Backbone resonance assignments for the SET domain of human methyltransferase NSD3 in complex with its cofactor.

Yan Li, Hui Qi Ng, Anna Ngo, Shuang Liu, Yih Wan Tan, Perlyn Zekui Kwek, Alvin W Hung, Joma Joy, Jeffrey Hill, Thomas H Keller, CongBao Kang

Journal: Biomolecular NMR assignments 2018;11(2):225-229

PMID: 28808922

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Abstract

NSD3 is a histone H3 methyltransferase that plays an important role in chromatin biology. A construct containing the methyltransferase domain encompassing residues Q1049-K1299 of human NSD3 was obtained and biochemical activity was demonstrated using histone as a substrate. Here we report the backbone HN, N, Cα, C', and side chain Cβ assignments of the construct in complex with S-adenosyl-L-methionine (SAM). Based on these assignments, secondary structures of NSD3/SAM complex in solution were determined.

Address: Experimental Therapeutics Centre, Agency for Science, Technology and Research, 31 Biopolis Way Nanos, #03-01, Singapore, 138669, Singapore.; Experimental Therapeutics Centre, Agency for Science, Technology and Research, 31 Biopolis Way Nanos, #03-01, Singapore, 138669, Singapore. [email protected].

DOI: 10.1007/s12104-017-9753-8

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MeSH Terms: Amino Acid Sequence, Coenzymes, Histone-Lysine N-Methyltransferase, Humans, Nuclear Magnetic Resonance, Biomolecular, Nuclear Proteins, PR-SET Domains