scholarly journals A Na + A 1 A O ATP synthase with a V‐type c subunit in a mesophilic bacterium

FEBS Journal ◽  
2020 ◽  
Vol 287 (14) ◽  
pp. 3012-3023
Author(s):  
Dennis Litty ◽  
Volker Müller
Keyword(s):  
Atp Synthase ◽  
C Subunit ◽  
Mesophilic Bacterium ◽  
Type C

scholarly journals Crystallographic structure of the turbine C-ring from spinach chloroplast F-ATP synthase

2014 ◽  
Vol 34 (2) ◽  
Author(s):  
Asha Manikkoth Balakrishna ◽  
Holger Seelert ◽  
Sven-Hendric Marx ◽  
Norbert A. Dencher ◽  
Gerhard Grüber
Keyword(s):  
Atp Synthase ◽  
Ring Width ◽  
Atp Synthesis ◽  
Crystallographic Structure ◽  
Unit Cell Parameters ◽  
Subunit C ◽  
Cell Parameters ◽  
Ring Diameter ◽  
C Subunit

In eukaryotic and prokaryotic cells, F-ATP synthases provide energy through the synthesis of ATP. The chloroplast F-ATP synthase (CF1FO-ATP synthase) of plants is integrated into the thylakoid membrane via its FO-domain subunits a, b, b’ and c. Subunit c with a stoichiometry of 14 and subunit a form the gate for H+-pumping, enabling the coupling of electrochemical energy with ATP synthesis in the F1 sector. Here we report the crystallization and structure determination of the c14-ring of subunit c of the CF1FO-ATP synthase from spinach chloroplasts. The crystals belonged to space group C2, with unit-cell parameters a=144.420, b=99.295, c=123.51 Å, and β=104.34° and diffracted to 4.5 Å resolution. Each c-ring contains 14 monomers in the asymmetric unit. The length of the c-ring is 60.32 Å, with an outer ring diameter 52.30 Å and an inner ring width of 40 Å.

scholarly journals Cellular Mechanisms of Metabolic Remodeling During Fluid Sheer Stress-Induced Metastasis

2020 ◽  
Vol 4 (Supplement_2) ◽  
pp. 322-322
Author(s):  
Tracie Dunn ◽  
Spenser Brown ◽  
Nelli Mnatsakanyan ◽  
Elizabeth Jonas ◽  
Kim Yonghyun ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Energy Metabolism ◽  
Cancer Cells ◽  
Atp Synthase ◽  
Breast Cancer Cells ◽  
Transport Systems ◽  
Cellular Mechanisms ◽  
Sheer Stress ◽  
Metabolic Remodeling ◽  
C Subunit

Abstract Objectives Fluid sheer stress (FSS) is a physical stimuli of circulating tumor cells responsible for development of and progression to cancer. FSS is reported to enhance chemoresistance and proliferation in breast cancer cells. However, cellular mechanisms explaining how FSS contributes to the metastatic phenotype of breast cancer cell are less known. Chemoresistance is highly dependent upon active transport systems, and cell division and growth require ATP. In this study, we hypothesize that FSS contributes to mitochondrial remodeling and leads to alterations in energy metabolism which favor metastasis. Methods MDA-MB-231 human breast cancer cells were exposed to fluid sheer stress (FSS). MDA-MB-231 cells were then grown in culture media for 24 h, and intracellular energy (ATP) and abundance of ATP synthase were analyzed. Results FSS significantly increases intracellular ATP in MDA-MB-231 breast cancer cells. Interestingly, MDA-MB-231 cells retained increased ATP after treatment with the uncoupler FCCP indicating remodeling and decreased reliance on mitochondrial energy metabolism. We then quantified the abundance of ATP synthase, the key enzyme complex that produces mitochondrial ATP. FSS significantly decreased protein levels of the c-subunit of ATP synthase. Conclusions Our data show that FSS causes metabolic remodeling of mitochondria-dependent ATP production. We suggest that the c-subunit of ATP synthase is an important target of FSS-mediated metastasis. Strategies to enhance the abundance or activity of the c-subunit may prevent metabolic remodeling-associated with metastasis in FSS-exposed circulating cancer cells. Funding Sources Alabama Life Research Institute (ALRI) 14,565.

3P100 The Active-Site Structure of Thermophilic F_oF_1-ATP Synthase c-Subunit Rings in Membranes(03. Membrane proteins,Poster)

2013 ◽  
Vol 53 (supplement1-2) ◽  
pp. S228
Author(s):  
Su-Jin Kang ◽  
Yasuto Todokoro ◽  
Ikuko Yumen ◽  
Bo Shen ◽  
Iku Iwasaki ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Atp Synthase ◽  
Active Site ◽  
Site Structure ◽  
C Subunit ◽  
Active Site Structure

scholarly journals Observations of rotation within the Fo F1 -ATP synthase: deciding between rotation of the Fo c subunit ring and artifact

FEBS Letters ◽  
2000 ◽  
Vol 470 (3) ◽  
pp. 244-248 ◽  
Author(s):  
Satoshi P. Tsunoda ◽  
Robert Aggeler ◽  
Hiroyuki Noji ◽  
Kazuhiko Kinosita ◽  
Masasuke Yoshida ◽  
...  
Keyword(s):  
Atp Synthase ◽  
C Subunit

scholarly journals The C-Subunit Ring of the F1FO ATP Synthase Constitutes a Leak Channel that Regulates Cellular Metabolic Efficiency by Counteracting the H+ Translocator

2012 ◽  
Vol 102 (3) ◽  
pp. 571a
Author(s):  
Kambiz N. Alavian ◽  
Emma Lazrove ◽  
Panah Nabili ◽  
Hongmei Li ◽  
Elizabeth A. Jonas
Keyword(s):  
Atp Synthase ◽  
Metabolic Efficiency ◽  
F1fo Atp Synthase ◽  
Leak Channel ◽  
C Subunit

scholarly journals Subunit rotation of ATP synthase embedded in membranes: a or   subunit rotation relative to the c subunit ring

2002 ◽  
Vol 99 (21) ◽  
pp. 13448-13452 ◽  
Author(s):  
K. Nishio ◽  
A. Iwamoto-Kihara ◽  
A. Yamamoto ◽  
Y. Wada ◽  
M. Futai
Keyword(s):  
Atp Synthase ◽  
C Subunit ◽  
Subunit Rotation
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