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Peer-reviewedCC BY-NC-NDNature communications

A ubiquitin carboxyl-terminal hydrolase facilitates H2A.Z removal in response to phosphate starvation.

  • Fanxiao Meng1,2,3
  • Xinlong Xiao2,4
  • Guojie Ma1
  • Viswanathan Satheesh5
  • Qigui Wu6
  • Yuhang Zhao2,3
  • Hao Chen1
  • Xianwei Lu1
  • Junfeng Jiang1
  • Mingguang Lei7
  • Mingguang Lei7
7 affiliations
  1. 1College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, China.
  2. 2Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai, China.
  3. 3University of Chinese Academy of Sciences, Beijing, China.
  4. 4State Key Laboratory of Ecological Safety and Sustainable Development in Arid Lands, Xinjiang Institute of Ecology and Geography, Chinese Academy of Sciences, Urumqi, China.
  5. 5Genome Informatics Facility, Office of Biotechnology, Iowa State University, Ames, IA, USA.
  6. 6Key Laboratory of Multi-Cell Systems, Shanghai Key Laboratory of Molecular Andrology, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Shanghai, China.
  7. 7College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, China. [email protected].
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Abstract

The histone variant H2A.Z plays a critical role in the modulation of environmental responses, but the mechanisms regulating H2A.Z dynamics in response to stresses remain poorly understood in plants. Here we identify the ubiquitin carboxyl-terminal hydrolase UCH2 as a Pi-responsive chromatin regulator that promotes Pi starvation-induced (PSI) gene activation. We show that PHR1 recruits UCH2 to PSI gene promoters under Pi deficiency, where UCH2 deubiquitinates H2A.Z and promotes reduction in H2A.Z occupancy at PSI gene promoters. Loss of UCH2 impairs this reduction in H2A.Z occupancy, represses PSI gene induction, and reduces Pi accumulation. A catalytically inactive UCH2 mutant fails to complement these defects, and ubiquitination-deficient H2A.Z variants render plants insensitive to UCH2 loss. Our findings establish UCH2 as a critical chromatin regulator linking Pi sensing with H2A.Z dynamics and provide insights into how plants integrate chromatin-based regulation to maintain Pi homeostasis.

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Cite

BibTeXRIS
BibTeX
@article{meng2026ubiquitin,
  title = {{A ubiquitin carboxyl-terminal hydrolase facilitates H2A.Z removal in response to phosphate starvation.}},
  author = {Fanxiao Meng and Xinlong Xiao and Guojie Ma and Viswanathan Satheesh and Qigui Wu and Yuhang Zhao and Hao Chen and Xianwei Lu and Junfeng Jiang and Mingguang Lei and Mingguang Lei},
  journal = {Nature communications},
  year = {2026},
  month = sep,
  doi = {10.1038/s41467-026-77882-6},
  url = {https://europepmc.org/article/MED/42897203},
  note = {CC BY-NC-ND},
}
RIS
TY  - JOUR
TI  - A ubiquitin carboxyl-terminal hydrolase facilitates H2A.Z removal in response to phosphate starvation.
AU  - Fanxiao Meng
AU  - Xinlong Xiao
AU  - Guojie Ma
AU  - Viswanathan Satheesh
AU  - Qigui Wu
AU  - Yuhang Zhao
AU  - Hao Chen
AU  - Xianwei Lu
AU  - Junfeng Jiang
AU  - Mingguang Lei
AU  - Mingguang Lei
PY  - 2026
DA  - 2026/09/18
JO  - Nature communications
DO  - 10.1038/s41467-026-77882-6
UR  - https://europepmc.org/article/MED/42897203
AB  - The histone variant H2A.Z plays a critical role in the modulation of environmental responses, but the mechanisms regulating H2A.Z dynamics in response to stresses remain poorly understood in plants. Here we identify the ubiquitin carboxyl-terminal hydrolase UCH2 as a Pi-responsive chromatin regulator that promotes Pi starvation-induced (PSI) gene activation. We show that PHR1 recruits UCH2 to PSI gene promoters under Pi deficiency, where UCH2 deubiquitinates H2A.Z and promotes reduction in H2A.Z occupancy at PSI gene promoters. Loss of UCH2 impairs this reduction in H2A.Z occupancy, represses PSI gene induction, and reduces Pi accumulation. A catalytically inactive UCH2 mutant fails to complement these defects, and ubiquitination-deficient H2A.Z variants render plants insensitive to UCH2 loss. Our findings establish UCH2 as a critical chromatin regulator linking Pi sensing with H2A.Z dynamics and provide insights into how plants integrate chromatin-based regulation to maintain Pi homeostasis.
SN  - 2041-1723
ER  -