scholarly journals The INA complex facilitates assembly of the peripheral stalk of the mitochondrial F 1 F o ‐ ATP synthase

2014 ◽  
Vol 33 (15) ◽  
pp. 1624-1638 ◽  
Author(s):  
Oleksandr Lytovchenko ◽  
Nataliia Naumenko ◽  
Silke Oeljeklaus ◽  
Bernhard Schmidt ◽  
Karina Malsburg ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Peripheral Stalk

Biophysics and Bioinformatics Reveal Structural Differences of the Two Peripheral Stalk Subunits in Chloroplast ATP Synthase

2006 ◽  
Vol 141 (3) ◽  
pp. 411-420 ◽  
Author(s):  
A. Poetsch ◽  
R. J. Berzborn ◽  
J. Heberle ◽  
T. A. Link ◽  
N. A. Dencher ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Peripheral Stalk ◽  
Chloroplast Atp Synthase ◽  
Structural Differences

scholarly journals The Proton-translocatingaSubunit of F0F1-ATP Synthase Is Allocated Asymmetrically to the Peripheral Stalk

2008 ◽  
Vol 283 (48) ◽  
pp. 33602-33610 ◽  
Author(s):  
Monika G. Düser ◽  
Yumin Bi ◽  
Nawid Zarrabi ◽  
Stanley D. Dunn ◽  
Michael Börsch
Keyword(s):  
Atp Synthase ◽  
Peripheral Stalk ◽  
F0f1 Atp Synthase

scholarly journals Structure of the mitochondrial ATP synthase from Pichia angusta determined by electron cryo-microscopy

2016 ◽  
Vol 113 (45) ◽  
pp. 12709-12714 ◽  
Author(s):  
Kutti R. Vinothkumar ◽  
Martin G. Montgomery ◽  
Sidong Liu ◽  
John E. Walker
Keyword(s):  
Atp Synthase ◽  
Catalytic Domain ◽  
Lateral Force ◽  
Membrane Domain ◽  
Subunit A ◽  
Mechanical Coupling ◽  
Peripheral Stalk ◽  
Mitochondrial Atp Synthase ◽  
A Subunit ◽  
Pichia Angusta

The structure of the intact monomeric ATP synthase from the fungus, Pichia angusta, has been solved by electron cryo-microscopy. The structure provides insights into the mechanical coupling of the transmembrane proton motive force across mitochondrial membranes in the synthesis of ATP. This mechanism requires a strong and integral stator, consisting of the catalytic α3β3-domain, peripheral stalk, and, in the membrane domain, subunit a and associated supernumerary subunits, kept in contact with the rotor turning at speeds up to 350 Hz. The stator’s integrity is ensured by robust attachment of both the oligomycin sensitivity conferral protein (OSCP) to the catalytic domain and the membrane domain of subunit b to subunit a. The ATP8 subunit provides an additional brace between the peripheral stalk and subunit a. At the junction between the OSCP and the apparently stiff, elongated α-helical b-subunit and associated d- and h-subunits, an elbow or joint allows the stator to bend to accommodate lateral movements during the activity of the catalytic domain. The stator may also apply lateral force to help keep the static a-subunit and rotating c10-ring together. The interface between the c10-ring and the a-subunit contains the transmembrane pathway for protons, and their passage across the membrane generates the turning of the rotor. The pathway has two half-channels containing conserved polar residues provided by a bundle of four α-helices inclined at ∼30° to the plane of the membrane, similar to those described in other species. The structure provides more insights into the workings of this amazing machine.

scholarly journals Near-Neighbor Relationships of the Atypical Subunits that Form the Peripheral Stalk of the Mitochondrial ATP Synthase in Chlorophycean Algae

2017 ◽  
Vol 112 (3) ◽  
pp. 2a-3a
Author(s):  
Miriam Vázquez-Acevedo ◽  
Félix Vega-DeLuna ◽  
Lorenzo Sánchez-Vásquez ◽  
Lilia Colina-Tenorio ◽  
Claire Remacle ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Near Neighbor ◽  
Peripheral Stalk ◽  
Mitochondrial Atp Synthase ◽  
Neighbor Relationships

scholarly journals Manipulations in the Peripheral Stalk of the Saccharomyces cerevisiae F1F0-ATP Synthase

2011 ◽  
Vol 286 (12) ◽  
pp. 10155-10162 ◽  
Author(s):  
Amanda K. Welch ◽  
Caleb J. Bostwick ◽  
Brian D. Cain
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Atp Synthase ◽  
Atp Hydrolysis ◽  
Ectopic Expression ◽  
Minimum Length ◽  
Subunit Structure ◽  
Peripheral Stalk ◽  
Mitochondrial Fractions ◽  
Membrane Spanning

The Saccharomyces cerevisiae F1F0-ATP synthase peripheral stalk is composed of the OSCP, h, d, and b subunits. The b subunit has two membrane-spanning domains and a large hydrophilic domain that extends along one side of the enzyme to the top of F1. In contrast, the Escherichia coli peripheral stalk has two identical b subunits, and subunits with substantially altered lengths can be incorporated into a functional F1F0-ATP synthase. The differences in subunit structure between the eukaryotic and prokaryotic peripheral stalks raised a question about whether the two stalks have similar physical and functional properties. In the present work, the length of the S. cerevisiae b subunit has been manipulated to determine whether the F1F0-ATP synthase exhibited the same tolerances as in the bacterial enzyme. Plasmid shuffling was used for ectopic expression of altered b subunits in a strain carrying a chromosomal disruption of the ATP4 gene. Wild type growth phenotypes were observed for insertions of up to 11 and a deletion of four amino acids on a nonfermentable carbon source. In mitochondria-enriched fractions, abundant ATP hydrolysis activity was seen for the insertion mutants. ATPase activity was largely oligomycin-insensitive in these mitochondrial fractions. In addition, very poor complementation was seen in a mutant with an insertion of 14 amino acids. Lengthier deletions yielded a defective enzyme. The results suggest that although the eukaryotic peripheral stalk is near its minimum length, the b subunit can be extended a considerable distance.

scholarly journals S1.16 Interaction of the peripheral stalk of the bovine ATP synthase with the F1 domain

2008 ◽  
Vol 1777 ◽  
pp. S12-S13
Author(s):  
David M. Rees ◽  
Michael J. Runswick ◽  
Martin G. Montgomery ◽  
Andrew G.W. Leslie ◽  
John E. Walker
Keyword(s):  
Atp Synthase ◽  
Peripheral Stalk
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