Proteomics

Dataset Information

0

Proteomic analysis of highly purified bovine F0F1 ATP Synthase


ABSTRACT: We performed a proteomic analysis of highly purified bovine F0F1 ATP synthase to assess the quality of the purification procedure adopted to isolate the protein complex and identify possible contaminant proteins.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Bos Taurus (bovine)

TISSUE(S): Heart

SUBMITTER: Giorgio Arrigoni  

LAB HEAD: Giorgio Arrigoni

PROVIDER: PXD015108 | Pride | 2019-09-25

REPOSITORIES: Pride

altmetric image

Publications

Purified F-ATP synthase forms a Ca<sup>2+</sup>-dependent high-conductance channel matching the mitochondrial permeability transition pore.

Urbani Andrea A   Giorgio Valentina V   Carrer Andrea A   Franchin Cinzia C   Arrigoni Giorgio G   Jiko Chimari C   Abe Kazuhiro K   Maeda Shintaro S   Shinzawa-Itoh Kyoko K   Bogers Janna F M JFM   McMillan Duncan G G DGG   Gerle Christoph C   Szabò Ildikò I   Bernardi Paolo P  

Nature communications 20190925 1


The molecular identity of the mitochondrial megachannel (MMC)/permeability transition pore (PTP), a key effector of cell death, remains controversial. By combining highly purified, fully active bovine F-ATP synthase with preformed liposomes we show that Ca<sup>2+</sup> dissipates the H<sup>+</sup> gradient generated by ATP hydrolysis. After incorporation of the same preparation into planar lipid bilayers Ca<sup>2+</sup> elicits currents matching those of the MMC/PTP. Currents were fully reversib  ...[more]

Similar Datasets

| S-EPMC1221561 | biostudies-other
2020-01-13 | PXD016255 | Pride
2019-05-01 | PXD013530 | Pride
2015-11-06 | PXD000696 | Pride
| S-EPMC5827637 | biostudies-literature
2012-11-21 | E-GEOD-42417 | biostudies-arrayexpress
2024-01-29 | PXD045079 | Pride
2018-06-18 | PXD009416 | Pride
| S-EPMC7519299 | biostudies-literature
| S-EPMC2903591 | biostudies-literature