Interaction of the HMG1 protein with nucleic acids.
Binding constants have been measured for the interaction of the protein HMG1 with native DNA, denatured DNA and a number of polynucleotides at near-physiological ionic strengths, using gel filtration and thermal denaturation. The interaction of HMG1 with DNA is shown to be noncooperative and reversible. Nucleic acids form the following series in order of increasing binding constants: poly(U) integral of poly(A) less than poly(dA) less than dsDNA integral of poly(dA) X poly(dT) integral of poly(dG) X poly(dC) much less than poly[d(A-T]) integral of ssDNA.
D000818:Animals; D002417:Cattle; D002645:Chickens; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism*; D004247:DNA / Q000378:metabolism*; D004277:DNA, Single-Stranded / Q000378:metabolism; D004279:DNA, Viral / Q000378:metabolism; D006609:High Mobility Group Proteins; D006358:Hot Temperature; D009691:Nucleic Acid Denaturation; D009994:Osmolar Concentration; D011089:Polydeoxyribonucleotides / Q000378:metabolism*; D011485:Protein Binding; D013604:T-Phages
D002868:Chromosomal Proteins, Non-Histone; D004277:DNA, Single-Stranded; D004279:DNA, Viral; D006609:High Mobility Group Proteins; D011089:Polydeoxyribonucleotides; D004247:DNA