scholarly journals Mitochondrial ATP synthase β-subunit production rate and ATP synthase specific activity are reduced in skeletal muscle of humans with obesity

2018 ◽  
Vol 104 (1) ◽  
pp. 126-135 ◽  
Author(s):  
Lee Tran ◽  
Paul R. Langlais ◽  
Nyssa Hoffman ◽  
Lori Roust ◽  
Christos S. Katsanos
Keyword(s):  
Skeletal Muscle ◽  
Production Rate ◽  
Atp Synthase ◽  
Specific Activity ◽  
Β Subunit ◽  
Mitochondrial Atp Synthase

scholarly journals Expression of Bovine F1-ATPase with Functional Complementation in Yeast Saccharomyces cerevisiae

2005 ◽  
Vol 280 (23) ◽  
pp. 22418-22424 ◽  
Author(s):  
Neeti Puri ◽  
Jie Lai-Zhang ◽  
Scott Meier ◽  
David M. Mueller
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Molecular Mass ◽  
Atp Synthase ◽  
Specific Activity ◽  
Functional Complementation ◽  
Yeast Saccharomyces Cerevisiae ◽  
F1 Atpase ◽  
Mitochondrial Atp Synthase ◽  
Genes Encoding ◽  
Molecular Machinery

The mitochondrial F1F0-ATP synthase is a multimeric enzyme complex composed of at least 16 unique peptides with an overall molecular mass of ∼600 kDa. F1-ATPase is composed of α3β3γδϵ with an overall molecular mass of 370 kDa. The genes encoding bovine F1-ATPase have been expressed in a quintuple yeast Saccharomyces cerevisiae deletion mutant (ΔαΔβΔγΔδΔϵ). This strain expressing bovine F1 is unable to grow on medium containing a non-fermentable carbon source (YPG), indicating that the enzyme is non-functional. However, daughter strains were easily selected for growth on YPG medium and these were evolved for improved growth on YPG medium. The evolution of the strains was presumably due to mutations, but mutations in the genes encoding the subunits of the bovine F1-ATPase were not required for the ability of the cell to grow on YPG medium. The bovine enzyme expressed in yeast was partially purified to a specific activity of about half of that of the enzyme purified from bovine heart mitochondria. These results indicate that the molecular machinery required for the assembly of the mitochondrial ATP synthase is conserved from bovine and yeast and suggest that yeast may be useful for the expression, mutagenesis, and analysis of the mammalian F1- or F1F0-ATP synthase.

scholarly journals Increased Levels of Mitochondrial ATP Synthase β-Subunit in Fast Skeletal Muscle of Carp Acclimated to Cold Temperature

1999 ◽  
Vol 65 (4) ◽  
pp. 629-636 ◽  
Author(s):  
Kiyoshi Kikuchi ◽  
Shiro Itoi ◽  
Shugo Watabe
Keyword(s):  
Skeletal Muscle ◽  
Atp Synthase ◽  
Cold Temperature ◽  
Beta Subunit ◽  
Fast Skeletal Muscle ◽  
Mitochondrial Atp Synthase

scholarly journals Proteome Analysis Reveals Phosphorylation of ATP Synthase β-Subunit in Human Skeletal Muscle and Proteins with Potential Roles in Type 2 Diabetes

2003 ◽  
Vol 278 (12) ◽  
pp. 10436-10442 ◽  
Author(s):  
Kurt Højlund ◽  
Krzysztof Wrzesinski ◽  
Peter Mose Larsen ◽  
Stephen J. Fey ◽  
Peter Roepstorff ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Skeletal Muscle ◽  
Atp Synthase ◽  
Human Skeletal Muscle ◽  
Proteome Analysis ◽  
Β Subunit

Mitochondrial ATP synthase F1 -β-subunit is a calcium-binding protein

FEBS Letters ◽  
1996 ◽  
Vol 391 (3) ◽  
pp. 323-329 ◽  
Author(s):  
Michael J. Hubbard ◽  
Nicola J. McHugh
Keyword(s):  
Atp Synthase ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Β Subunit ◽  
Mitochondrial Atp Synthase

scholarly journals Mitochondrial ATP synthase is dispensable in blood-stage Plasmodium berghei rodent malaria but essential in the mosquito phase

2015 ◽  
Vol 112 (33) ◽  
pp. 10216-10223 ◽  
Author(s):  
Angelika Sturm ◽  
Vanessa Mollard ◽  
Anton Cozijnsen ◽  
Christopher D. Goodman ◽  
Geoffrey I. McFadden
Keyword(s):  
Atp Synthase ◽  
Plasmodium Berghei ◽  
Blood Stage ◽  
Mosquito Vector ◽  
Β Subunit ◽  
Subunit Gene ◽  
Parasite Life Cycle ◽  
Asexual Blood Stage ◽  
Rodent Malaria ◽  
Mitochondrial Atp Synthase

