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 language | English |
|---|---|
| Pages (from-to) | 44502-44503 |
| Number of pages | 2 |
| Journal | Journal of Biological Chemistry |
| Volume | 276 |
| Issue number | 48 |
| DOIs | |
| Publication status | Published - 30 Nov 2001 |
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