Postsynthetic modification of high mobility group proteins. Evidence that high mobility group proteins are acetylated.
High mobility group proteins were isolated from calf thymus and duck erythrocyte nuclei and the possibility was investigated that these proteins undergo acetylation similar to that occurring in some histones. Dinitrophenylation of the proteins followed by acid hydrolysis and amino acid analysis indicated that 2 to 3% of the lysine residues present were unavailable for reaction with fluorodinitrobenzene. Extensive enzymatic degradation with trypsin and pronase and subsequent amino acid analysis showed a significant amount of material eluting at the position of epsilon-N-acetyllysine. Recovery and acid hydrolysis of this material generated a peak eluting in the lysine position. In vitro radioactive labeling of calf thymus nuclei with [3H]acetate yielded labeled high mobility group proteins. All of these findings are in accord with the conclusion that high mobility group proteins are acetylated and that acetylation occurs as a postsynthetic modification of these proteins.
D000107:Acetylation; D000818:Animals; D001798:Blood Proteins / Q000378:metabolism*; D002417:Cattle; D004140:Dinitrophenols; D004372:Ducks; D004912:Erythrocytes / Q000378:metabolism*; D008970:Molecular Weight; D011506:Proteins / Q000378:metabolism*; D013950:Thymus Gland / Q000378:metabolism*
D001798:Blood Proteins; D004140:Dinitrophenols; D011506:Proteins