Characterization of Transplasma Membrane Electron Transport Chain in Wild and Drug-Resistant Leishmania donovani Promastigote and Amastigote

2019 ◽  
Vol 64 (4) ◽  
pp. 710-719
Author(s):  
Dipti Debnath ◽  
Md Akil Hossain ◽  
Munny Das ◽  
Asma Kabir ◽  
Md Ibrahim ◽  
...  
Keyword(s):  
Electron Transport ◽  
Electron Transport Chain ◽  
Leishmania Donovani ◽  
Drug Resistant ◽  
Transplasma Membrane Electron Transport ◽  
Transport Chain

scholarly journals Functional characterization of mutants deficient in N-terminal phosphorylation of the CF1 subunit beta

2021 ◽  
Author(s):  
Ralph Bock ◽  
Deserah D Strand ◽  
Daniel Karcher ◽  
Stephanie Ruf ◽  
Anne Schadach ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Electron Transport ◽  
Atp Synthase ◽  
Electron Transport Chain ◽  
Atp Hydrolysis ◽  
Molecular Motor ◽  
Functional Characterization ◽  
Phosphorylation Sites ◽  
Transport Chain

Understanding the regulation of photosynthetic light harvesting and electron transfer is of great importance to efforts to improve the ability of the electron transport chain to supply downstream metabolism. The central regulator of the electron transport chain is the ATP synthase, the molecular motor that harnesses the chemiosmotic potential generated from proton coupled electron transport to synthesize ATP. The ATP synthase is regulated both thermodynamically and post-translationally, with proposed phosphorylation sites on multiple subunits. In this study we focused on two N-terminal serines on the catalytic subunit beta, previously proposed to be important for dark inactivation of the complex to avoid ATP hydrolysis at night. Here we show that there is no clear role for phosphorylation in the dark inactivation of ATP synthase. Instead, mutation of one of the two phosphorylated serine residues to aspartate strongly decreased ATP synthase abundance. We propose that the loss of N-terminal phosphorylation of ATP beta may be involved in proper ATP synthase accumulation during complex assembly.

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