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

doi:10.1007/s12104-017-9772-5

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

Biomol NMR Assign. 2018 Apr;12(1):15-22. doi: 10.1007/s12104-017-9772-5. Epub 2017 Sep 6.

Authors

Edith Buchinger¹, Siv Å Wiik^{1

2}, Anna Kusnierczyk³, Renana Rabe³, Per A Aas³, Bodil Kavli³, Geir Slupphaug³, Finn L Aachmann⁴

Affiliations

¹ NOBIPOL, Department of Biotechnology, NTNU-Norwegian University of Science and Technology, 7491, Trondheim, Norway.
² Department of Nutrition, Institute of Basic Medical Sciences, University of Oslo, 0317, Oslo, Norway.
³ Department of Cancer Research and Molecular Medicine, NTNU - Norwegian University of Science and Technology, 7491, Trondheim, Norway.
⁴ NOBIPOL, Department of Biotechnology, NTNU-Norwegian University of Science and Technology, 7491, Trondheim, Norway. finn.l.aachmann@ntnu.no.

PMID: 28879561
DOI: 10.1007/s12104-017-9772-5

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

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

DNA Glycosylases / chemistry*
DNA Glycosylases / metabolism
Humans
Nuclear Magnetic Resonance, Biomolecular*
Protein Domains
Protein Structure, Secondary

Substances

CCNO protein, human
DNA Glycosylases