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赖氨酸乙酰化组谱分析揭示了.中的新型组蛋白去乙酰化酶底物蛋白

Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins in .

机构信息

Plant Proteomics, Max Planck Institute for Plant Breeding Research, Cologne, Germany.

Plant Molecular Biology, Department Biology I, Ludwig-Maximilians-University Munich, Martinsried, Germany.

出版信息

Mol Syst Biol. 2017 Oct 23;13(10):949. doi: 10.15252/msb.20177819.

DOI:10.15252/msb.20177819
PMID:29061669
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5658702/
Abstract

Histone deacetylases have central functions in regulating stress defenses and development in plants. However, the knowledge about the deacetylase functions is largely limited to histones, although these enzymes were found in diverse subcellular compartments. In this study, we determined the proteome-wide signatures of the RPD3/HDA1 class of histone deacetylases in Relative quantification of the changes in the lysine acetylation levels was determined on a proteome-wide scale after treatment of leaves with deacetylase inhibitors apicidin and trichostatin A. We identified 91 new acetylated candidate proteins other than histones, which are potential substrates of the RPD3/HDA1-like histone deacetylases in , of which at least 30 of these proteins function in nucleic acid binding. Furthermore, our analysis revealed that histone deacetylase 14 (HDA14) is the first organellar-localized RPD3/HDA1 class protein found to reside in the chloroplasts and that the majority of its protein targets have functions in photosynthesis. Finally, the analysis of HDA14 loss-of-function mutants revealed that the activation state of RuBisCO is controlled by lysine acetylation of RuBisCO activase under low-light conditions.

摘要

组蛋白去乙酰化酶在调节植物的应激防御和发育方面具有核心功能。然而,尽管这些酶存在于不同的亚细胞区室中,但关于去乙酰化酶功能的知识在很大程度上仅限于组蛋白。在这项研究中,我们确定了 RPD3/HDA1 类组蛋白去乙酰化酶在 中的全蛋白组特征。在用去乙酰化酶抑制剂 apicidin 和 trichostatin A 处理叶片后,我们在全蛋白组范围内确定了赖氨酸乙酰化水平变化的相对定量。我们鉴定了 91 种新的组蛋白乙酰化候选蛋白,它们是 中的 RPD3/HDA1 样组蛋白去乙酰化酶的潜在底物,其中至少有 30 种蛋白质的功能与核酸结合有关。此外,我们的分析表明,组蛋白去乙酰化酶 14(HDA14)是第一个定位于细胞器的 RPD3/HDA1 类蛋白,它存在于叶绿体中,并且其大多数蛋白质靶标具有光合作用功能。最后,对 HDA14 功能丧失突变体的分析表明,在低光条件下,RuBisCO 激活酶的赖氨酸乙酰化控制 RuBisCO 的激活状态。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ffd9/5658702/0facbd7543b1/MSB-13-949-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ffd9/5658702/3197135a801f/MSB-13-949-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ffd9/5658702/8715a2e867dd/MSB-13-949-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ffd9/5658702/2d517a7463c3/MSB-13-949-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ffd9/5658702/d61c6b7db684/MSB-13-949-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ffd9/5658702/d2f43bb09529/MSB-13-949-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ffd9/5658702/0facbd7543b1/MSB-13-949-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ffd9/5658702/3197135a801f/MSB-13-949-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ffd9/5658702/8715a2e867dd/MSB-13-949-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ffd9/5658702/2d517a7463c3/MSB-13-949-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ffd9/5658702/d61c6b7db684/MSB-13-949-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ffd9/5658702/d2f43bb09529/MSB-13-949-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ffd9/5658702/0facbd7543b1/MSB-13-949-g007.jpg

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