人类p100蛋白与G3BP蛋白之间的结合与功能研究
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摘要
目的：p100蛋白是一种多功能蛋白,是基因转录和pre-mRNA剪接加工的双重调控因子,由4个重复的葡萄球菌核酸酶同源性结构域SN片段和随后的Tudor-SN (TSN)结构域构成。本课题小组在前期的工作中利用p100蛋白作为诱饵钓取可以与之结合的蛋白时钓到了G3BP蛋白。由此,我们提出疑问：p100蛋白与G3BP蛋白之间的结合是在某一种特定的环境下偶然地存在还是一种稳定的细胞内结合?两种蛋白之间是直接结合还是需要其他的辅助成分进行桥接?与结合有关的结构区域各位于两种蛋白质的哪一个部分?为了解决这些疑问,我们开展了关于p100蛋白与G3BP蛋白之间的相互结合的研究工作,并对结合后的潜在功能进行了初步的探讨。
方法：
第一部分：p100蛋白与G3BP蛋白的结合研究。首先利用p100蛋白不同片段的GST融合蛋白钓取细胞内过表达的G3BP蛋白以确认我们前期研究工作中发现的二者之间的结合关系。为了确定二者之间的结合关系是否稳定,通过细胞内过表达的p100蛋白与G3BP蛋白之间及细胞内源性p100蛋白与G3BP蛋白之间的免疫共沉淀实验再次印证实验一的结果。最后利用免疫荧光实验观察二者在细胞内的定位情况。
第二部分：p100蛋白与G3BP蛋白相互结合的功能片段的确定。首先根据G3BP的结构特点构建了表达G3BP不同结构域的GST-G3BP片段融合蛋白表达质粒和用于体外翻译的带有T7启动子的pcDNA3.1(+)-G3BP质粒。然后通过GST-Pull Down方法用GST-G3BP片段1-5融合蛋白体外翻译的p100蛋白,放射白显影的方法观察结果。反之,利用GST-p100片段融合蛋白钓取体外翻译的G3BP蛋白,从而确定二者之间相互结合的功能片段。为了进一步验证我们的实验结果,重复GST-pullDown实验部分,不同之处在于用GST融合蛋白钓取细胞内过表达的蛋白质,Western Blot方法检测。
第三部分：p100蛋白与G3BP蛋白结合后的功能探讨。通过免疫免疫荧光方法观察共转染pEGFP-CI-G3BP与pRFP-p100/p100-SN/p100-TSN质粒的HeLa细胞给予亚砷酸盐刺激或热休克刺激后,两种蛋白质在细胞中的共定位情况,并确定共定位的功能片段。同时研究p100蛋白与G3BP蛋白结合后对细胞内mRNA代谢的影响：将COS7细胞分别转染p100或G3BP或共转p100与G3BP质粒,给予亚砷酸盐或45℃热休克刺激后观察细胞内RNA降解情况。
结果：
第一部分：无论是细胞内源性p100蛋白与G3BP蛋白之间还是细胞内过表达的p100蛋白与G3BP蛋白质之间都可以发生共沉淀,表明p100蛋白和G3BP蛋白可以稳定结合。在转染后的细胞内观察到p100蛋白与G3BP蛋白在细胞内的定位基本一致,主要分布于胞浆内,少量p100蛋白分布于胞核内。
第二部分：p100蛋白的SN片段可以与G3BP蛋白的多个片段结合,包括NTF2-like片段、PxxP模序、RRM片段,RGG片段结合不稳定。而p100蛋白的TSN片段和TD片段及G3BP蛋白的酸性氨基酸富集区片段则与二者之间的结合无关。
第三部分：转染后的细胞给予亚砷酸盐刺激或热休克刺激后,胞浆内开始出现绿色和红色的荧光颗粒,二种荧光颗粒在胞浆中的定位基本一致。随着刺激时间的延长,颗粒的数量和体积不断发生变化。P100蛋白的SN片段在细胞内可形成与G3BP共定位的颗粒,而TSN片段和空载体pEGFP-CI和pRFP在胞浆内不能形成明显的颗粒状结构。热休克刺激去除后,颗粒的数量和体积有一定的减少,其中红色颗粒的消散比较明显。
细胞转染了p100或G3BP或共转p100与G3BP后,细胞内提取到RNA与未转染细胞之间无明显差异。各组细胞在给予亚砷酸盐或45℃热休克前后的RNA代谢情况也未有明显差异。
结论：通过研究证实,G3BP与p100蛋白在细胞内、外均可结合,不需要辅助因子的参与。二者之间的结合是由G3BP的NTF2-like片段、PxxP模序、RRM片段和p100蛋白的SN片段介导的。应激状态下,p100蛋白与G3BP蛋白共同参与了应激颗粒的形成,介导p100蛋白进入应激颗粒的是SN片段。
Objectives:
p100is a multiple functions Protein which is a co-factor of transcription and pre-mRNA splicing. It has4repeated SN domains and a Tudor-SN(TSN)domain. We has done a lot of research on p100recent years. We found that G3BP is one of the proteins pulled down by p100protein in our previous research. It is not known if the proteins interact in some specific situation or in common conditions, if they combine to each other directly or indirectly, or if the interaction needs some co-factors. Nor is it known which domain(s) mediates the interaction. So we carry out the following study on the mechanisms and functional consequences of the interaction between p100and G3BP proteins.
