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

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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.

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Polesskaya, A., & Harel-Bellan, A. (2001). Acetylation of MyoD by p300 Requires More Than Its Histone Acetyltransferase Domain. Journal of Biological Chemistry, 276(48), 44502–44503. https://doi.org/10.1074/jbc.M106501200

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