An evolutionarily conserved iron-sulfur cluster underlies redox sensory function of the Chloroplast Sensor Kinase
Abstract
Photosynthetic efficiency depends on equal light energy conversion by two spectrally distinct, serially-connected photosystems. The redox state of the plastoquinone pool, located between the two photosystems, is a key regulatory signal that initiates acclimatory changes in the relative abundance of photosystems. The Chloroplast Sensor Kinase (CSK) links the plastoquinone redox signal with photosystem gene expression but the mechanism by which it monitors the plastoquinone redox state is unclear. Here we show that the purified Arabidopsis and Phaeodactylum CSK and the cyanobacterial CSK homologue, Histidine kinase 2 (Hik2), are iron-sulfur proteins. The Fe-S cluster of CSK is further revealed to be a high potential redox-responsive [3Fe-4S] center. CSK responds to redox agents with reduced plastoquinone suppressing its autokinase activity. Redox changes within the CSK iron-sulfur cluster translate into conformational changes in the protein fold. These results provide key insights into redox signal perception and propagation by the CSK-based chloroplast two-component system.
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS); Purdue Univ., West Lafayette, IN (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES); Showalter Trust; National Science Foundation (NSF); Canadian Light Source
- OSTI Identifier:
- 1624537
- Grant/Contract Number:
- AC02-06CH11357; SC0018238; CHE-1900476
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Communications Biology
- Additional Journal Information:
- Journal Volume: 3; Journal Issue: 1; Journal ID: ISSN 2399-3642
- Publisher:
- Springer Nature
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; life sciences & biomedicine - other topics; science & technology - other topics; C3 photosynthesis; light responses
Citation Formats
Ibrahim, Iskander M., Wu, Huan, Ezhov, Roman, Kayanja, Gilbert E., Zakharov, Stanislav D., Du, Yanyan, Tao, Weiguo Andy, Pushkar, Yulia, Cramer, William A., and Puthiyaveetil, Sujith. An evolutionarily conserved iron-sulfur cluster underlies redox sensory function of the Chloroplast Sensor Kinase. United States: N. p., 2020.
Web. doi:10.1038/s42003-019-0728-4.
Ibrahim, Iskander M., Wu, Huan, Ezhov, Roman, Kayanja, Gilbert E., Zakharov, Stanislav D., Du, Yanyan, Tao, Weiguo Andy, Pushkar, Yulia, Cramer, William A., & Puthiyaveetil, Sujith. An evolutionarily conserved iron-sulfur cluster underlies redox sensory function of the Chloroplast Sensor Kinase. United States. https://doi.org/10.1038/s42003-019-0728-4
Ibrahim, Iskander M., Wu, Huan, Ezhov, Roman, Kayanja, Gilbert E., Zakharov, Stanislav D., Du, Yanyan, Tao, Weiguo Andy, Pushkar, Yulia, Cramer, William A., and Puthiyaveetil, Sujith. Wed .
"An evolutionarily conserved iron-sulfur cluster underlies redox sensory function of the Chloroplast Sensor Kinase". United States. https://doi.org/10.1038/s42003-019-0728-4. https://www.osti.gov/servlets/purl/1624537.
@article{osti_1624537,
title = {An evolutionarily conserved iron-sulfur cluster underlies redox sensory function of the Chloroplast Sensor Kinase},
author = {Ibrahim, Iskander M. and Wu, Huan and Ezhov, Roman and Kayanja, Gilbert E. and Zakharov, Stanislav D. and Du, Yanyan and Tao, Weiguo Andy and Pushkar, Yulia and Cramer, William A. and Puthiyaveetil, Sujith},
abstractNote = {Photosynthetic efficiency depends on equal light energy conversion by two spectrally distinct, serially-connected photosystems. The redox state of the plastoquinone pool, located between the two photosystems, is a key regulatory signal that initiates acclimatory changes in the relative abundance of photosystems. The Chloroplast Sensor Kinase (CSK) links the plastoquinone redox signal with photosystem gene expression but the mechanism by which it monitors the plastoquinone redox state is unclear. Here we show that the purified Arabidopsis and Phaeodactylum CSK and the cyanobacterial CSK homologue, Histidine kinase 2 (Hik2), are iron-sulfur proteins. The Fe-S cluster of CSK is further revealed to be a high potential redox-responsive [3Fe-4S] center. CSK responds to redox agents with reduced plastoquinone suppressing its autokinase activity. Redox changes within the CSK iron-sulfur cluster translate into conformational changes in the protein fold. These results provide key insights into redox signal perception and propagation by the CSK-based chloroplast two-component system.},
doi = {10.1038/s42003-019-0728-4},
journal = {Communications Biology},
number = 1,
volume = 3,
place = {United States},
year = {Wed Jan 08 00:00:00 EST 2020},
month = {Wed Jan 08 00:00:00 EST 2020}
}
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Figures / Tables:
Fig. 1: UV-Vis absorbance spectra of cyanobacterial and chloroplast CSK proteins. Coloration of the purified and reconstituted proteins. a On the far-left side is Syn-CSK purified from bacteria, followed by buffer control and the reconstituted CSK proteins. UV-Vis absorbance spectra of b Synechocystis sp. PCC 6803 CSK, c Phaeodactylum tricornutummore »
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