Cryptococcal Hsf3 controls intramitochondrial ROS homeostasis by regulating the respiratory process

Xindi Gao, Yi Fu, Shengyi Sun, Tingyi Gu, Yanjian Li, Tianshu Sun, Hailong Li, Wei Du, Chenhao Suo, Chao Li, Yiru Gao, Yang Meng, Yue Ni, Sheng Yang, Tian Lan, Sixiang Sai, Jiayi Li, Kun Yu, Ping Wang and Chen Ding ()
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Xindi Gao: Northeastern University
Yi Fu: Northeastern University
Shengyi Sun: Northeastern University
Tingyi Gu: Northeastern University
Yanjian Li: Northeastern University
Tianshu Sun: Beijing Key Laboratory for Mechanisms Research and Precision Diagnosis of Invasive Fungal Diseases
Hailong Li: The First Affiliated Hospital of China Medical University
Wei Du: Northeastern University
Chenhao Suo: Northeastern University
Chao Li: Northeastern University
Yiru Gao: Northeastern University
Yang Meng: Northeastern University
Yue Ni: Northeastern University
Sheng Yang: Northeastern University
Tian Lan: Northeastern University
Sixiang Sai: Binzhou Medical University
Jiayi Li: BMC A10
Kun Yu: Northeastern University
Ping Wang: Louisiana State University Health Sciences Center
Chen Ding: Northeastern University

Nature Communications, 2022, vol. 13, issue 1, 1-16

Abstract: Abstract Mitochondrial quality control prevents accumulation of intramitochondrial-derived reactive oxygen species (mtROS), thereby protecting cells against DNA damage, genome instability, and programmed cell death. However, underlying mechanisms are incompletely understood, particularly in fungal species. Here, we show that Cryptococcus neoformans heat shock factor 3 (CnHsf3) exhibits an atypical function in regulating mtROS independent of the unfolded protein response. CnHsf3 acts in nuclei and mitochondria, and nuclear- and mitochondrial-targeting signals are required for its organelle-specific functions. It represses the expression of genes involved in the tricarboxylic acid cycle while promoting expression of genes involved in electron transfer chain. In addition, CnHsf3 responds to multiple intramitochondrial stresses; this response is mediated by oxidation of the cysteine residue on its DNA binding domain, which enhances DNA binding. Our results reveal a function of HSF proteins in regulating mtROS homeostasis that is independent of the unfolded protein response.

Date: 2022
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DOI: 10.1038/s41467-022-33168-1

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