The interaction of high mobility proteins HMG14 and 17 with nucleosomes.
The interaction of the high mobility group proteins, HMG14 and HMG17, with nucleosome core particles has been studied. The results show that two molecules of HMG14/17 can be bound tightly but reversibly to each core particle and that their affinity for core particles is greater than their affinity for histone-free DNA of core size. Thermal denaturation and nuclease digestion studies suggest that major sites of interaction are located near the ends of the nucleosome core DNA. When nucleosome preparations from chicken erythrocyte nuclei stripped of HMG proteins are partially titrated with HMG14/17, the nucleosome-HMG complex fraction is enriched in beta-globin gene sequences.
D000818:Animals; D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism; D002645:Chickens; D002868:Chromosomal Proteins, Non-Histone / Q000097:blood*; D004247:DNA / Q000097:blood; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000378:metabolism; D006609:High Mobility Group Proteins; D007700:Kinetics; D009707:Nucleosomes / Q000378:metabolism*; D011485:Protein Binding
D002868:Chromosomal Proteins, Non-Histone; D006609:High Mobility Group Proteins; D009707:Nucleosomes; D004247:DNA