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Journal Article

In situ architecture of the algal nuclear pore complex

MPS-Authors
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Albert,  Sahradha
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Schaffer,  Miroslava
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Plitzko,  Jürgen M.
Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Baumeister,  Wolfgang
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Engel,  Benjamin D.
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Fulltext (public)

s41467-018-04739-y.pdf
(Publisher version), 2MB

Supplementary Material (public)

41467_2018_4739_MOESM1_ESM.pdf
(Supplementary material), 13MB

Citation

Mosalaganti, S., Kosinski, J., Albert, S., Schaffer, M., Strenkert, D., Salome, P. A., et al. (2018). In situ architecture of the algal nuclear pore complex. Nature Communications, 9: 2361. doi:10.1038/s41467-018-04739-y.


Cite as: http://hdl.handle.net/21.11116/0000-0002-7138-0
Abstract
Nuclear pore complexes (NPCs) span the nuclear envelope and mediate nucleocytoplasmic exchange. They are a hallmark of eukaryotes and deeply rooted in the evolutionary origin of cellular compartmentalization. NPCs have an elaborate architecture that has been well studied in vertebrates. Whether this architecture is unique or varies significantly in other eukaryotic kingdoms remains unknown, predominantly due to missing in situ structural data. Here, we report the architecture of the algal NPC from the early branching eukaryote Chlamydomonas reinhardtii and compare it to the human NPC. We find that the inner ring of the Chlamydomonas NPC has an unexpectedly large diameter, and the outer rings exhibit an asymmetric oligomeric state that has not been observed or predicted previously. Our study provides evidence that the NPC is subject to substantial structural variation between species. The divergent and conserved features of NPC architecture provide insights into the evolution of the nucleocytoplasmic transport machinery.