Asymmetry of the α Subunit of the Chloroplast ATP Synthase as Probed by the Binding of Lucifer Yellow Vinyl Sulfone†

Biochemistry ◽  
1998 ◽  
Vol 37 (8) ◽  
pp. 2507-2514 ◽  
Author(s):  
Kristina M. Lowe ◽  
Richard E. McCarty
Keyword(s):  
Atp Synthase ◽  
Lucifer Yellow ◽  
Vinyl Sulfone ◽  
Α Subunit ◽  
Chloroplast Atp Synthase

scholarly journals Alpha-subunit of the Chloroplast ATP Synthase of Tomato Reinforces the Resistance to Grey Mold and Broad-spectrum Resistance in Transgenic Tobacco

2020 ◽  
Author(s):  
Chao Gong ◽  
Mozhen Cheng ◽  
Jingfu Li ◽  
Hongyu Chen ◽  
Zhenzhu Zhang ◽  
...  
Keyword(s):  
Transgenic Tobacco ◽  
Atp Synthase ◽  
Broad Spectrum ◽  
Disease Incidence ◽  
Alpha Subunit ◽  
Clonostachys Rosea ◽  
Α Subunit ◽  
Chloroplast Atp Synthase ◽  
Broad Spectrum Resistance ◽  
Atpa Gene

Chloroplast ATP synthase (cpATPase) is responsible for ATP production during photosynthesis. Our previous studies showed the cpATPase CF1 alpha subunit (AtpA) is a key protein involved in Clonostachys rosea (C. rosea)-induced resistance to the fungus Botrytis cinerea (B. cinerea) in tomato. Here, we show the expression level of tomato’s cpATPase CF1 alpha subunit gene (atpA) was up-regulated by B. cinerea and C. rosea. The tomato atpA gene was then isolated, and transgenic tobacco lines were obtained. Compared with untransformed plants, the atpA-overexpressing tobacco showed an increased resistance to B. cinerea, characterized by reduced disease incidence, defense-associated hypersensitive response (HR)-like reactions, balanced reactive oxygen species, alleviated damage to chloroplast ultra-structure of leaf cell, elevated levels of ATP content and cpATPase activity, enhanced expression of carbon metabolism-, photosynthesis-, and defense-related genes. Incremental Ca2+ efflux and steady H+ efflux were observed in transgenic tobacco after their inoculation with B. cinerea. Additionally, overexpression of atpA gene conferred enhanced tolerance to salinity and resistance to the fungus Cladosporium fulvum. Thus, the α subunit of cpATPase is a key regulator that links signaling to cellular redox homeostasis, ATP biosynthesis, and gene expression of resistance traits to modulate immunity to pathogen infection, in the process providing broad-spectrum resistance in plants.

Characterization of a Phosphate Binding Domain on the α-Subunit of Chloroplast ATP Synthase Using the Photoaffinity Phosphate Analogue 4-Azido-2-nitrophenyl Phosphate†

Biochemistry ◽  
2000 ◽  
Vol 39 (45) ◽  
pp. 13781-13787 ◽  
Author(s):  
Georg Groth ◽  
Denise A. Mills ◽  
Erika Christiansen ◽  
Mark L. Richter ◽  
Bernhard Huchzermeyer
Keyword(s):  
Atp Synthase ◽  
Binding Domain ◽  
Phosphate Binding ◽  
Α Subunit ◽  
Chloroplast Atp Synthase ◽  
Nitrophenyl Phosphate

scholarly journals Two genes, atpC1 and atpC2, for the γ subunit of Arabidopsis thaliana chloroplast ATP synthase

1991 ◽  
Vol 266 (12) ◽  
pp. 7333-7338
Author(s):  
N Inohara ◽  
A Iwamoto ◽  
Y Moriyama ◽  
S Shimomura ◽  
M Maeda ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Atp Synthase ◽  
Chloroplast Atp Synthase ◽  
Γ Subunit

Import and processing of the precursor of the delta subunit of tobacco chloroplast ATP synthase

