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Interaction of the HMG1 protein with nucleic acids
Author(s) -
Shepelev V.A.,
Kosaganov Yu.N.,
Lazurkin Yu.S.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81120-5
Subject(s) - polynucleotide , nucleic acid , dna , chemistry , denaturation (fissile materials) , ionic strength , size exclusion chromatography , ionic bonding , biophysics , biochemistry , ion , organic chemistry , nuclear chemistry , biology , aqueous solution , enzyme
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) ∞ poly(A) < poly(dA) < dsDNA ∞ poly(dA) · poly(dT) ∞ poly(dG) · poly(dC) « poly[d(A‐T)] ∞ ssDNA.