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- Title
A Coil-to-Helix Transition Serves as a Binding Motif for hSNF5 and BAF155 Interaction.
- Authors
Han, Jeongmin; Kim, Iktae; Park, Jae-Hyun; Yun, Ji-Hye; Joo, Keehyoung; Kim, Taehee; Park, Gye-Young; Ryu, Kyoung-Seok; Ko, Yoon-Joo; Mizutani, Kenji; Park, Sam-Young; Seong, Rho Hyun; Lee, Jooyoung; Suh, Jeong-Yong; Lee, Weontae
- Abstract
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 hSNF5171–258 and BAF155SWIRM are both monomeric in solution and they form a heterodimer. NMR data and crystal structure of the hSNF5171–258/BAF155SWIRM complex further reveal a unique binding interface, which involves a coil-to-helix transition upon protein binding. The newly formed αN helix of hSNF5171–258 interacts with the β2–α1 loop of hSNF5 via hydrogen bonds and it also displays a hydrophobic interaction with BAF155SWIRM. Therefore, the N-terminal region of hSNF5171–258 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.
- Subjects
CHROMATIN-remodeling complexes; X-ray crystallography; NUCLEAR magnetic resonance; HYDROPHOBIC interactions; PROTEIN binding; LIGHT scattering
- Publication
International Journal of Molecular Sciences, 2020, Vol 21, Issue 7, p2452
- ISSN
1661-6596
- Publication type
Article
- DOI
10.3390/ijms21072452