Interaction of high mobility group proteins HMG 1 and HMG 2 with nucleosomes studied by gel electrophoresis.
The binding of isolated high mobility group proteins HMG (1 + 2) with nucleosomes was studied using gel electrophoresis. The interaction of HMG (1 + 2) with mononucleosomes could be detected as a new discrete electrophoretic band with a decreased mobility only after cross-linking of HMG (1 + 2)-nucleosome complex by formaldehyde. Approximately two molecules of the large HMG proteins were bound per nucleosomal particle of a DNA length of approximately 185 base pairs, lacking histones H1 and H5. Using the same techniques, no binding was observed with core particles of a DNA length of approximately 145 base pairs.
D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism; D002645:Chickens; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D004912:Erythrocytes / Q000378:metabolism; D006609:High Mobility Group Proteins / Q000097:blood* / Q000302:isolation & purification; D006657:Histones / Q000097:blood; D008970:Molecular Weight; D009707:Nucleosomes / Q000378:metabolism*; D011485:Protein Binding
D006609:High Mobility Group Proteins; D006657:Histones; D009707:Nucleosomes