4.8 Article

AtpΘ is an inhibitor of F0F1 ATP synthase to arrest ATP hydrolysis during low-energy conditions in cyanobacteria

Journal

CURRENT BIOLOGY
Volume 32, Issue 1, Pages 136-+

Publisher

CELL PRESS
DOI: 10.1016/j.cub.2021.10.051

Keywords

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Funding

  1. German Research Foundation (DFG) [HE 2544/12-2, HA 2002/22-2, BE 3869/5-2]
  2. research training group BioInMe [322977937/GRK2344]
  3. AEI/FEDER, UE [PID2019-105526GB-I00/AEI]
  4. China Scholarship Council

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ATP synthase is an important enzyme for ATP production. A small protein called Atp Theta has been discovered to mainly inhibit ATPase activity in cyanobacteria, preventing the reverse reaction of ATP synthase under unfavorable conditions.
Biological processes in all living cells are powered by ATP, a nearly universal molecule of energy transfer. ATP synthases produce ATP utilizing proton gradients that are usually generated by either respiration or photosynthesis. However, cyanobacteria are unique in combining photosynthetic and respiratory electron transport chains in the same membrane system, the thylakoids, How cyanobacteria prevent the futile reverse operation of ATP synthase under unfavorable conditions pumping protons while hydrolyzing ATP is mostly unclear Here, we provide evidence that the small protein Atp Theta, which is widely conserved in cyanobacteria, is mainly fulfilling this task. The expression of Atp Theta becomes induced under conditions such as darkness or heat shock, which can lead to a weakening of the proton gradient. Translational fusions of Atp Theta to the green fluorescent protein revealed targeting to the thylakoid membrane. lmmunoprecipitation assays followed by mass spectrometry and far western blots identified subunits of ATP synthase as interacting partners of Atp Theta. ATP hydrolysis assays with isolated membrane fractions, as well as purified ATP synthase complexes, demonstrated that Atp Theta inhibits ATPase activity in a dose-dependent manner similar to the F0F1-ATP synthase inhibitor N,N-dicyclohexylcarbodimide. The results show that, even in a well-investigated process, crucial new players can be discovered if small proteins are taken into consideration and indicate that ATP synthase activity can be controlled in surprisingly different ways.

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