Acetylated HMG1 protein interacts specifically with homologous DNA polymerase alpha in vitro.
The acetylated, deacetylated and nonacetylated forms of HMG1 proteins from Guerin ascites tumour cells and calf thymus were separated and their in vitro interactions with homologous and heterologous DNA polymerases were studied. It has been found that only the acetylated form of HMG1 proteins forms a specific complex with homologous DNA polymerase alpha and stimulates its activity in vitro. The acetylation therefore is necessary for their possible function in DNA replication. This finding represents an evidence for a relationship between the acetylation of HMG1 proteins and their biological role.
D000107:Acetylation; D000818:Animals; D004257:DNA Polymerase II / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology; D006609:High Mobility Group Proteins / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D009374:Neoplasms, Experimental / Q000201:enzymology; D009994:Osmolar Concentration; D011485:Protein Binding; D051381:Rats; D013950:Thymus Gland / Q000378:metabolism
D006609:High Mobility Group Proteins; D004257:DNA Polymerase II