PDF(Pubmed)
Abstract：
In all eukaryotes, acetylation of histone lysine residues correlates with transcription activation. Whether histone acetylation is a cause or consequence of transcription is debated. One model suggests that transcription promotes the recruitment and/or activation of acetyltransferases, and histone acetylation occurs as a consequence of ongoing transcription. However, the extent to which transcription shapes the global protein acetylation landscapes is not known. Here, we show that global protein acetylation remains virtually unaltered after acute transcription inhibition. Transcription inhibition ablates the co-transcriptionally occurring ubiquitylation of H2BK120 but does not reduce histone acetylation. The combined inhibition of transcription and CBP/p300 further demonstrates that acetyltransferases remain active and continue to acetylate histones independently of transcription. Together, these results show that histone acetylation is not a mere consequence of transcription; acetyltransferase recruitment and activation are uncoupled from the act of transcription, and histone and non-histone protein acetylation are sustained in the absence of ongoing transcription.
摘要：
在所有真核生物中，组蛋白赖氨酸残基的乙酰化与转录激活相关。组蛋白乙酰化是转录的原因还是结果存在争议。一个模型表明转录促进乙酰转移酶的募集和/或激活，和组蛋白乙酰化作为正在进行的转录的结果发生。然而,转录在多大程度上塑造了全球蛋白质乙酰化景观尚不清楚。这里,我们表明，在急性转录抑制后，整体蛋白质乙酰化几乎没有改变。转录抑制消除H2BK120的共同转录发生的泛素化,但不减少组蛋白乙酰化。转录和CBP/p300的联合抑制进一步证明乙酰转移酶保持活性并继续独立于转录使组蛋白乙酰化。一起,这些结果表明，组蛋白乙酰化不仅仅是转录的结果；乙酰转移酶的募集和激活与转录行为是分离的，在没有正在进行的转录的情况下，组蛋白和非组蛋白蛋白乙酰化是持续的。
