Interaction of the HMG1 protein with nucleic acids

FEBS Letters

Kosaganov, Yu.N.¹  Shepelev, V.A.¹  Lazurkin, Yu.S.¹ 

[1] Institute of Molecular Genetics, USSR Academy of Sciences, 46 Kurchatov Sq., Moscow 123182. USSR

关键词: Nonhistone protein HMG1;    DNA binding;    Gel filtration;    DNA melting;    ssDNA;    single-stranded DNA;    dsDNA;    double-stranded DNA;    HMG1;    high mobility group protein 1;   

DOI  :  10.1016/0014-5793(84)81120-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown