Crystal structure of thymine DNA glycosylase conjugated to SUMO-1

Daichi Baba, Nobuo Maita, Jun-Goo Jee, Yasuhiro Uchimura, Hisato Saitoh, Kaoru Sugasawa, Fumio Hanaoka, Hidehito Tochio, Hidekazu Hiroaki and Masahiro Shirakawa ()
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Daichi Baba: Yokohama City University
Nobuo Maita: Yokohama City University
Jun-Goo Jee: RIKEN Genomic Sciences Center
Yasuhiro Uchimura: Kumamoto University
Hisato Saitoh: Kumamoto University
Kaoru Sugasawa: Discovery Research Institute, RIKEN
Fumio Hanaoka: Discovery Research Institute, RIKEN
Hidehito Tochio: Yokohama City University
Hidekazu Hiroaki: Yokohama City University
Masahiro Shirakawa: Yokohama City University

Nature, 2005, vol. 435, issue 7044, 979-982

Abstract: Abstract Members of the small ubiquitin-like modifier (SUMO) family can be covalently attached to the lysine residue of a target protein through an enzymatic pathway similar to that used in ubiquitin conjugation1, and are involved in various cellular events that do not rely on degradative signalling via the proteasome or lysosome2,3,4,5. However, little is known about the molecular mechanisms of SUMO-modification-induced protein functional transfer. During DNA mismatch repair, SUMO conjugation of the uracil/thymine DNA glycosylase TDG promotes the release of TDG from the abasic (AP) site created after base excision, and coordinates its transfer to AP endonuclease 1, which catalyses the next step in the repair pathway6. Here we report the crystal structure of the central region of human TDG conjugated to SUMO-1 at 2.1 Å resolution. The structure reveals a helix protruding from the protein surface, which presumably interferes with the product DNA and thus promotes the dissociation of TDG from the DNA molecule. This helix is formed by covalent and non-covalent contacts between TDG and SUMO-1. The non-covalent contacts are also essential for release from the product DNA, as verified by mutagenesis.

Date: 2005
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DOI: 10.1038/nature03634

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