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

Yonsei University
Seoul National University
Korea Basic Science Institute

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

1 Scopus citations

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
State	Published - 1 Jan 2021
Externally published	Yes

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

BAF60A
NMR
p53
SWItch/Sucrose non-fermentable
Tumor suppressor

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10.1016/j.bbrc.2020.10.101

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@article{1ae6f720086341efa9226b2be96adfed,

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.",

keywords = "BAF60A, NMR, p53, SWItch/Sucrose non-fermentable, Tumor suppressor",

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",

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year = "2021",

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day = "1",

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

language = "English",

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TY - JOUR

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

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.

KW - BAF60A

KW - NMR

KW - p53

KW - SWItch/Sucrose non-fermentable

KW - Tumor suppressor

UR - https://www.scopus.com/pages/publications/85095752279

U2 - 10.1016/j.bbrc.2020.10.101

DO - 10.1016/j.bbrc.2020.10.101

M3 - Article

C2 - 33168186

AN - SCOPUS:85095752279

SN - 0006-291X

VL - 534

SP - 815

EP - 821

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

ER -

NMR spectroscopy uncovers direct interaction between BAF60A and p53

Abstract

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Keywords

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