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首页> 外文期刊>EMBO reports >Crystal structure of the N-terminal region of human Ash2L shows a winged-helix motif involved in DNA binding
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Crystal structure of the N-terminal region of human Ash2L shows a winged-helix motif involved in DNA binding

机译:人类Ash2L N末端区域的晶体结构显示参与DNA结合的有翼螺旋基序

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摘要

Ash2L is a core component of the MLL family histone methyltransferases and has an important role in regulating the methylation of histone H3 on lysine 4. Here, we report the crystal structure of the N-terminal domain of Ash2L and reveal a new function of Ash2L. The structure shows that Ash2L contains an atypical PHD finger that does not have histone tail-binding activity. Unexpectedly, the structure shows a previously unrecognized winged-helix motif that directly binds to DNA. The DNA-binding-deficient mutants of Ash2L reduced Ash2L localization to the HOX locus. Strikingly, a single mutation in Ash2L WH (K131A) breaks the chromatin domain boundary, suggesting that Ash2L also has a role in chromosome demarcation.
机译:Ash2L是MLL家族组蛋白甲基转移酶的核心组成部分,在调节赖氨酸4上组蛋白H3的甲基化中具有重要作用。在这里,我们报道Ash2L N端结构域的晶体结构,并揭示Ash2L的新功能。该结构表明,Ash2L包含不具有组蛋白尾部结合活性的非典型PHD手指。出乎意料的是,该结构显示了以前无法识别的直接与DNA结合的带翼螺旋基序。 Ash2L的DNA结合缺陷型突变体减少Ash2L定位到HOX基因座。令人惊讶的是,Ash2L WH(K131A)中的单个突变打破了染色质结构域边界,表明Ash2L在染色体分界中也有作用。

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