信号识别颗粒蛋白SRP68和SRP72结合组蛋白H4活性及转录调控功能的研究
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摘要
作为染色质基本组成单位的核小体,是由4种核心组蛋白(H3、H4,H2A和H2B)紧密结合在一起构成的八聚体复合物,其外盘绕着周长度有147个碱基对的核酸链。核心组蛋白精氨酸甲基化(histone arginine methylation)广泛发生在其N端暴露在外的“尾部”,具有基因表达调控的重要功能。组蛋白精氨酸甲基化修饰被认为是表观遗传学密码(histone code)的一部分,以影响下游效应子的结合或排斥染色质。尽管如此,人们对这种修饰体系参与调控机制的认识还很少。因而,我们采用体外pulldown方法,分别富集与组蛋白H4第3位精氨酸对称双甲基化修饰(H4R3me2s)、组蛋白H4第3位精氨酸非对称双甲基化修饰(H4R3me2a)和未修饰H4多肽特异性结合的哺乳动物细胞核蛋白。虽然pulldown:结果没有发现能特异结合组蛋白H4第3位精氨酸(H4R3)双甲基化修饰多肽的蛋白,但是我们发现H4R3的双甲基化修饰能特异抑制两个高丰度核蛋白与修饰H4多肽的结合,质谱分析表明这两个蛋白即信号识别颗粒蛋白的亚基SRP68和SRP72。
SRP68和SRP72是信号识别颗粒蛋白(Signal recognition particle)的两个亚基。在哺乳动物细胞中,它与SRP RNA、SRP9、SRPl4、SRPl9,SRP54一起组装成SRP复合体,主要功能是帮助分泌蛋白和膜蛋白向内质网膜的转运。
在本课题研究中,采用凝胶过滤层析(gel filtration chromatography)纯化真核细胞大分子复合体和pulldown联用的方法,结果显示结合H4多肽并不是完整的SRP复合体。体外实验结果证明,SRP68和SRP72都具有结合H4N-末端多肽的活性,H4R3甲基化修饰明显削弱SRP68和SRP72蛋白与组蛋白H4尾部的结合。细胞实验证明SRP68和SRP72主要定位于细胞核并能结合H4N-末端多肽。染色质免疫共沉淀加Western免疫印迹证明SRP68/SRP72与染色质结合并主要与H4R3未甲基化修饰的染色质相互作用。在细胞内过表达组蛋白精氨酸甲基化酶PRMT5,也会增加组蛋白精氨酸对称甲基化水平,导致SRP68/SRP72蛋白和染色质的相互作用显著减弱及SRP68和SRP72从细胞核至细胞质的转运。
我们通过染色质免疫沉淀技术和高通量测序联用的方法(ChIP—seq),鉴定并发现SRP68的结合位点在全基因组上广泛分布。将SRP68的DNA结合位点与已知转录因子模体(motif)数据库配对分析,我们发现在SRP68的结合位点上显著富集NFATc2和K1f4的DNA结合序列。随后,免疫共沉淀实验也证明了SRP68可以分别与NFATc2和Klf4相互作用,这暗示SRP68可能通过与转录因子NFATc2、Klf4相互作用而招募至靶基因上,调控基因转录。
以上的研究结果表明,组蛋白H4R3精氨酸甲基化修饰抑制SRP68/SRP72与染色质组蛋白的结合活性。此外,我们的研究还揭示了SRP68/SRP72具有潜在的调控基因转录的功能。
The nucleosome is the fundamental unit of chromatin and it is composed of an octamer of the four core histones (H3, H4, H2A, H2B) around which147base pairs of DNA are wrapped. Arginine methylation, which plays a important role on transcription regulation, broadly occurs in the N-teminal tails of core histones. Histone arginine methylation, described as a part of "Histone code", is required for the downstream effctor recruiment or rejection. However, the mechanisms by which histone arginine methylation regulates transcription remain poorly understood. In this study we have attempted to purify nuclear proteins in mammalian cell that recognize specifically the symmetric dimethylated arginine3in histone H4tail(H4R3me2s), the asymmetric dimethylated arginine3in histone H4tail(H4R3me2as) and unmethylated arginine3in histone H4tail using Pull down assay. No major nuclear protein was observed to bind specifically the methylated H4R3peptides. However, both H4R3me2s and H4R3me2as markedly inhibit the binding of two proteins to unmethylated H4R3tail. These proteins were identified as the signal recognition particle SRP68and SRP72heterodimers by an unbiased proteomic approach.
SRP68and SRP72are two polypeptides of the signal recognition particle. SRP68and SRP72together with SRP RNA、SRP9、SRP14、SRP19、SRP54could form a SRP complex, which plays an key role in the delivery of secretory proteins and membrane proteins to endoplasmic reticulum membrane.
Here we show that only SRP68and SRP72, but not the SRP complex, bind to the unmethylated H4R3peptide according to gel filtration chromatography and pull down assay result. In vitro, SRP68and SRP72bind to H4R3tail in a methylation sensitive manner. In vivo, SRP68and SRP72associate with chromatin and bind to H4N-terminal polypeptide. Chromatin immunoprecipitation and western blot result prove that SRP68/SRP72mainly combine with chromatin without H4R3methylation modification. Overexpressing arginine methylation enzyme PRMT5, also can increase histone arginine symmetric methylation level in the cells, leading to the interaction between SRP68/SRP72protein and chromatin reduce. In the meanwile, SRP68and SRP72cytoplasm localization increase.
