Studies on the interaction of H1 histone with superhelical DNA: characterization of the recognition and binding regions of H1 histones.
The very lysine rich histone, H1, isolated from a variety of sources interacts preferentially with superhelical DNA compared to relaxed DNA duplexes. The nature of this specific interaction has been investigated by studying the ability of various purified fragments of H1 histone from calf thymus to recognize and bind superhelical DNA. The data suggest that the globular region of the H1 histone molecule (amino acid residues 72-106) is involved in the recognition of superhelical DNA. Thus, the H1 histone carboxy-terminal fragment, 72-212, resembles native H1 histone both quantitatively and qualitatively in its ability to discriminate between and bind to superhelical and relaxed DNA while the H1 histone carboxy-terminal fragment, residues 106-212, has lost this specificity, binding superhelical and relaxed DNA equally well. Furthermore, under conditions in which the globular region of the intact H1 histone has been unfolded, the molecule loses its ability to discriminate between superhelical and relaxed DNA, and binds both forms of DNA equally.
D000818:Animals; D001974:Bromosuccinimide; D002417:Cattle; D002918:Chymotrypsin; D004270:DNA, Circular / Q000378:metabolism*; D004279:DNA, Viral / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D009690:Nucleic Acid Conformation; D009994:Osmolar Concentration; D010455:Peptides / Q000378:metabolism; D011485:Protein Binding / Q000187:drug effects; D011487:Protein Conformation / Q000187:drug effects; D013539:Simian virus 40; D012965:Sodium Chloride / Q000494:pharmacology; D013329:Structure-Activity Relationship; D013950:Thymus Gland; D014508:Urea / Q000494:pharmacology
D004270:DNA, Circular; D004279:DNA, Viral; D006657:Histones; D010455:Peptides; D012965:Sodium Chloride; D014508:Urea; D002918:Chymotrypsin; D001974:Bromosuccinimide