Preferential binding of H1e histone to GC-rich DNA.
We have investigated the binding of a pure H1 histone, the mouse variant H1e, to a 214 bp fragment of DNA from pBR322. Binding was monitored by observing the effects of the protein on melting of the DNA and by a gel-mobility-shift assay. We found, using this highly purified system, that H1e protein binds preferentially and cooperatively to the GC-rich region of the DNA. A chemically synthesized peptide containing 25 residues, corresponding to a region of the carboxyl-terminal domain of H1e, shows the same sequence preference but does not exhibit cooperativity.
Wellman
S E
SE
Department of Pharmacology and Toxicology, University of Mississippi Medical Center, Jackson 39216-4505.
Sittman
D B
DB
Chaires
J B
JB
D016475:3T3 Cells; D000595:Amino Acid Sequence; D000818:Animals; D001482:Base Composition; D002942:Circular Dichroism; D017124:Conserved Sequence; D003596:Cytosine; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D006147:Guanine; D006657:Histones / Q000737:chemistry* / Q000378:metabolism; D004915:Leukemia, Erythroblastic, Acute; D051379:Mice; D008969:Molecular Sequence Data; D009691:Nucleic Acid Denaturation; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D011489:Protein Denaturation; D014407:Tumor Cells, Cultured
D006657:Histones; D010446:Peptide Fragments; D006147:Guanine; D003596:Cytosine; D004247:DNA