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Backbone 1H, 13C and 15N chemical shift assignment of full-length human uracil DNA glycosylase UNG2

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Abstract

Human uracil N-glycosylase isoform 2—UNG2 consists of an N-terminal intrinsically disordered regulatory domain (UNG2 residues 1–92, 9.3 kDa) and a C-terminal structured catalytic domain (UNG2 residues 93–313, 25.1 kDa). Here, we report the backbone 1H, 13C, and 15N chemical shift assignment as well as secondary structure analysis of the N-and C-terminal domains of UNG2 representing the full-length UNG2 protein.

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Abbreviations

SLIC:

Sequence- and ligation independent cloning

UNG2:

Uracil N-glycosylase isoform 2

N-UNG2:

Residues 1–92 of UNG2

AA:

Amino acid

PCNA:

Proliferating cell nuclear antigen

RPA:

Replication protein A

CBD:

Chitin binding domain

C-UNG2:

Residues 93–313 of UNG2-G93C

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Acknowledgements

This work was financed by the MARPOL project, the Norwegian NMR Platform and a FRINAT project, all from the Research Council of Norway (Grant Numbers 221576, 226244, and 221538, respectively).

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Author notes

  1. Siv Å. Wiik

    Present address: Department of Nutrition, Institute of Basic Medical Sciences, University of Oslo, 0317, Oslo, Norway

Authors and Affiliations

  1. NOBIPOL, Department of Biotechnology, NTNU-Norwegian University of Science and Technology, 7491, Trondheim, Norway

    Edith Buchinger, Siv Å. Wiik & Finn L. Aachmann

  2. Department of Cancer Research and Molecular Medicine, NTNU - Norwegian University of Science and Technology, 7491, Trondheim, Norway

    Anna Kusnierczyk, Renana Rabe, Per. A. Aas, Bodil Kavli & Geir Slupphaug

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  1. Edith Buchinger
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Correspondence to Finn L. Aachmann.

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Buchinger, E., Wiik, S.Å., Kusnierczyk, A. et al. Backbone 1H, 13C and 15N chemical shift assignment of full-length human uracil DNA glycosylase UNG2. Biomol NMR Assign 12, 15–22 (2018). https://doi.org/10.1007/s12104-017-9772-5

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