Acetylation of MyoD by p300 requires more than its histone acetyltransferase domain.
MyoD, an essential transcription factor involved in muscle cell terminal differentiation, is regulated by acetylation, as are a number of other transcription factors, but the histone acetyltransferase enzyme responsible for this acetylation is a matter of controversy. In particular, contradictory findings have been reported concerning the ability of CBP/p300 to acetylate MyoD in vitro. Here we provide an explanation for this discrepancy: although full-length p300 does indeed acetylate MyoD, a fragment of p300 corresponding to its histone acetyltransferase domain does not. In addition to clearly demonstrating that p300 acetylates MyoD in vitro, these results underscore the necessity of using full-length histone acetyltransferase enzymes to draw valid conclusions from acetylation experiments.
Polesskaya
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CNRS UPR 9079, Institut André Lwoff, 7 Rue Guy Moquet, 94800 Villejuif, France.
Harel-Bellan
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D000123:Acetyltransferases / Q000378:metabolism*; D000596:Amino Acids / Q000737:chemistry; D006367:HeLa Cells; D051548:Histone Acetyltransferases; D006801:Humans; D017570:MyoD Protein / Q000378:metabolism*; D009687:Nuclear Proteins / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry; D011233:Precipitin Tests; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D015534:Trans-Activators / Q000378:metabolism*
D000596:Amino Acids; D017570:MyoD Protein; D009687:Nuclear Proteins; D010455:Peptides; D011994:Recombinant Proteins; D029701:Saccharomyces cerevisiae Proteins; D015534:Trans-Activators; D000123:Acetyltransferases; D051548:Histone Acetyltransferases