The function of lysine-methylated PCAF molecule

存在几种靶向组蛋白分子的甲基转移酶（HMTase）。我们之前报道了一种HMTase， Set9，甲基化p300/ cbp相关因子（PCAF）的多个赖氨酸残基。为了阐明这种PCAF甲基化的生物学相关性，我们检测了甲基化导致的PCAF功能变化。我们发现赖氨酸甲基化不会改变PCAF的稳定性和自乙酰化；然而，这种修饰使其对P53和组蛋白H3分子的乙酰化活性受损。我们的研究结果暗示了一种新的转录途径，包括Set9和PCAF通过多个赖氨酸甲基化。

There exist several methyltransferases targeting histone molecules (HMTase). We previously reported that one of HMTase, Set9, methylates multiple lysine residues of p300/CBP-associated factor (PCAF). To elucidate biological relevance of this PCAF methylation, we examined functional change of PCAF cased by methylation. We found that lysine methylation did not alter stability and self-acethylation of PCAF; however, its acethylation activity to P53 and histone H3 molecules was impaired by this modification. Our results implicate a novel transcription pathway including Set9 and PCAF via multiple lysine methylation.