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首页> 外文期刊>Biochimica et Biophysica Acta. Gene Regulatory Mechanisms >Non-histone protein acetylation by the evolutionarily conserved GCN5 and PCAF acetyltransferases
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Non-histone protein acetylation by the evolutionarily conserved GCN5 and PCAF acetyltransferases

机译:通过进化保守的GCN5和PCAF乙酰转移酶进行非组蛋白蛋白乙酰化

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摘要

GCN5, conserved from yeast to humans, and the vertebrate specific PCAF, are lysine acetyltransferase enzymes found in large protein complexes. Both enzymes have well documented roles in the histone acetylation and the concomitant regulation of transcription. However, these enzymes also acetylate non-histone substrates to impact diverse aspects of cell physiology. Here, I review our current understanding of non-histone acetylation by GCN5 and PCAF across eukaryotes, from target identification to molecular mechanism and regulation. I focus mainly on budding yeast, where Gcn5 was first discovered, and mammalian systems, where the bulk of non-histone substrates have been characterized. I end the review by defining critical caveats and open questions that apply to all models.
机译:GCN5,从酵母和脊椎动物特异性PCAF保存,是赖氨酸乙酰转移酶在大蛋白质复合物中发现。 两种酶在组蛋白乙酰化和转录的伴随调节中有很好的记录作用。 然而,这些酶也乙酰化非组蛋白基质,以影响细胞生理学的不同方面。 在这里,我认为我们目前的了解GCN5和PCAF在真核中,从目标鉴定到分子机制和调节。 我主要专注于萌芽酵母,首次发现GCN5和哺乳动物系统,其中本体的非组蛋白基材的特征在于。 我通过定义关键的警告和打开适用于所有模型的问题来结束审查。

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