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Article

A Coil-to-Helix Transition Serves as a Binding Motif for hSNF5 and BAF155 Interaction

1
Structural Biochemistry & Molecular Biophysics Laboratory, Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-740, Korea
2
Department of Agricultural Biotechnology and Research Institute of Agriculture and Life Sciences, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 08826, Korea
3
Center for In Silico Protein Science and Center for Advanced Computation, Korea Institute for Advanced Study, Seoul 130-722, Korea
4
Division of Magnetic Resonance Research, Korea Basic Science Institute, Yangcheong-Ri 804-1, Ochang-Eup, Cheongwon-Gun, Chungcheongbuk-Do 363-883, Korea
5
National Center for Inter-University Research Facilities, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 08826, Korea
6
Drug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, Tsurumi, Yokohama 230-0045, Japan
7
Department of Biological Sciences, Institute of Molecular Biology and Genetics, Research Center for Functional Cellulomics, Seoul National University, Seoul 151-742, Korea
8
Center for In Silico Protein Science and School of Computational Sciences, Korea Institute for Advanced Study, Seoul 130-722, Korea
*
Authors to whom correspondence should be addressed.
These authors contributed equally.
Int. J. Mol. Sci. 2020, 21(7), 2452; https://doi.org/10.3390/ijms21072452
Received: 13 March 2020 / Revised: 27 March 2020 / Accepted: 30 March 2020 / Published: 1 April 2020
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. View Full-Text
Keywords: BAF155; hSNF5; coupled folding and binding; NMR spectroscopy; X-ray crystallography BAF155; hSNF5; coupled folding and binding; NMR spectroscopy; X-ray crystallography
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MDPI and ACS Style

Han, J.; Kim, I.; Park, J.-H.; Yun, J.-H.; Joo, K.; Kim, T.; Park, G.-Y.; Ryu, K.-S.; Ko, Y.-J.; Mizutani, K.; Park, S.-Y.; Seong, R.H.; Lee, J.; Suh, J.-Y.; Lee, W. A Coil-to-Helix Transition Serves as a Binding Motif for hSNF5 and BAF155 Interaction. Int. J. Mol. Sci. 2020, 21, 2452. https://doi.org/10.3390/ijms21072452

AMA Style

Han J, Kim I, Park J-H, Yun J-H, Joo K, Kim T, Park G-Y, Ryu K-S, Ko Y-J, Mizutani K, Park S-Y, Seong RH, Lee J, Suh J-Y, Lee W. A Coil-to-Helix Transition Serves as a Binding Motif for hSNF5 and BAF155 Interaction. International Journal of Molecular Sciences. 2020; 21(7):2452. https://doi.org/10.3390/ijms21072452

Chicago/Turabian Style

Han, Jeongmin, Iktae Kim, Jae-Hyun Park, Ji-Hye Yun, Keehyoung Joo, Taehee Kim, Gye-Young Park, Kyoung-Seok Ryu, Yoon-Joo Ko, Kenji Mizutani, Sam-Young Park, Rho H. Seong, Jooyoung Lee, Jeong-Yong Suh, and Weontae Lee. 2020. "A Coil-to-Helix Transition Serves as a Binding Motif for hSNF5 and BAF155 Interaction" International Journal of Molecular Sciences 21, no. 7: 2452. https://doi.org/10.3390/ijms21072452

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