NMR spectroscopy uncovers direct interaction between BAF60A and p53

Jeongmin Han; Taehee Kim; Sunjin Moon; Jae Hyun Park; Wonbin Lee; Yoon Joo Ko; Kyoung Seok Ryu; Ji Hye Yun; Weontae Lee

doi:10.1016/j.bbrc.2020.10.101

NMR spectroscopy uncovers direct interaction between BAF60A and p53

Jeongmin Han, Taehee Kim, Sunjin Moon, Jae Hyun Park, Wonbin Lee, Yoon Joo Ko, Kyoung Seok Ryu, Ji Hye Yun, Weontae Lee

Research output: Contribution to journal › Article › peer-review

1 Citation (Scopus)

Abstract

The BRG1-associated factor 60A (BAF60A), an SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1, has been known to be important for transcriptional activation and inhibition through the alteration of the DNA nucleosome. Although the association between BAF60A and p53 plays a critical role in tumor suppression, the interaction mode is still unclear. Here, we report the detailed interactions between BAF60A and p53 by both NMR spectroscopy and pull-down analysis. Both N-terminal region (BAF60A^NR) and the SWIB domain (BAF60A^SWIB) of BAF60A directly interact with the tetramerization domain of p53 (p53^TET). NMR data show that Ile315, Met366, Ala388, and Tyr390 of BAF60A^SWIB are mostly involved in p53^TET binding. The calculated dissociation constant (K_D) value between BAF60A^SWIB and p53^TET revealed relatively weak binding affinity, at approximately 0.3 ± 0.065 mM. Our data will enhance detailed interaction mechanism to elucidate the molecular basis of p53-mediated integration via BAF60A interaction.

Original language	English
Pages (from-to)	815-821
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	534
DOIs	https://doi.org/10.1016/j.bbrc.2020.10.101
Publication status	Published - 2021 Jan 1

Bibliographical note

Funding Information:
This work was supported by the Mid-career Researcher Program ( NRF-2017R1A2B2008483 , NRF-2019M3E5D6063903 , NRF-2017M3A9F6029753 to W. Lee and NRF-20161A6A3A04010213 to J. H. Yun) through the National Research Foundation of Korea (NRF) and the Brain Korea Plus (BK+) program (J.H. Park).

Publisher Copyright:
© 2020 Elsevier Inc.

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2020.10.101

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title = "NMR spectroscopy uncovers direct interaction between BAF60A and p53",

abstract = "The BRG1-associated factor 60A (BAF60A), an SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1, has been known to be important for transcriptional activation and inhibition through the alteration of the DNA nucleosome. Although the association between BAF60A and p53 plays a critical role in tumor suppression, the interaction mode is still unclear. Here, we report the detailed interactions between BAF60A and p53 by both NMR spectroscopy and pull-down analysis. Both N-terminal region (BAF60ANR) and the SWIB domain (BAF60ASWIB) of BAF60A directly interact with the tetramerization domain of p53 (p53TET). NMR data show that Ile315, Met366, Ala388, and Tyr390 of BAF60ASWIB are mostly involved in p53TET binding. The calculated dissociation constant (KD) value between BAF60ASWIB and p53TET revealed relatively weak binding affinity, at approximately 0.3 ± 0.065 mM. Our data will enhance detailed interaction mechanism to elucidate the molecular basis of p53-mediated integration via BAF60A interaction.",

author = "Jeongmin Han and Taehee Kim and Sunjin Moon and Park, {Jae Hyun} and Wonbin Lee and Ko, {Yoon Joo} and Ryu, {Kyoung Seok} and Yun, {Ji Hye} and Weontae Lee",

note = "Funding Information: This work was supported by the Mid-career Researcher Program ( NRF-2017R1A2B2008483 , NRF-2019M3E5D6063903 , NRF-2017M3A9F6029753 to W. Lee and NRF-20161A6A3A04010213 to J. H. Yun) through the National Research Foundation of Korea (NRF) and the Brain Korea Plus (BK+) program (J.H. Park). Publisher Copyright: {\textcopyright} 2020 Elsevier Inc.",

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doi = "10.1016/j.bbrc.2020.10.101",

language = "English",

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T1 - NMR spectroscopy uncovers direct interaction between BAF60A and p53

AU - Han, Jeongmin

AU - Kim, Taehee

AU - Moon, Sunjin

AU - Park, Jae Hyun

AU - Lee, Wonbin

AU - Ko, Yoon Joo

AU - Ryu, Kyoung Seok

AU - Yun, Ji Hye

AU - Lee, Weontae

N1 - Funding Information: This work was supported by the Mid-career Researcher Program ( NRF-2017R1A2B2008483 , NRF-2019M3E5D6063903 , NRF-2017M3A9F6029753 to W. Lee and NRF-20161A6A3A04010213 to J. H. Yun) through the National Research Foundation of Korea (NRF) and the Brain Korea Plus (BK+) program (J.H. Park). Publisher Copyright: © 2020 Elsevier Inc.

PY - 2021/1/1

Y1 - 2021/1/1

N2 - The BRG1-associated factor 60A (BAF60A), an SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1, has been known to be important for transcriptional activation and inhibition through the alteration of the DNA nucleosome. Although the association between BAF60A and p53 plays a critical role in tumor suppression, the interaction mode is still unclear. Here, we report the detailed interactions between BAF60A and p53 by both NMR spectroscopy and pull-down analysis. Both N-terminal region (BAF60ANR) and the SWIB domain (BAF60ASWIB) of BAF60A directly interact with the tetramerization domain of p53 (p53TET). NMR data show that Ile315, Met366, Ala388, and Tyr390 of BAF60ASWIB are mostly involved in p53TET binding. The calculated dissociation constant (KD) value between BAF60ASWIB and p53TET revealed relatively weak binding affinity, at approximately 0.3 ± 0.065 mM. Our data will enhance detailed interaction mechanism to elucidate the molecular basis of p53-mediated integration via BAF60A interaction.

AB - The BRG1-associated factor 60A (BAF60A), an SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1, has been known to be important for transcriptional activation and inhibition through the alteration of the DNA nucleosome. Although the association between BAF60A and p53 plays a critical role in tumor suppression, the interaction mode is still unclear. Here, we report the detailed interactions between BAF60A and p53 by both NMR spectroscopy and pull-down analysis. Both N-terminal region (BAF60ANR) and the SWIB domain (BAF60ASWIB) of BAF60A directly interact with the tetramerization domain of p53 (p53TET). NMR data show that Ile315, Met366, Ala388, and Tyr390 of BAF60ASWIB are mostly involved in p53TET binding. The calculated dissociation constant (KD) value between BAF60ASWIB and p53TET revealed relatively weak binding affinity, at approximately 0.3 ± 0.065 mM. Our data will enhance detailed interaction mechanism to elucidate the molecular basis of p53-mediated integration via BAF60A interaction.

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JO - Biochemical and Biophysical Research Communications

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ER -

NMR spectroscopy uncovers direct interaction between BAF60A and p53

Abstract

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