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식물노화·수명연구단
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The C-Domain of the NAC Transcription Factor ANAC019 Is Necessary for pH-Tuned DNA Binding through a Histidine Switch in the N-Domain

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Title
The C-Domain of the NAC Transcription Factor ANAC019 Is Necessary for pH-Tuned DNA Binding through a Histidine Switch in the N-Domain
Author(s)
Mooseok Kang; Sangyeol Kim; Hyo Jung Kim; Shrestha, P; Yun, JH; Bong-Kwan Phee; Weontae Lee; Hong Gil Nam; Iksoo Chang
Subject
electric dipole moment, ; histidine switch, ; intrinsically disordered region, ; pH-tuned DNA-binding affinity, ; transcription factor
Publication Date
2018-01
Journal
CELL REPORTS, v.22, no.5, pp.1141 - 1150
Publisher
CELL PRESS
Abstract
The affinity of transcription factors (TFs) for their target DNA is a critical determinant of gene expression. Whether the DNA-binding domain (DBD) of TFs alone can regulate binding affinity to DNA is an important question for identifying the design principle of TFs. We studied ANAC019, a member of the NAC TF family of proteins in Arabidopsis, and found a well-conserved histidine switch located in its DBD, which regulates both homodimerization and transcriptional control of the TF through H135 protonation. We found that the removal of a C-terminal intrinsically disordered region (IDR) in the TF abolished the pH-dependent binding of the N-terminal DBD to DNA. We propose a mechanism in which long-range electrostatic interactions between DNA and the negatively charged C-terminal IDR turns on the pH dependency of the DNA-binding affinity of the N-terminal DBD (c) 2018 The Authors
URI
https://pr.ibs.re.kr/handle/8788114/4707
DOI
10.1016/j.celrep.2018.01.002
ISSN
2211-1247
Appears in Collections:
Center for Plant Aging Research (식물 노화·수명 연구단) > 1. Journal Papers (저널논문)
Files in This Item:
Cell Reports_Vol. 22(5) pp. 1141-1150.pdfDownload

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