Raw data related to DELTEX2 C-terminal domain recognizes and recruits ADP-ribosylated proteins for ubiquitination

Crosstalk between ubiquitination and ADP-ribosylation regulates spatio-temporal recruitment of key players during DNA damage repair (DDR). The Deltex family of ubiquitin ligases (DTX1–4 and DTX3L), are characterized by a RING domain followed by a C-terminal domain (DTC) of unknown function; four Deltex proteins have other domains or partner proteins for binding poly-ADP-ribose (PAR), suggesting a role for these proteins in mediating crosstalk between ubiquitination and ADP-ribosylation. Here, we use two label-free mass spectrometry techniques to identify substrates of human DTX2 and uncover a new ADP-ribose-binding domain that facilitates PAR-dependent ubiquitination.泛素化与ADP核糖基化的串扰，可调控DNA损伤修复（DNA damage repair, DDR）过程中关键调控因子的时空招募。泛素连接酶德尔塔克斯家族（Deltex family）涵盖DTX1–4与DTX3L，其结构特征为包含一个RING结构域（RING domain）以及一个功能未知的C端结构域（C-terminal domain, DTC）；其中4种德尔塔克斯蛋白带有可结合多聚ADP核糖（poly-ADP-ribose, PAR）的其他结构域或伴侣蛋白，提示这类蛋白能够介导泛素化与ADP核糖基化之间的串扰。本研究借助两种无标记质谱技术（label-free mass spectrometry）鉴定人类DTX2的蛋白底物，并发现一个可促进PAR依赖型泛素化的新型ADP核糖结合结构域（ADP-ribose-binding domain）。