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. 2021 Sep 11;49(18):10477–10492. doi: 10.1093/nar/gkab771

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© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 1. — TARG1 removes thymidine-linked ADP-ribose from DNA and confers resistance to DarT toxicity in bacteria. (A) Structural comparison between TaqDarG-macrodomain (orange) bound to ADP-ribose (red) and TARG1 (light blue) with a covalent lysyl-ADP-ribose linkage (dark blue). To the right is a detailed view of the DarG catalytic lysine 80 (orange sticks) and TARG1 catalytic lysine 84 (blue sticks). (B) UV detection of DarT ADP-ribosylated DNA oligonucleotide de-ADP-ribosylation reactions with TaqDarG-macrodomain and TARG1. (C) Bacterial DarT toxicity rescue assay in BL21 DE3 using pBAD DarT and pET encoding DarG-macrodomain WT, DarG-macrodomain K80A, TARG1 WT or TARG1 K84A. pBAD expression is controlled with glucose or arabinose and pET expression is controlled with IPTG.