JournalInternational Journal of Molecular Sciences
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AbstractThe evolution of the eukaryotic cell from the primal endosymbiotic event involved a complex series of adaptations driven primarily by energy optimization. Transfer of genes from endosymbiont to host and concomitant expansion (by infolding) of the endosymbiont’s chemiosmotic membrane greatly increased output of adenosine triphosphate (ATP) and placed selective pressure on the membrane at the host–endosymbiont interface to sustain the energy advantage. It is hypothesized that critical functions at this interface (metabolite exchange, polypeptide import, barrier integrity to proteins and DNA) were managed by a precursor β-barrel protein (“pβB”) from which the voltage-dependent anion-selective channel (VDAC) descended. VDAC’s role as hub for disparate and increasingly complex processes suggests an adaptability that likely springs from a feature inherited from pβB, retained because of important advantages conferred. It is proposed that this property is the remarkable structural flexibility evidenced in VDAC’s gating mechanism, a possible origin of which is discussed. Copyright 2021 by the author. Licensee MDPI, Basel, Switzerland.
SponsorsFunding: Research by the author relevant to this paper was funded by several research grants from the National Science Foundation and by National Institutes of Health grants P41RR01219 and U01HLI16321.
Identifier to cite or link to this itemhttp://hdl.handle.net/10713/15228
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