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A systematic study of nuclear interactome of C-terminal domain small phosphatase-like 2 using inducible expression system and shotgun proteomics

机译:使用诱导型表达系统和霰弹枪蛋白质组学的C末端域小磷酸酶样核蛋白酶的系统研究

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摘要

RNA polymerase II C-terminal domain phosphatases are newly emerging family of phosphatases that contain FCPH domain with Mg+2-binding DXDX(T/V) signature motif. Its subfamily includes small CTD phosphatases (SCPs). Recently, we identified several interacting partners of human SCP1 with appearance of dephosphorylation and O-GlcNAcylation. In this study, using an established cell line with inducible CTDSPL2 protein (a member of the new phosphatase family), proteomic screening was conducted to identify binding partners of CTDSPL2 in nuclear extract through immunoprecipitation of CTDSPL2 with its associated. This approach led to the identification of several interacting partners of CTDSPL2. This will provide a better understanding on CTDSPL2.
机译:RNA聚合酶II C-末端域磷酸酶是新出现的磷酸酶,含有含有Mg + 2结合DXDX(T / V)签名基序的FCPH结构域。其亚家族包括小型CTD磷酸酶(SCPS)。最近,我们确定了几种人SCP1的互动伴侣,具有脱磷酸化和O-Glcnacylation的外观。在该研究中,使用具有诱导型CTDSPL2蛋白(新的磷酸酶家族的成员)的建立的细胞系,进行蛋白质组学筛选,以通过CTDSPL2与其相关的CTDSPL2鉴定CTDSPL2在核提取物中的结合伴侣。这种方法导致识别CTDSPL2的几个互动伴侣。这将为CTDSPL2提供更好的理解。

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