The genome-wide occupancy study of SRP68reveals a broad distribution of SRP68in genome. The SRP68binding sites were mapped to the known transcription factor motif data, we discovery that the two DNA binding motifs of the transcription factors NFAT and KLF4are dramaticly rich in SRP68binding sites.
Together our study underscores a role of H4R3methylation in blocking the binding of effector protein SRP68and SRP72to chromatin. In addition, our study reveals a novel role for SRP68and SRP72in transcriptional regulation.
SRP68和SRP72是信号识别颗粒蛋白(Signal recognition particle)的两个亚基。在哺乳动物细胞中,它与SRP RNA、SRP9、SRPl4、SRPl9,SRP54一起组装成SRP复合体,主要功能是帮助分泌蛋白和膜蛋白向内质网膜的转运。
在本课题研究中,采用凝胶过滤层析(gel filtration chromatography)纯化真核细胞大分子复合体和pulldown联用的方法,结果显示结合H4多肽并不是完整的SRP复合体。体外实验结果证明,SRP68和SRP72都具有结合H4N-末端多肽的活性,H4R3甲基化修饰明显削弱SRP68和SRP72蛋白与组蛋白H4尾部的结合。细胞实验证明SRP68和SRP72主要定位于细胞核并能结合H4N-末端多肽。染色质免疫共沉淀加Western免疫印迹证明SRP68/SRP72与染色质结合并主要与H4R3未甲基化修饰的染色质相互作用。在细胞内过表达组蛋白精氨酸甲基化酶PRMT5,也会增加组蛋白精氨酸对称甲基化水平,导致SRP68/SRP72蛋白和染色质的相互作用显著减弱及SRP68和SRP72从细胞核至细胞质的转运。
我们通过染色质免疫沉淀技术和高通量测序联用的方法(ChIP—seq),鉴定并发现SRP68的结合位点在全基因组上广泛分布。将SRP68的DNA结合位点与已知转录因子模体(motif)数据库配对分析,我们发现在SRP68的结合位点上显著富集NFATc2和K1f4的DNA结合序列。随后,免疫共沉淀实验也证明了SRP68可以分别与NFATc2和Klf4相互作用,这暗示SRP68可能通过与转录因子NFATc2、Klf4相互作用而招募至靶基因上,调控基因转录。
以上的研究结果表明,组蛋白H4R3精氨酸甲基化修饰抑制SRP68/SRP72与染色质组蛋白的结合活性。此外,我们的研究还揭示了SRP68/SRP72具有潜在的调控基因转录的功能。
The nucleosome is the fundamental unit of chromatin and it is composed of an octamer of the four core histones (H3, H4, H2A, H2B) around which147base pairs of DNA are wrapped. Arginine methylation, which plays a important role on transcription regulation, broadly occurs in the N-teminal tails of core histones. Histone arginine methylation, described as a part of "Histone code", is required for the downstream effctor recruiment or rejection. However, the mechanisms by which histone arginine methylation regulates transcription remain poorly understood. In this study we have attempted to purify nuclear proteins in mammalian cell that recognize specifically the symmetric dimethylated arginine3in histone H4tail(H4R3me2s), the asymmetric dimethylated arginine3in histone H4tail(H4R3me2as) and unmethylated arginine3in histone H4tail using Pull down assay. No major nuclear protein was observed to bind specifically the methylated H4R3peptides. However, both H4R3me2s and H4R3me2as markedly inhibit the binding of two proteins to unmethylated H4R3tail. These proteins were identified as the signal recognition particle SRP68and SRP72heterodimers by an unbiased proteomic approach.
SRP68and SRP72are two polypeptides of the signal recognition particle. SRP68and SRP72together with SRP RNA、SRP9、SRP14、SRP19、SRP54could form a SRP complex, which plays an key role in the delivery of secretory proteins and membrane proteins to endoplasmic reticulum membrane.
Here we show that only SRP68and SRP72, but not the SRP complex, bind to the unmethylated H4R3peptide according to gel filtration chromatography and pull down assay result. In vitro, SRP68and SRP72bind to H4R3tail in a methylation sensitive manner. In vivo, SRP68and SRP72associate with chromatin and bind to H4N-terminal polypeptide. Chromatin immunoprecipitation and western blot result prove that SRP68/SRP72mainly combine with chromatin without H4R3methylation modification. Overexpressing arginine methylation enzyme PRMT5, also can increase histone arginine symmetric methylation level in the cells, leading to the interaction between SRP68/SRP72protein and chromatin reduce. In the meanwile, SRP68and SRP72cytoplasm localization increase.
The genome-wide occupancy study of SRP68reveals a broad distribution of SRP68in genome. The SRP68binding sites were mapped to the known transcription factor motif data, we discovery that the two DNA binding motifs of the transcription factors NFAT and KLF4are dramaticly rich in SRP68binding sites.
Together our study underscores a role of H4R3methylation in blocking the binding of effector protein SRP68and SRP72to chromatin. In addition, our study reveals a novel role for SRP68and SRP72in transcriptional regulation.
引文
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