In situ architecture of the algal nuclear pore complex

Shyamal Mosalaganti, Jan Kosinski, Sahradha Albert, Miroslava Schaffer, Daniela Strenkert, Patrice A. Salomé, Sabeeha S. Merchant, Jürgen M. Plitzko, Wolfgang Baumeister (), Benjamin D. Engel () and Martin Beck ()
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Shyamal Mosalaganti: European Molecular Biology Laboratory
Jan Kosinski: European Molecular Biology Laboratory
Sahradha Albert: Max Planck Institute of Biochemistry
Miroslava Schaffer: Max Planck Institute of Biochemistry
Daniela Strenkert: UCLA
Patrice A. Salomé: UCLA
Sabeeha S. Merchant: UCLA
Jürgen M. Plitzko: Max Planck Institute of Biochemistry
Wolfgang Baumeister: Max Planck Institute of Biochemistry
Benjamin D. Engel: Max Planck Institute of Biochemistry
Martin Beck: European Molecular Biology Laboratory

Nature Communications, 2018, vol. 9, issue 1, 1-8

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-04739-y

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