In:
Frontiers in Physiology, Frontiers Media SA, Vol. 12 ( 2021-9-17)
Kurzfassung:
The voltage-dependent anion-selective channel (VDAC) is a porin in the mitochondrial outer membrane (MOM). Unlike bacterial porins, several mitochondrial β-barrels comprise an odd number of β-strands, as is the case for the 19-β-stranded VDAC. Previously, a variant of a VDAC from Neurospora crassa , VDAC-ΔC, lacking the predicted 19th β-strand, was found to form gated, anion-selective channels in artificial membranes. In vivo , the two C-terminal β-strands (β18 and β19) in VDAC form a β-hairpin necessary for import from the cytoplasm into mitochondria and the β-signal required for assembly in the mitochondrial outer membrane resides in β19. The current study demonstrated that the putative 18-stranded β-barrel formed by VDAC-ΔC can be imported and assembled in the MOM in vivo and can also partially rescue the phenotype associated with the deletion of VDAC from a strain of N. crassa . Furthermore, when expressed and purified from Escherichia coli , VDAC-ΔC can be folded into a β-strand-rich form in decyl-maltoside. Size exclusion chromatography (SEC) alone or combined with multi-angle light scattering (SEC-MALS) and analytical ultracentrifugation revealed that, unlike full-length VDACs, VDAC-ΔC can self-organize into dimers and higher order oligomers in the absence of sterol.
Materialart:
Online-Ressource
ISSN:
1664-042X
DOI:
10.3389/fphys.2021.739001
DOI:
10.3389/fphys.2021.739001.s001
DOI:
10.3389/fphys.2021.739001.s002
DOI:
10.3389/fphys.2021.739001.s003
DOI:
10.3389/fphys.2021.739001.s004
DOI:
10.3389/fphys.2021.739001.s005
DOI:
10.3389/fphys.2021.739001.s006
DOI:
10.3389/fphys.2021.739001.s007
DOI:
10.3389/fphys.2021.739001.s008
Sprache:
Unbekannt
Verlag:
Frontiers Media SA
Publikationsdatum:
2021
ZDB Id:
2564217-0
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