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Acetylation of MyoD by p300 Requires More Than Its Histone Acetyltransferase Domain

  • CNRS UPR 9079 Oncogénèse, Différenciation et Transduction du Signal

Research output: Contribution to journal › Article › peer-review

38 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)44502-44503
Number of pages2
JournalJournal of Biological Chemistry
Volume276
Issue number48
DOIs
Publication statusPublished - 30 Nov 2001

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