Highly compacted chromatin formed in vitro reflects the dynamics of transcription activation in vivo.
Highly compacted chromatin formed in vitro reflects the dynamics of transcription activation in vivo.
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DOI：
10.1016/j.molcel.2010.01.042
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发表时间：
2010-04-09
期刊：
影响因子：
16
通讯作者：
Reinberg D
中科院分区：
文献类型：
--
作者：
Li G;Margueron R;Hu G;Stokes D;Wang YH;Reinberg D
High order chromatin was reconstituted in vitro. This species reflects the criteria associated with transcriptional regulation in vivo. Histone H1 was determinant to formation of condensed structures, with deacetylated histones giving rise to highly compacted chromatin that approximated 30-nm fibers as evidenced by electron microscopy. Using the model PEPCK promoter, we validated the integrity of these templates that were refractory to transcription by attaining transcription through the progressive action of the pertinent factors. The retinoic acid receptor binds to highly compacted chromatin, but the NF1 transcription factor binds only after histone acetylation by p300 and SWI/SNF-mediated nucleosome mobilization, reflecting the in vivo case, as evidenced by ChIP analyses. Mapping studies revealed the same pattern of nucleosomal repositioning on the PEPCK promoter in vitro and in vivo, correlating with NF1 binding and transcription. The reconstitution of such highly compacted “30-nm” chromatin that mimics in vivo characteristics should advance studies of its conversion to a transcriptionally active form, as well as the relevant function(s) of histone posttranslational modifications.
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