D006657:Histones / Q000378:metabolism* / Q000502:physiology; D011485:Protein Binding; D013950:Thymus Gland / Q000166:cytology / Q000648:ultrastructure; D014452:Ubiquitins / Q000378:metabolism* / Q000502:physiology
D002843:Chromatin; D006657:Histones; D014452:Ubiquitins; C021645:chromatin conjugate protein A24; D004247:DNA