Multiple lysine methylation of PCAF by Set9 methyltransferase.
Multiple lysine methylation of PCAF by Set9 methyltransferase.
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DOI：
10.1016/j.bbrc.2009.01.185
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发表时间：
2009-03
影响因子：
3.1
通讯作者：
T. Masatsugu;Ken Yamamoto
中科院分区：
文献类型：
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作者：
T. Masatsugu;Ken Yamamoto
几种非组蛋白的分子功能通过组蛋白甲基转移酶的赖氨酸修饰来调节。 p300/CBP 相关因子 (PCAF) 是一种乙酰转移酶，与许多细胞过程有关。在这里，我们报道 PCAF 是 Set9 甲基转移酶的新型底物。体外作图实验表明，Set9 可以甲基化 6 个赖氨酸残基。目标位点氨基酸序列的比较揭示了与先前鉴定的 Set9 共有序列不同的新共有基序。针对六个赖氨酸残基的进一步甲基转移酶测定表明，K78 和 K89 在体外全长 PCAF 中优先甲基化。使用识别单甲基化 K89 的特异性抗体，证明了体内 PCAF 甲基化及其核定位。我们的数据可能会带来对 PCAF 功能的新见解，并提供额外信息来识别 Set9 的未知目标。
The molecular functions of several non-histone proteins are regulated through lysine modification by histone methyltransferases. The p300/CBP-associated factor (PCAF) is an acetyltransferase that has been implicated in many cellular processes. Here, we report that PCAF is a novel substrate of Set9 methyltransferase. In vitro mapping experiments revealed six lysine residues could be methylated by Set9. A comparison of amino acid sequences of target sites revealed the novel consensus motif which differs from previously identified Set9-consensus sequence. Further methyltransferase assays focusing on the six lysine residues showed that K78 and K89 are preferentially methylated in full-length PCAF in vitro. Using specific antibodies recognizing mono-methylated K89, in vivo PCAF methylation and its nuclear localization were demonstrated. Our data may lead to a new insight into PCAF functions and provide additional information to identify unknown targets of Set9.