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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
- 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, Moo Seok; Kim, Sang Yeol; Kim, Hyo Jung; Shrestha, Pravesh; Yun, Ji-Hye; Phee, Bong-Kwan; Lee, Weontae; Nam, Hong Gil; Chang, Ik Soo
- DGIST Authors
- Nam, Hong Gil; Chang, Ik Soo
- Issue Date
- Cell Reports, 22(5), 1141-1150
- Article Type
- ARABIDOPSIS-THALIANA; SIGNAL-TRANSDUCTION; FACTOR FAMILY; MEMBER
- 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.
- CELL PRESS
- Related Researcher
Chang, Ik Soo
Theoretical and Computational Biophysics Laboratory
Theoretical and Computational Biophysics; Supercomputing Simulation of Biomolecules; 이론?계산 생물물리학; 통계물리학; 단백질체의 슈퍼컴퓨터 모델링 및 시물레이션
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