Preferential affinity of high molecular weight high mobility group non-histone chromatin proteins for single-stranded DNA.
We have subjected proteins dissociated from chicken erythrocyte or calf thymus chromatin by 0.35 M NaCl to sequential chromatography on columns containing immobilized double-stranded DNA and single-stranded DNA. At 0.2 M NaCl, 1 mM Tris . Cl (pH 7.5), the high molecular weight, high mobility group proteins (HMG-1, HMG-2, and HMG-E), were not retained by double-stranded DNA columns, but were retained by single-stranded DNA columns. Thus, in that solvent, those proteins exhibit selective affinity for single-stranded DNA. This suggests that the functions of the high molecular weight, high mobility group proteins might involve destabilizing the DNA double helix by virtue of their preferential affinity for single-stranded DNA.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002352:Carrier Proteins; D002417:Cattle; D002645:Chickens; D002868:Chromosomal Proteins, Non-Histone / Q000302:isolation & purification; D004247:DNA; D004277:DNA, Single-Stranded; D003852:Deoxyribonucleoproteins; D004912:Erythrocytes / Q000032:analysis; D008970:Molecular Weight; D011485:Protein Binding; D013329:Structure-Activity Relationship; D013950:Thymus Gland / Q000032:analysis
D000596:Amino Acids; D002352:Carrier Proteins; D002868:Chromosomal Proteins, Non-Histone; D004277:DNA, Single-Stranded; D003852:Deoxyribonucleoproteins; D004247:DNA