Solution structure of a zinc‐finger domain that binds to poly‐ADP‐ribose |
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| Authors: | Shin Isogai Shin‐Ichiro Kanno Mariko Ariyoshi Hidehito Tochio Yutaka Ito Akira Yasui Masahiro Shirakawa |
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| Affiliation: | 1. Department of Molecular Engineering, Graduate School of Engineering, Kyoto University, Kyoto‐Daigaku Katsura, Kyoto 615‐8510, Japan;2. Department of Molecular Genetics, Institute of Development, Aging and Cancer, Tohoku University, Seiryomachi 4‐1, Sendai 980‐8575, Japan;3. CREST, JST, 4‐1‐8 Honcho, Kawaguchi, Saitama 332‐0012, Japan;4. Department of Chemistry, Tokyo Metropolitan University, 1‐1 Minami‐Osawa, Hachioji, Tokyo 192‐0397, Japan;5. RIKEN, Yokohama Institute, 1‐7‐22, Suehirocho, Tsurumi, Yokohama 230‐0045, Japan |
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| Abstract: | Poly‐ADP‐ribosylation is a unique post‐translational modification that controls various nuclear events such as repair of DNA single‐strand breaks. Recently, the protein containing the poly‐ADP‐ribose (pADPr)‐binding zinc‐finger (PBZ) domain was shown to be a novel AP endonuclease and involved in a cell cycle checkpoint. Here, we determined the three‐dimensional structure of the PBZ domain from Drosophila melanogaster CG1218‐PA using NMR spectroscopy. The domain folds into a C2H2‐type zinc‐finger structure in an S configuration, containing a characteristic loop between the zinc‐coordinating cysteine and histidine residues. This is distinct from the structure of other C2H2‐type zinc fingers. NMR signal changes that occur when pADPr binds to the PBZ domains from CG1218‐PA and human checkpoint with FHA (forkhead‐associated) and ring finger (CHFR) and mutagenesis suggest that a surface relatively well conserved among PBZ domains may serve as a major interface with pADPr. |
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