Cromatin and core particles formed from the inner histones and synthetic polydeoxyribonucleotides of defined sequence.
Chicken erythrocyte inner histones (H2A, H2B, H3 and H4) were associated with the two complementary homopolymeric polydeoxyribonucleotides and the two alternating copolymeric polydeoxyribonucleotides. No evidence for formation of chromatin-like structures was obtained for the complexes with poly(dG) . poly(dC) or poly(dA) . poly(dT). Both poly (dGdC) . poly(dGdC) and poly(dAdT) . poly(dAdT) could be folded by histones to yield material digested by DNAase I to multiples of about 10 and by staphylococcal nuclease to 146 bp core particles. Due to the lack of sequence heterogeniety in the complex of histones with poly(dAdT) . poly(dAdT), core particles with remarkable fine structural detail are obtained. The internal organization of DNA in the AT-containing and GC-containing core particles appears not to be identical.
D000818:Animals; D001483:Base Sequence; D002467:Cell Nucleus / Q000032:analysis; D002645:Chickens; D002843:Chromatin / Q000648:ultrastructure*; D003852:Deoxyribonucleoproteins; D004912:Erythrocytes / Q000032:analysis; D006657:Histones / Q000097:blood; D009690:Nucleic Acid Conformation; D009691:Nucleic Acid Denaturation; D009698:Nucleoproteins; D011089:Polydeoxyribonucleotides; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D002843:Chromatin; D003852:Deoxyribonucleoproteins; D006657:Histones; D009698:Nucleoproteins; D011089:Polydeoxyribonucleotides