Mitochondrial ATP synthase is driven by chemiosmotic oxidation of pyruvate derived from glycolysis. Blood-stage malaria parasites eschew chemiosmosis, instead relying almost solely on glycolysis for their ATP generation, which begs the question of whether mitochondrial ATP synthase is necessary during the blood stage of the parasite life cycle. We knocked out the mitochondrial ATP synthase β subunit gene in the rodent malaria parasite, Plasmodium berghei, ablating the protein that converts ADP to ATP. Disruption of the β subunit gene of the ATP synthase only marginally reduced asexual blood-stage parasite growth but completely blocked mouse-to-mouse transmission via Anopheles stephensi mosquitoes. Parasites lacking the β subunit gene of the ATP synthase generated viable gametes that fuse and form ookinetes but cannot progress beyond this stage. Ookinetes lacking the β subunit gene of the ATP synthase had normal motility but were not viable in the mosquito midgut and never made oocysts or sporozoites, thereby abrogating transmission to naive mice via mosquito bite. We crossed the self-infertile ATP synthase β subunit knockout parasites with a male-deficient, self-infertile strain of P. berghei, which restored fertility and production of oocysts and sporozoites, which demonstrates that mitochondrial ATP synthase is essential for ongoing viability through the female, mitochondrion-carrying line of sexual reproduction in P. berghei malaria. Perturbation of ATP synthase completely blocks transmission to the mosquito vector and could potentially be targeted for disease control.

scholarly journals The mitochondrial ATP synthase inhibitor protein binds near the C-terminus of the F1 β-subunit

FEBS Letters ◽  
1988 ◽  
Vol 229 (1) ◽  
pp. 224-228 ◽  
Author(s):  
Philip J. Jackson ◽  
David A. Harris
Keyword(s):  
Atp Synthase ◽  
Β Subunit ◽  
Inhibitor Protein ◽  
C Terminus ◽  
Mitochondrial Atp Synthase ◽  
Synthase Inhibitor

scholarly journals Bcl-xL regulates mitochondrial energetics by stabilizing the inner membrane potential

2011 ◽  
Vol 195 (2) ◽  
pp. 263-276 ◽  
Author(s):  
Ying-bei Chen ◽  
Miguel A. Aon ◽  
Yi-Te Hsu ◽  
Lucian Soane ◽  
Xinchen Teng ◽  
...  
Keyword(s):  
Membrane Potential ◽  
Mitochondrial Membrane Potential ◽  
Atp Synthase ◽  
Mitochondrial Membrane ◽  
Ion Flux ◽  
Β Subunit ◽  
Inner Mitochondrial Membrane ◽  
Two Photon Microscopy ◽  
Mitochondrial Atp Synthase ◽  
Large Fluctuations

Mammalian Bcl-xL protein localizes to the outer mitochondrial membrane, where it inhibits apoptosis by binding Bax and inhibiting Bax-induced outer membrane permeabilization. Contrary to expectation, we found by electron microscopy and biochemical approaches that endogenous Bcl-xL also localized to inner mitochondrial cristae. Two-photon microscopy of cultured neurons revealed large fluctuations in inner mitochondrial membrane potential when Bcl-xL was genetically deleted or pharmacologically inhibited, indicating increased total ion flux into and out of mitochondria. Computational, biochemical, and genetic evidence indicated that Bcl-xL reduces futile ion flux across the inner mitochondrial membrane to prevent a wasteful drain on cellular resources, thereby preventing an energetic crisis during stress. Given that F1FO–ATP synthase directly affects mitochondrial membrane potential and having identified the mitochondrial ATP synthase β subunit in a screen for Bcl-xL–binding partners, we tested and found that Bcl-xL failed to protect β subunit–deficient yeast. Thus, by bolstering mitochondrial energetic capacity, Bcl-xL may contribute importantly to cell survival independently of other Bcl-2 family proteins.

The β-subunit of pea stem mitochondrial ATP synthase exhibits PPiase activity

Mitochondrion ◽  
2003 ◽  
Vol 3 (2) ◽  
pp. 111-118 ◽  
Author(s):  
Marco Zancani ◽  
Valentino Casolo ◽  
Carlo Peresson ◽  
Giorgio Federici ◽  
Andrea Urbani ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Β Subunit ◽  
Ppiase Activity ◽  
Mitochondrial Atp Synthase
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