Methods:
Part Ⅰ:Interactions of p100and G3BP proteins in cells. First, we used the GST-p100fusion protein to pull down G3BP protein and coimmunoprecipitaion of G3BP and p100to confirm our previous observation. We also studied the colocalization of p100and G3BP by immunofluorescence microscopy.
Part Ⅱ:Identification of interaction domains of p100and G3BP.
1. We constructed several recombinant plasmids including5GST fusion constructs with different G3BP domains and one pcDNA3.1(+)-G3BP as template for in vitro translation.
2. GST fusion proteins with various fragments of either G3BP or p100were used to pull down in vitro translated full length p100or G3BP labeled with35S to identify the interaction domains of p100and G3BP. Western Blot xperiments were also used to confirm the specific interactions of p100and G3BP.
Part Ⅲ:Functional studies of the interactions between p100and G3BP in cells under stress.
1. We transfected pEGFP-CI-G3BP and pRFP-p100/p100-SN/p100-TSN plasmids into HeLa cells, then treated the cells with arsenite or heat shock and observed the colocalization of green and red fluorescence.
2. Effect of mRNA metabolism by the association of p100and G3BP. We transfected COS7cells with pEGFP-G3BP or pSG5-p100or both and treated cells with arsenite or heat shock. Total RNA was extracted and used to study mRNA degradation.
Results
Part Ⅰ:We observed the partial colocalization of G3BP green fluorescence, which is mainly located in cytoplasm especially near the nucleus membrane, and p100red fluorescence, which spreads throughout the whole cell. Coimmunoprecipitation and Western Blot experiments also confirmed the interaction of both over-express and endogenous G3BP and p100.
Part Ⅱ:We found that p100can bind to several domains, especially domain3and4of G3BP. The interaction between domain5of G3BP and p100was unstable, and probably unspecific. Domain2can not mediate the interaction. SN domain of p100mediates the interaction. The TSN and TD domains do not participate the interaction.
Part Ⅲ:After arsenite or heat shock treatment, some green particles colocalized with the red ones. The number and size of particles increased with time. The SN domain, but not the TSN domain, of p100behaved the same way as the full length p100protein. We didn't detect any difference in mRNA metabolism after transfection of various combination of plasmids after stress treatment.
Conclusions:The interaction of G3BP and p100is direct and specific. The interacting domains are NTF2-like domain (domainl)、PxxP motif (domain3、RRM domain (domain4) of G3BP and SN domain of p100. G3BP is involved in stress granule formation and p100protein were recruited to the granules which is mediated by the SN domain.
方法：
第一部分：p100蛋白与G3BP蛋白的结合研究。首先利用p100蛋白不同片段的GST融合蛋白钓取细胞内过表达的G3BP蛋白以确认我们前期研究工作中发现的二者之间的结合关系。为了确定二者之间的结合关系是否稳定,通过细胞内过表达的p100蛋白与G3BP蛋白之间及细胞内源性p100蛋白与G3BP蛋白之间的免疫共沉淀实验再次印证实验一的结果。最后利用免疫荧光实验观察二者在细胞内的定位情况。
第二部分：p100蛋白与G3BP蛋白相互结合的功能片段的确定。首先根据G3BP的结构特点构建了表达G3BP不同结构域的GST-G3BP片段融合蛋白表达质粒和用于体外翻译的带有T7启动子的pcDNA3.1(+)-G3BP质粒。然后通过GST-Pull Down方法用GST-G3BP片段1-5融合蛋白体外翻译的p100蛋白,放射白显影的方法观察结果。反之,利用GST-p100片段融合蛋白钓取体外翻译的G3BP蛋白,从而确定二者之间相互结合的功能片段。为了进一步验证我们的实验结果,重复GST-pullDown实验部分,不同之处在于用GST融合蛋白钓取细胞内过表达的蛋白质,Western Blot方法检测。
第三部分：p100蛋白与G3BP蛋白结合后的功能探讨。通过免疫免疫荧光方法观察共转染pEGFP-CI-G3BP与pRFP-p100/p100-SN/p100-TSN质粒的HeLa细胞给予亚砷酸盐刺激或热休克刺激后,两种蛋白质在细胞中的共定位情况,并确定共定位的功能片段。同时研究p100蛋白与G3BP蛋白结合后对细胞内mRNA代谢的影响：将COS7细胞分别转染p100或G3BP或共转p100与G3BP质粒,给予亚砷酸盐或45℃热休克刺激后观察细胞内RNA降解情况。
结果：
第一部分：无论是细胞内源性p100蛋白与G3BP蛋白之间还是细胞内过表达的p100蛋白与G3BP蛋白质之间都可以发生共沉淀,表明p100蛋白和G3BP蛋白可以稳定结合。在转染后的细胞内观察到p100蛋白与G3BP蛋白在细胞内的定位基本一致,主要分布于胞浆内,少量p100蛋白分布于胞核内。
第二部分：p100蛋白的SN片段可以与G3BP蛋白的多个片段结合,包括NTF2-like片段、PxxP模序、RRM片段,RGG片段结合不稳定。而p100蛋白的TSN片段和TD片段及G3BP蛋白的酸性氨基酸富集区片段则与二者之间的结合无关。
