Acetylation of MyoD directed by PCAF is necessary for the execution of the muscle program

Vittorio Sartorelli, Pier Lorenzo Puri, Yasuo Hamamori, Vasily Ogryzko, Gene Chung, Yoshihiro Nakatani, Jean Y J Wang, Larry Kedes

Research output: Contribution to journalArticlepeer-review

Abstract

p300/CBP and PCAF coactivators have acetyltransferase activities and regulate transcription, cell cycle progression, and differentiation. They are both required for MyoD activity and muscle differentiation. Nevertheless, their roles must be different since the acetyltransferase activity of PCAF but not of p300 is involved in controlling myogenic transcription and differentiation. Here, we provide a molecular explanation of this phenomenon and report that MyoD is directly acetylated by PCAF at evolutionarily conserved lysines. Acetylated MyoD displays an increased affinity for its DNA target. Importantly, conservative substitutions of acetylated lysines with nonacetylatable arginines impair the ability of MyoD to stimulate transcription and to induce muscle conversion indicating that acetylation of MyoD is functionally critical.

Original languageEnglish
Pages (from-to)725-734
Number of pages10
JournalMolecular Cell
Volume4
Issue number5
Publication statusPublished - Nov 1999

ASJC Scopus subject areas

  • Molecular Biology

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