Abstract
The protocoatomer hypothesis states that MC proteins were key to the origin of the eukaryotes because they form the scaffold of the multi-protein complexes that they use to manipulate membranes. Despite their common origin, eukaryotic MCs display impressive variations in sequence, structure, architecture, interaction, and cage formation. Using a structural approach, proteins with the MC architecture have been detected in bacteria, in the PVC superphylum and in Bacteroidetes. In one bacterial species, Gemmata obscuriglobus, at least one MC-like protein is in tight interaction with the internal membranes and involved in endocytosis. This represents the first molecular link between a bacterial and the eukaryotic endomembrane systems, suggestive of a possible evolutionary relationship between both systems.
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Notes
- 1.
Nomenclature referring to the yeast proteins throughout the manuscript and the figures.
- 2.
It has been argued that eukaryotic MC helical domains are distinct from a regular α-solenoid arrangement. This only illustrates the inconsistent usage of the term (Field et al. 2011). For this reason, we prefer to use the denomination of SPAH (stacked pairs of alpha-helices) domain, which only refers to the commonality of the fold types.
- 3.
The pair is also referred to as Nup96-Nup98, e.g. in human.
Abbreviations
- PVC:
-
Planctomycetes-Verrucomicrobiae-Chlamydiae
- MC:
-
Membrane coat
- NPC:
-
Nuclear pore complex
- nup:
-
Nucleoporin protein of a nuclear pore complex
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Acknowledgements
We are grateful to Iain Mattaj and his group at EMBL, Germany.
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Devos, D.P. (2013). Structural Aspects of MC Proteins of PVC Superphylum Members. In: Fuerst, J. (eds) Planctomycetes: Cell Structure, Origins and Biology. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-502-6_3
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DOI: https://doi.org/10.1007/978-1-62703-502-6_3
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