p300-mediated Acetylation of Human Transcriptional Coactivator PC4 Is Inhibited by Phosphorylation
| Autor: | B. R. Prashanth Kumar, V. Swaminathan, Tapas K. Kundu, Sourav Banerjee |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Transcription Genetic Cell Cycle Proteins Protein Serine-Threonine Kinases Biochemistry Immediate-Early Proteins Histones Mice Acetyltransferases Coactivator Animals Humans p300-CBP Transcription Factors Phosphorylation Casein Kinase II Molecular Biology Histone Acetyltransferases Cell Nucleus Chemistry Lysine Membrane Proteins Acetylation Cell Biology Recombinant Proteins Repressor Proteins Nuclear receptor coactivator 1 Nuclear receptor coactivator 3 Trans-Activators Nuclear receptor coactivator 2 bacteria PPARGC1A Casein kinase 2 HeLa Cells Transcription Factors |
| Zdroj: | Journal of Biological Chemistry. 276:16804-16809 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m100934200 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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