Raw data related to DTX2-mediated ubiquitination of ADP-ribosylated substrates

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（ubiquitination）与ADP核糖基化（ADP-ribosylation）之间的交叉调控，在DNA损伤修复（DDR）过程中调控关键效应分子的时空招募。Deltex家族泛素连接酶（ubiquitin ligases，DTX1–4及DTX3L）的典型特征为含有RING结构域（RING domain）与一段功能未知的C端结构域（DTC）；其中4种Deltex蛋白具备可结合多聚ADP核糖（poly-ADP-ribose，PAR）的额外结构域或伴侣蛋白，提示这类蛋白可介导泛素化与ADP核糖基化之间的交叉调控。本研究采用两种无标记质谱技术，鉴定人源DTX2的底物，并发现一个全新的ADP核糖结合结构域（ADP-ribose-binding domain），该结构域可促进PAR依赖型泛素化。