Global analysis of lysine acetylation suggests the involvement of protein acetylation in diverse biological processes in rice (Oryza sativa).
Global analysis of lysine acetylation suggests the involvement of protein acetylation in diverse biological processes in rice (Oryza sativa).
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DOI：
10.1371/journal.pone.0089283
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发表时间：
2014
期刊：
影响因子：
3.7
通讯作者：
Peng Z
中科院分区：
文献类型：
--
作者：
Nallamilli BR;Edelmann MJ;Zhong X;Tan F;Mujahid H;Zhang J;Nanduri B;Peng Z
赖氨酸乙酰化是一种可逆的、动态的蛋白质修饰，受赖氨酸乙酰转移酶和脱乙酰酶的调节。高通量蛋白质组学的最新进展极大地促进了赖氨酸乙酰化的全球分析的成功。在人类细胞、大肠杆菌和双子叶植物中，大量具有不同生物学功能的蛋白质已被证明是乙酰化的。然而，在单子叶植物中，尤其是在谷类作物中，非组蛋白中赖氨酸乙酰化的程度仍然很大程度上是未知的。本文报道了水稻赖氨酸乙酰化的质谱学检测。我们在44种具有不同生物学功能的蛋白质上鉴定了60个赖氨酸乙酰化位点。免疫印迹研究进一步证实了大量乙酰化非组蛋白的存在。对氨基酸组成的检测表明，乙酰化位点周围有很大的氨基酸偏向，不同生物之间的氨基酸偏好是保守的。基因本体论分析表明，除了组蛋白修饰外，赖氨酸乙酰化还存在于多种细胞质、叶绿体和线粒体蛋白中。我们的结果表明，赖氨酸乙酰化可能构成了许多蛋白质的调节机制，包括具有不同生物学功能的组蛋白和非组蛋白蛋白。
Lysine acetylation is a reversible, dynamic protein modification regulated by lysine acetyltransferases and deacetylases. Recent advances in high-throughput proteomics have greatly contributed to the success of global analysis of lysine acetylation. A large number of proteins of diverse biological functions have been shown to be acetylated in several reports in human cells, E.coli, and dicot plants. However, the extent of lysine acetylation in non-histone proteins remains largely unknown in monocots, particularly in the cereal crops. Here we report the mass spectrometric examination of lysine acetylation in rice (Oryza sativa). We identified 60 lysine acetylated sites on 44 proteins of diverse biological functions. Immunoblot studies further validated the presence of a large number of acetylated non-histone proteins. Examination of the amino acid composition revealed substantial amino acid bias around the acetylation sites and the amino acid preference is conserved among different organisms. Gene ontology analysis demonstrates that lysine acetylation occurs in diverse cytoplasmic, chloroplast and mitochondrial proteins in addition to the histone modifications. Our results suggest that lysine acetylation might constitute a regulatory mechanism for many proteins, including both histones and non-histone proteins of diverse biological functions.
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