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Biomolecular NMR Assignments

, Volume 12, Issue 1, pp 15–22 | Cite as

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

  • Edith Buchinger
  • Siv Å. Wiik
  • Anna Kusnierczyk
  • Renana Rabe
  • Per. A. Aas
  • Bodil Kavli
  • Geir Slupphaug
  • Finn L. Aachmann
Article
First Online:
Received:
Accepted:

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.

Keywords

Uracil-DNA glycosylase Uracil N-glycosylase isoform 2 UNG2 DNA repair Intrinsically disordered domain 

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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Notes

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).

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

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Copyright information

© Springer Science+Business Media B.V. 2017

Authors and Affiliations

  1. 1.NOBIPOL, Department of BiotechnologyNTNU-Norwegian University of Science and TechnologyTrondheimNorway
  2. 2.Department of Cancer Research and Molecular MedicineNTNU - Norwegian University of Science and TechnologyTrondheimNorway
  3. 3.Department of Nutrition, Institute of Basic Medical SciencesUniversity of OsloOsloNorway

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