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Structure and mechanism of non-histone protein acetyltransferase enzymes

机译:非组蛋白乙酰转移酶的结构和机理

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摘要

Post-translational modification of proteins is ubiquitous and mediates many cellular processes, including intracellular localization, protein-protein interactions, enzyme activity, transcriptional regulation and protein stability. While the role of phosphorylation as a key post-translational modification has been well studied, the more evolutionarily conserved post-translational modification acetylation has only recently attracted attention as a key regulator of cellular events. Protein acetylation has been largely studied in the context of its role in histone modification and gene regulation, where histones are modified by histone acetyltransferases to promote transcription. However, more recent acetylomic and biochemical studies have revealed that acetylation is mediated by a broader family of protein acetyltransferases. The recent structure determination of several protein acetyltransferases has provided a wealth of molecular information regarding structural features of protein acetyltransferases, their enzymatic mechanisms, their mode of substrate-specific recognition and their regulatory elements. In this review, we briefly describe what is known about non-histone protein substrates, but mainly focus on a few recent structures of protein acetyltransferases to compare and contrast them with histone acetyltransferases to better understand the molecular basis for protein recognition and modification by this family of protein modification enzymes.
机译:蛋白质的翻译后修饰无处不在,并介导许多细胞过程,包括细胞内定位,蛋白质-蛋白质相互作用,酶活性,转录调节和蛋白质稳定性。虽然磷酸化作为关键的翻译后修饰的作用已得到很好的研究,但在进化上更保守的翻译后修饰的乙酰化作为细胞事件的关键调节剂最近才引起关注。蛋白质乙酰化在其在组蛋白修饰和基因调控中的作用的背景下已得到广泛研究,其中组蛋白被组蛋白乙酰转移酶修饰以促进转录。但是,最近的乙酰组学和生化研究表明,乙酰化是由更广泛的蛋白质乙酰基转移酶家族介导的。最近对几种蛋白质乙酰基转移酶的结构测定提供了有关蛋白质乙酰基转移酶的结构特征,其酶促机制,其底物特异性识别方式及其调节元件的大量分子信息。在本文中,我们简要介绍了非组蛋白的蛋白质底物,但主要关注蛋白质乙酰基转移酶的一些最新结构,以与组蛋白乙酰基转移酶进行比较和对比,以更好地理解该家族蛋白质识别和修饰的分子基础。蛋白修饰酶

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