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首页> 外文期刊>Molecular cell >Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase.
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Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase.

机译:组蛋白H3-赖氨酸4特异性甲基转移酶的纯化和功能表征。

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摘要

Methylation of histone H3 at lysine 9 by SUV39H1 and subsequent recruitment of the heterochromatin protein HP1 has recently been linked to gene silencing. In addition to lysine 9, histone H3 methylation also occurs at lysines 4, 27, and 36. Here, we report the purification, molecular identification, and functional characterization of an H3-lysine 4-specific methyltransferase (H3-K4-HMTase), SET7. We demonstrate that SET7 methylates H3-K4 in vitro and in vivo. In addition, we found that methylation of H3-K4 and H3-K9 inhibit each other. Furthermore, H3-K4 and H3-K9 methylation by SET7 and SUV39H1, respectively, have differential effects on subsequent histone acetylation by p300. Thus, our study provides a molecular explanation to the differential effects of H3-K4 and H3-K9 methylation on transcription.
机译:SUV39H1使赖氨酸9处的组蛋白H3甲基化,并随后募集异染色质蛋白HP1与基因沉默相关。除了赖氨酸9外,组蛋白H3甲基化还发生在赖氨酸4、27和36处。在这里,我们报道了H3-赖氨酸4特异性甲基转移酶(H3-K4-HMTase)的纯化,分子鉴定和功能表征, SET7。我们证明SET7甲基化H3-K4在体外和体内。另外,我们发现H3-K4和H3-K9的甲基化彼此抑制。此外,SET7和SUV39H1分别对H3-K4和H3-K9进行甲基化,对随后的p300组蛋白乙酰化具有不同的影响。因此,我们的研究为H3-K4和H3-K9甲基化对转录的不同作用提供了分子解释。

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