第三部分：转染后的细胞给予亚砷酸盐刺激或热休克刺激后,胞浆内开始出现绿色和红色的荧光颗粒,二种荧光颗粒在胞浆中的定位基本一致。随着刺激时间的延长,颗粒的数量和体积不断发生变化。P100蛋白的SN片段在细胞内可形成与G3BP共定位的颗粒,而TSN片段和空载体pEGFP-CI和pRFP在胞浆内不能形成明显的颗粒状结构。热休克刺激去除后,颗粒的数量和体积有一定的减少,其中红色颗粒的消散比较明显。
细胞转染了p100或G3BP或共转p100与G3BP后,细胞内提取到RNA与未转染细胞之间无明显差异。各组细胞在给予亚砷酸盐或45℃热休克前后的RNA代谢情况也未有明显差异。
结论：通过研究证实,G3BP与p100蛋白在细胞内、外均可结合,不需要辅助因子的参与。二者之间的结合是由G3BP的NTF2-like片段、PxxP模序、RRM片段和p100蛋白的SN片段介导的。应激状态下,p100蛋白与G3BP蛋白共同参与了应激颗粒的形成,介导p100蛋白进入应激颗粒的是SN片段。
Objectives:
p100is a multiple functions Protein which is a co-factor of transcription and pre-mRNA splicing. It has4repeated SN domains and a Tudor-SN(TSN)domain. We has done a lot of research on p100recent years. We found that G3BP is one of the proteins pulled down by p100protein in our previous research. It is not known if the proteins interact in some specific situation or in common conditions, if they combine to each other directly or indirectly, or if the interaction needs some co-factors. Nor is it known which domain(s) mediates the interaction. So we carry out the following study on the mechanisms and functional consequences of the interaction between p100and G3BP proteins.
Methods:
Part Ⅰ:Interactions of p100and G3BP proteins in cells. First, we used the GST-p100fusion protein to pull down G3BP protein and coimmunoprecipitaion of G3BP and p100to confirm our previous observation. We also studied the colocalization of p100and G3BP by immunofluorescence microscopy.
Part Ⅱ:Identification of interaction domains of p100and G3BP.
1. We constructed several recombinant plasmids including5GST fusion constructs with different G3BP domains and one pcDNA3.1(+)-G3BP as template for in vitro translation.
2. GST fusion proteins with various fragments of either G3BP or p100were used to pull down in vitro translated full length p100or G3BP labeled with35S to identify the interaction domains of p100and G3BP. Western Blot xperiments were also used to confirm the specific interactions of p100and G3BP.
Part Ⅲ:Functional studies of the interactions between p100and G3BP in cells under stress.
1. We transfected pEGFP-CI-G3BP and pRFP-p100/p100-SN/p100-TSN plasmids into HeLa cells, then treated the cells with arsenite or heat shock and observed the colocalization of green and red fluorescence.
2. Effect of mRNA metabolism by the association of p100and G3BP. We transfected COS7cells with pEGFP-G3BP or pSG5-p100or both and treated cells with arsenite or heat shock. Total RNA was extracted and used to study mRNA degradation.
Results
Part Ⅰ:We observed the partial colocalization of G3BP green fluorescence, which is mainly located in cytoplasm especially near the nucleus membrane, and p100red fluorescence, which spreads throughout the whole cell. Coimmunoprecipitation and Western Blot experiments also confirmed the interaction of both over-express and endogenous G3BP and p100.
Part Ⅱ:We found that p100can bind to several domains, especially domain3and4of G3BP. The interaction between domain5of G3BP and p100was unstable, and probably unspecific. Domain2can not mediate the interaction. SN domain of p100mediates the interaction. The TSN and TD domains do not participate the interaction.
Part Ⅲ:After arsenite or heat shock treatment, some green particles colocalized with the red ones. The number and size of particles increased with time. The SN domain, but not the TSN domain, of p100behaved the same way as the full length p100protein. We didn't detect any difference in mRNA metabolism after transfection of various combination of plasmids after stress treatment.
Conclusions:The interaction of G3BP and p100is direct and specific. The interacting domains are NTF2-like domain (domainl)、PxxP motif (domain3、RRM domain (domain4) of G3BP and SN domain of p100. G3BP is involved in stress granule formation and p100protein were recruited to the granules which is mediated by the SN domain.
引文
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