p300-mediated acetylation of human transcriptional coactivator PC4 is inhibited by phosphorylation.
The human positive coactivator 4 (PC4) acts as a general coactivator for activator-dependent transcription, the activity of which is regulated negatively by phosphorylation. We report here that PC4 can be acetylated specifically by another coactivator, p300. Interestingly, phosphorylation of PC4 by casein kinase II inhibits the p300-mediated acetylation. Mass spectral ... analysis revealed that there are at least two lysine residues acetylated in PC4, as a result of which its DNA binding activity is stimulated.
Mesh Terms:
Acetylation, Acetyltransferases, Animals, Casein Kinase II, Cell Cycle Proteins, Cell Nucleus, Hela Cells, Histone Acetyltransferases, Histones, Humans, Immediate-Early Proteins, Lysine, Membrane Proteins, Mice, Phosphorylation, Protein-Serine-Threonine Kinases, Recombinant Proteins, Repressor Proteins, Saccharomyces cerevisiae Proteins, Trans-Activators, Transcription Factors, Transcription, Genetic, p300-CBP Transcription Factors
Acetylation, Acetyltransferases, Animals, Casein Kinase II, Cell Cycle Proteins, Cell Nucleus, Hela Cells, Histone Acetyltransferases, Histones, Humans, Immediate-Early Proteins, Lysine, Membrane Proteins, Mice, Phosphorylation, Protein-Serine-Threonine Kinases, Recombinant Proteins, Repressor Proteins, Saccharomyces cerevisiae Proteins, Trans-Activators, Transcription Factors, Transcription, Genetic, p300-CBP Transcription Factors
J. Biol. Chem.
Date: May. 18, 2001
PubMed ID: 11279157
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