Journal
FEBS LETTERS
Volume 596, Issue 12, Pages 1533-1543Publisher
WILEY
DOI: 10.1002/1873-3468.14340
Keywords
Hik2; RpaA; RpaB; Rre1; thiol regulation; TrxA
Funding
- United States Department of Energy (DOE) [DE-SC0020639]
- U.S. Department of Energy (DOE) [DE-SC0018238]
- Henry Koffler Professorship
- Biotechnology and Biological Sciences Research Council [BB/L014130/1, BB/T010525/1]
- Engineering and Physical Sciences Research Council [EP/F047940/1]
- Spicer Consulting Ltd
- U.S. Department of Energy (DOE) [DE-SC0018238, DE-SC0020639] Funding Source: U.S. Department of Energy (DOE)
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Cyanobacteria employ two-component sensor-response regulator systems to monitor and respond to environmental challenges. The response regulators RpaA, RpaB, Rre1, and RppA are integral to circadian clock function and abiotic stress acclimation in cyanobacteria. Researchers have discovered that Rre1, RpaA, and RpaB exist as higher-order oligomers under oxidizing conditions and can be converted to monomers by reduced thioredoxin A, suggesting a direct thiol modulation of their activity independent of their cognate sensor kinases.
Cyanobacteria employ two-component sensor-response regulator systems to monitor and respond to environmental challenges. The response regulators RpaA, RpaB, Rre1 and RppA are integral to circadian clock function and abiotic stress acclimation in cyanobacteria. RpaA, RpaB and Rre1 are known to interact with ferredoxin or thioredoxin, raising the possibility of their thiol regulation. Here, we report that Synechocystis sp. PCC 6803 Rre1, RpaA and RpaB exist as higher-order oligomers under oxidising conditions and that reduced thioredoxin A converts them to monomers. We further show that these response regulators contain redox-responsive cysteine residues with an E-m7 around -300 mV. These findings suggest a direct thiol modulation of the activity of these response regulators, independent of their cognate sensor kinases.
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