期刊
MOLECULAR AND CELLULAR BIOLOGY
卷 25, 期 10, 页码 3997-4009出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.25.10.3997-4009.2005
关键词
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资金
- NCI NIH HHS [T32 CA09657, T32 CA009657] Funding Source: Medline
- NIAMS NIH HHS [R01 AR045113, AR045113] Funding Source: Medline
- NIGMS NIH HHS [R01 GM056244, GM56244] Funding Source: Medline
The activation of muscle-specific gene expression requires the coordinated action of muscle regulatory proteins and chromatin-remodeling enzymes. Microarray analysis performed in the presence or absence of a dominant-negative BRG1 ATPase demonstrated that approximately one-third of MyoD-induced genes were highly dependent on SWI/SNF enzymes. To understand the mechanism of activation, we performed chromatin immunoprecipitations analyzing the myogenin promoter. We found that H4 hyperacetylation preceded Brg1 binding in a MyoD-dependent manner but that MyoD binding occurred subsequent to H4 modification and Brg1 interaction. In the absence of functional SWI/SNF enzymes, muscle regulatory proteins did not bind to the myogenin promoter, thereby providing evidence for SWI/SNF-dependent activator binding. We observed that the homeodomain factor Pbx1, which cooperates with MyoD to stimulate myogenin expression, is constitutively bound to the myogenin promoter in a SWI/SNF-independent manner, suggesting a two-step mechanism in which MyoD initially interacts indirectly with the myogenin promoter and attracts chromatin-remodeling enzymes, which then facilitate direct binding by MyoD and other regulatory proteins.
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