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. Kang et al. find a histidine switch in the DNA-binding N-domain of the transcription factor ANAC019 that regulates both pH-dependent homodimerization and DNA binding. They propose that long-range electrostatic interactions between DNA and the negatively charged C-terminal turns on the pH dependency of the DNA-binding affinity of the N-terminal DNA-binding domain.
| Original language | English |
|---|---|
| Pages (from-to) | 1141-1150 |
| Number of pages | 10 |
| Journal | Cell Reports |
| Volume | 22 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 2018 Jan 30 |
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All Science Journal Classification (ASJC) codes
- Biochemistry, Genetics and Molecular Biology(all)
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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. / Kang, Mooseok; Kim, Sangyeol; Kim, Hyo Jung; Shrestha, Pravesh; Yun, Ji hye; Phee, Bong Kwan; Lee, Weon Tae; Nam, Hong Gil; Chang, Iksoo.
In: Cell Reports, Vol. 22, No. 5, 30.01.2018, p. 1141-1150.Research output: Contribution to journal › Article
TY - JOUR
T1 - The C-Domain of the NAC Transcription Factor ANAC019 Is Necessary for pH-Tuned DNA Binding through a Histidine Switch in the N-Domain
AU - Kang, Mooseok
AU - Kim, Sangyeol
AU - Kim, Hyo Jung
AU - Shrestha, Pravesh
AU - Yun, Ji hye
AU - Phee, Bong Kwan
AU - Lee, Weon Tae
AU - Nam, Hong Gil
AU - Chang, Iksoo
PY - 2018/1/30
Y1 - 2018/1/30
N2 - 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. Kang et al. find a histidine switch in the DNA-binding N-domain of the transcription factor ANAC019 that regulates both pH-dependent homodimerization and DNA binding. They propose that long-range electrostatic interactions between DNA and the negatively charged C-terminal turns on the pH dependency of the DNA-binding affinity of the N-terminal DNA-binding domain.
AB - 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. Kang et al. find a histidine switch in the DNA-binding N-domain of the transcription factor ANAC019 that regulates both pH-dependent homodimerization and DNA binding. They propose that long-range electrostatic interactions between DNA and the negatively charged C-terminal turns on the pH dependency of the DNA-binding affinity of the N-terminal DNA-binding domain.
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UR - http://www.scopus.com/inward/citedby.url?scp=85044864664&partnerID=8YFLogxK
U2 - 10.1016/j.celrep.2018.01.002
DO - 10.1016/j.celrep.2018.01.002
M3 - Article
C2 - 29386103
AN - SCOPUS:85044864664
VL - 22
SP - 1141
EP - 1150
JO - Cell Reports
JF - Cell Reports
SN - 2211-1247
IS - 5
ER -