Resonance assignments for the tandem PWWP-ARID domains of human RBBP1

Weibin Gong; Xingzhe Yao; Qihui Liang; Yufeng Tong; Sarah Perrett; Yingang Feng

doi:10.1007/s12104-019-09873-2

Resonance assignments for the tandem PWWP-ARID domains of human RBBP1

Biomol NMR Assign. 2019 Apr;13(1):177-181. doi: 10.1007/s12104-019-09873-2. Epub 2019 Jan 21.

Authors

Weibin Gong¹, Xingzhe Yao^{2

3

4}, Qihui Liang^{1

4}, Yufeng Tong⁵, Sarah Perrett^{6

7}, Yingang Feng^{8

9}

Affiliations

¹ National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
² Shandong Provincial Key Laboratory of Synthetic Biology, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China.
³ CAS Key Laboratory of Biofuels, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China.
⁴ University of the Chinese Academy of Sciences, 19A Yuquan Road, Shijingshan District, Beijing, 100049, China.
⁵ Department of Chemistry & Biochemistry, University of Windsor, Windsor, ON, N9B 3P4, Canada.
⁶ National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China. sarah.perrett@cantab.net.
⁷ University of the Chinese Academy of Sciences, 19A Yuquan Road, Shijingshan District, Beijing, 100049, China. sarah.perrett@cantab.net.
⁸ Shandong Provincial Key Laboratory of Synthetic Biology, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China. fengyg@qibebt.ac.cn.
⁹ CAS Key Laboratory of Biofuels, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China. fengyg@qibebt.ac.cn.

PMID: 30666492
DOI: 10.1007/s12104-019-09873-2

Abstract

Retinoblastoma-binding protein 1 (RBBP1), also known as AT-rich interaction domain 4A (ARID4A), is a tumour suppressor involved in the regulation of the epigenetic programming in leukemia and Prader-Willi/Angelman syndromes. The ARID domain of RBBP1 binds to DNA non-specifically and has gene suppression activity. However, no structural data has been obtained for the human RBBP1 ARID domain so far. Here we report the near-complete ¹H, ¹³C, ¹⁵N backbone and side-chain NMR assignment of a 27 kDa tandem PWWP-ARID domain construct that spans residues 171-414 with the removal of a short disordered region between the two domains. The predicted secondary structure based on the assigned chemical shifts is consistent with the structures of the isolated PWWP domain of human RBBP1 previously solved and the homologous ARID domains of other proteins.

Keywords: ARID domain; NMR assignments; RBBP1; Secondary structure; Tandem domains.

Publication types

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

MeSH terms

Amino Acid Sequence
Humans
Nuclear Magnetic Resonance, Biomolecular*
Protein Structure, Tertiary
Retinoblastoma-Binding Protein 1 / chemistry*

Substances

ARID4A protein, human
Retinoblastoma-Binding Protein 1