期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 21, 期 7, 页码 -出版社
MDPI
DOI: 10.3390/ijms21072452
关键词
BAF155; hSNF5; coupled folding and binding; NMR spectroscopy; X-ray crystallography
资金
- National Research Foundation of Korea (NRF) [NRF-2017R1A2B2008483, 2019M3A9F6021810, NRF-2017M3A9F6029753, NRF-2019M3E5D6063903, NRF-20161A6A3A04010213, NRF-2018R1D1A1B07049312, NRF-2017R1E1A1A01077717]
- Brain Korea Plus (BK+) program
- Cooperative Research Program for Agriculture Science & Technology Development, Rural Development Administration, Republic of Korea [PJ011112, PJ01495901]
- Creative-Pioneering Researchers Program, through Seoul National University (SNU)
- National Research Foundation of Korea [2019M3E5D6063903] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Human SNF5 and BAF155 constitute the core subunit of multi-protein SWI/SNF chromatin-remodeling complexes that are required for ATP-dependent nucleosome mobility and transcriptional control. Human SNF5 (hSNF5) utilizes its repeat 1 (RPT1) domain to associate with the SWIRM domain of BAF155. Here, we employed X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and various biophysical methods in order to investigate the detailed binding mechanism between hSNF5 and BAF155. Multi-angle light scattering data clearly indicate that hSNF5(171-258) and BAF155(SWIRM) are both monomeric in solution and they form a heterodimer. NMR data and crystal structure of the hSNF5(171-258)/BAF155(SWIRM) complex further reveal a unique binding interface, which involves a coil-to-helix transition upon protein binding. The newly formed alpha(N) helix of hSNF5(171-258) interacts with the beta 2-alpha 1 loop of hSNF5 via hydrogen bonds and it also displays a hydrophobic interaction with BAF155(SWIRM). Therefore, the N-terminal region of hSNF5(171-258) plays an important role in tumorigenesis and our data will provide a structural clue for the pathogenesis of Rhabdoid tumors and malignant melanomas that originate from mutations in the N-terminal loop region of hSNF5.
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