1992 ◽  
Vol 20 (3) ◽  
pp. 549-554 ◽  
Author(s):  
J. A. Napier ◽  
K. H. Larsson ◽  
F. Madue�o ◽  
J. C. Gray
Keyword(s):  
Atp Synthase ◽  
Chloroplast Atp Synthase ◽  
Tobacco Chloroplast ◽  
Delta Subunit

scholarly journals Targeting Mycobacterial F-ATP Synthase C-Terminal α Subunit Interaction Motif on Rotary Subunit γ

Antibiotics ◽  
2021 ◽  
Vol 10 (12) ◽  
pp. 1456
Author(s):  
Amaravadhi Harikishore ◽  
Chui-Fann Wong ◽  
Priya Ragunathan ◽  
Dennis Litty ◽  
Volker Müller ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Atp Hydrolysis ◽  
Atp Synthesis ◽  
Membrane Vesicles ◽  
Α Subunit ◽  
Rotational States ◽  
C Terminus ◽  
Inverted Membrane Vesicles ◽  
Hydrolysis Of ◽  
Micromolar Range

Mycobacteria regulate their energy (ATP) levels to sustain their survival even in stringent living conditions. Recent studies have shown that mycobacteria not only slow down their respiratory rate but also block ATP hydrolysis of the F-ATP synthase (α3:β3:γ:δ:ε:a:b:b’:c9) to maintain ATP homeostasis in situations not amenable for growth. The mycobacteria-specific α C-terminus (α533-545) has unraveled to be the major regulative of latent ATP hydrolysis. Its deletion stimulates ATPase activity while reducing ATP synthesis. In one of the six rotational states of F-ATP synthase, α533-545 has been visualized to dock deep into subunit γ, thereby blocking rotation of γ within the engine. The functional role(s) of this C-terminus in the other rotational states are not clarified yet and are being still pursued in structural studies. Based on the interaction pattern of the docked α533-545 region with subunit γ, we attempted to study the druggability of the α533-545 motif. In this direction, our computational work has led to the development of an eight-featured α533-545 peptide pharmacophore, followed by database screening, molecular docking, and pose selection, resulting in eleven hit molecules. ATP synthesis inhibition assays using recombinant ATP synthase as well as mycobacterial inverted membrane vesicles show that one of the hits, AlMF1, inhibited the mycobacterial F-ATP synthase in a micromolar range. The successful targeting of the α533-545-γ interaction motif demonstrates the potential to develop inhibitors targeting the α site to interrupt rotary coupling with ATP synthesis.

scholarly journals Structure of the ATP synthase from Mycobacterium smegmatis provides targets for treating tuberculosis

2021 ◽  
Vol 118 (47) ◽  
pp. e2111899118
Author(s):  
Martin G. Montgomery ◽  
Jessica Petri ◽  
Tobias E. Spikes ◽  
John E. Walker
Keyword(s):  
Atp Synthase ◽  
Mycobacterium Smegmatis ◽  
Atp Hydrolysis ◽  
Terminal Region ◽  
Catalytic Cycle ◽  
Α Subunit ◽  
Antitubercular Drugs ◽  
Safe Mechanism ◽  
Fail Safe ◽  
Α Subunits

The structure has been determined by electron cryomicroscopy of the adenosine triphosphate (ATP) synthase from Mycobacterium smegmatis. This analysis confirms features in a prior description of the structure of the enzyme, but it also describes other highly significant attributes not recognized before that are crucial for understanding the mechanism and regulation of the mycobacterial enzyme. First, we resolved not only the three main states in the catalytic cycle described before but also eight substates that portray structural and mechanistic changes occurring during a 360° catalytic cycle. Second, a mechanism of auto-inhibition of ATP hydrolysis involves not only the engagement of the C-terminal region of an α-subunit in a loop in the γ-subunit, as proposed before, but also a “fail-safe” mechanism involving the b′-subunit in the peripheral stalk that enhances engagement. A third unreported characteristic is that the fused bδ-subunit contains a duplicated domain in its N-terminal region where the two copies of the domain participate in similar modes of attachment of the two of three N-terminal regions of the α-subunits. The auto-inhibitory plus the associated “fail-safe” mechanisms and the modes of attachment of the α-subunits provide targets for development of innovative antitubercular drugs. The structure also provides support for an observation made in the bovine ATP synthase that the transmembrane proton-motive force that provides the energy to drive the rotary mechanism is delivered directly and tangentially to the rotor via a Grotthuss water chain in a polar L-shaped tunnel.

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