A coil-to-helix transition serves as a binding motif for hSNF5 and BAF155 interaction

Jeongmin Han; 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 Hyun Seong; Jooyoung Lee; Jeong Yong Suh; Weontae Lee

doi:10.3390/ijms21072452

A coil-to-helix transition serves as a binding motif for hSNF5 and BAF155 interaction

Jeongmin Han, 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 Hyun Seong, Jooyoung Lee, Jeong Yong Suh, Weontae Lee

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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 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 α_N helix of hSNF5^171–258 interacts with the β2–α1 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.

Original language	English
Article number	2452
Journal	International journal of molecular sciences
Volume	21
Issue number	7
DOIs	https://doi.org/10.3390/ijms21072452
Publication status	Published - 2020 Apr 1

Bibliographical note

Funding Information:
Funding: This work was supported by several grants (NRF-2017R1A2B2008483, 2019M3A9F6021810, NRF-2017M3A9F6029753, NRF-2019M3E5D6063903 to W. Lee, NRF-20161A6A3A04010213 to J.-H. Yun, NRF-2018R1D1A1B07049312 to K.J. and NRF-2017R1E1A1A01077717 to J.L.), through the National Research Foundation of Korea (NRF) and Brain Korea Plus (BK+) program (J. Han). This research was also supported by the Cooperative Research Program for Agriculture Science & Technology Development, Rural Development Administration, Republic of Korea (PJ011112, PJ01495901), and the Creative-Pioneering Researchers Program, through Seoul National University (SNU).

Funding Information:
Acknowledgments: We thank the Research Institute of Agriculture and Life Sciences, the high-field NMR facility at the Korea Institute of Science and Technology, the Korea Basic Science Institute, and the National Center for Inter-University Research Facilities. We would like to express our gratitude to the staff scientists at the NCI station of the Pohang Accelerator Laboratory X-ray Free-Electron Laser, 5C and 7C beamline of the Pohang Accelerator Laboratory.

Publisher Copyright:
© 2020 by the authors. Licensee MDPI, Basel, Switzerland.

All Science Journal Classification (ASJC) codes

Catalysis
Molecular Biology
Spectroscopy
Computer Science Applications
Physical and Theoretical Chemistry
Organic Chemistry
Inorganic Chemistry

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@article{aff0ed79e12646228184e51914a85e90,

title = "A coil-to-helix transition serves as a binding motif for hSNF5 and BAF155 interaction",

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.",

author = "Jeongmin Han and Iktae Kim and Park, {Jae Hyun} and Yun, {Ji Hye} and Keehyoung Joo and Taehee Kim and Park, {Gye Young} and Ryu, {Kyoung Seok} and Ko, {Yoon Joo} and Kenji Mizutani and Park, {Sam Young} and Seong, {Rho Hyun} and Jooyoung Lee and Suh, {Jeong Yong} and Weontae Lee",

note = "Funding Information: Funding: This work was supported by several grants (NRF-2017R1A2B2008483, 2019M3A9F6021810, NRF-2017M3A9F6029753, NRF-2019M3E5D6063903 to W. Lee, NRF-20161A6A3A04010213 to J.-H. Yun, NRF-2018R1D1A1B07049312 to K.J. and NRF-2017R1E1A1A01077717 to J.L.), through the National Research Foundation of Korea (NRF) and Brain Korea Plus (BK+) program (J. Han). This research was also supported by the Cooperative Research Program for Agriculture Science & Technology Development, Rural Development Administration, Republic of Korea (PJ011112, PJ01495901), and the Creative-Pioneering Researchers Program, through Seoul National University (SNU). Funding Information: Acknowledgments: We thank the Research Institute of Agriculture and Life Sciences, the high-field NMR facility at the Korea Institute of Science and Technology, the Korea Basic Science Institute, and the National Center for Inter-University Research Facilities. We would like to express our gratitude to the staff scientists at the NCI station of the Pohang Accelerator Laboratory X-ray Free-Electron Laser, 5C and 7C beamline of the Pohang Accelerator Laboratory. Publisher Copyright: {\textcopyright} 2020 by the authors. Licensee MDPI, Basel, Switzerland.",

year = "2020",

month = apr,

day = "1",

doi = "10.3390/ijms21072452",

language = "English",

volume = "21",

journal = "International Journal of Molecular Sciences",

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T1 - A coil-to-helix transition serves as a binding motif for hSNF5 and BAF155 interaction

AU - Han, Jeongmin

AU - Kim, Iktae

AU - Park, Jae Hyun

AU - Yun, Ji Hye

AU - Joo, Keehyoung

AU - Kim, Taehee

AU - Park, Gye Young

AU - Ryu, Kyoung Seok

AU - Ko, Yoon Joo

AU - Mizutani, Kenji

AU - Park, Sam Young

AU - Seong, Rho Hyun

AU - Lee, Jooyoung

AU - Suh, Jeong Yong

AU - Lee, Weontae

N1 - Funding Information: Funding: This work was supported by several grants (NRF-2017R1A2B2008483, 2019M3A9F6021810, NRF-2017M3A9F6029753, NRF-2019M3E5D6063903 to W. Lee, NRF-20161A6A3A04010213 to J.-H. Yun, NRF-2018R1D1A1B07049312 to K.J. and NRF-2017R1E1A1A01077717 to J.L.), through the National Research Foundation of Korea (NRF) and Brain Korea Plus (BK+) program (J. Han). This research was also supported by the Cooperative Research Program for Agriculture Science & Technology Development, Rural Development Administration, Republic of Korea (PJ011112, PJ01495901), and the Creative-Pioneering Researchers Program, through Seoul National University (SNU). Funding Information: Acknowledgments: We thank the Research Institute of Agriculture and Life Sciences, the high-field NMR facility at the Korea Institute of Science and Technology, the Korea Basic Science Institute, and the National Center for Inter-University Research Facilities. We would like to express our gratitude to the staff scientists at the NCI station of the Pohang Accelerator Laboratory X-ray Free-Electron Laser, 5C and 7C beamline of the Pohang Accelerator Laboratory. Publisher Copyright: © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

PY - 2020/4/1

Y1 - 2020/4/1

N2 - 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.

AB - 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.

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A coil-to-helix transition serves as a binding motif for hSNF5 and BAF155 interaction

Abstract

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