Ruth Kunze
Heidelberg University
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Publication
Featured researches published by Ruth Kunze.
The EMBO Journal | 2002
Malik Lutzmann; Ruth Kunze; Andrea Buerer; Ueli Aebi; Ed Hurt
Now that it is likely that all yeast nucleoporins are known, one of the ultimate goals is the in vitro assembly of the entire nuclear pore complex from its ∼30 individual components. Here, we report the reconstitution of seven proteins (Nup133p, Nup145p‐C, Nup120p, Nup85p, Nup84p, Seh1p and Sec13p) into a heptameric 0.5 MDa nuclear pore subcomplex. We found that double plasmid transformation combined with bi‐cistronic mRNA translation allow the expression and assembly of distinct subcomplexes of up to five nucleoporins in a single Escherichia coli cell. During the sequential reconstitution of the Nup84p complex, smaller assembly intermediates can be isolated, which exhibit modular structures determined by electron microscopy that finally make up the whole Y‐shaped Nup84p complex. Importantly, a seventh subunit, Nup133p, was incorporated into the complex through its interaction with Nup84p, thereby elongating one arm of the Y‐shaped assembly to an ∼40 nm long stalk. Taken together, our data document that the Nup84p–Nup133p complex self‐assembles in a modular concept from distinct smaller nucleoporin construction sets.
Cell | 2011
Stefan Amlacher; Phillip Sarges; Dirk Flemming; Vera van Noort; Ruth Kunze; Damien P. Devos; Manimozhiyan Arumugam; Peer Bork; Ed Hurt
Despite decades of research, the structure and assembly of the nuclear pore complex (NPC), which is composed of ∼30 nucleoporins (Nups), remain elusive. Here, we report the genome of the thermophilic fungus Chaetomium thermophilum (ct) and identify the complete repertoire of Nups therein. The thermophilic proteins show improved properties for structural and biochemical studies compared to their mesophilic counterparts, and purified ctNups enabled the reconstitution of the inner pore ring module that spans the width of the NPC from the anchoring membrane to the central transport channel. This module is composed of two large Nups, Nup192 and Nup170, which are flexibly bridged by short linear motifs made up of linker Nups, Nic96 and Nup53. This assembly illustrates how Nup interactions can generate structural plasticity within the NPC scaffold. Our findings therefore demonstrate the utility of the genome of a thermophilic eukaryote for studying complex molecular machines.
Molecular Cell | 2008
Nils Schrader; Philipp Stelter; Dirk Flemming; Ruth Kunze; Ed Hurt; Ingrid R. Vetter
Nic96 is a conserved nucleoporin that recruits the Nsp1-Nup49-Nup57 complex, a module with Phe-Gly (FG) repeats, to the central transport channel of the nuclear pore complex (NPC). Nic96 binds the Nsp1 complex via its N domain and assembles into the NPC framework via its central and C domain. Here, we report the crystal structure of a large structural nucleoporin, Nic96 without its N domain (Nic96DeltaN). Nic96DeltaN is composed of three domains and is a straight molecule that--although almost entirely helical--exhibits strong deviations from the predicted alpha-solenoid fold. The missing N domain projects midway from the Nic96 molecule, indicating how the Nsp1 complex might be located with respect to the rod-like Nic96. Notably, Nic96DeltaN binds in vitro to FG repeats of the Nsp1 complex. These data suggest a model of how Nic96 could organize a transport module with coiled-coil domains and FG repeats in the central pore channel.
Nature Structural & Molecular Biology | 2015
Jessica Fischer; Roman Teimer; Stefan Amlacher; Ruth Kunze; Ed Hurt
Nuclear pore complexes (NPCs) mediate transport between the nucleus and cytoplasm. NPCs are composed of ∼30 nucleoporins (Nups), most of which are organized in stable subcomplexes. How these modules are interconnected within the large NPC framework has been unknown. Here we show a mechanism of how supercomplexes can form between NPC modules. The Nup192 inner-pore-ring complex serves as a seed to which the Nup82 outer-ring complex and Nsp1 channel complex are tethered. The linkage between these subcomplexes is generated by short sequences within linker Nups. The conserved Nup145N is the most versatile connector of NPC modules because it has three discrete binding sites for Nup192, Nup170 and Nup82. We assembled a large part of a Chaetomium thermophilum NPC protomer in vitro, providing a step forward toward the reconstitution of the entire NPC.
Journal of Cell Biology | 2011
Philipp Stelter; Ruth Kunze; Jessica Fischer; Ed Hurt
A new tool to probe the FG repeat network of the nuclear pore complex transport channel in vivo provides insight into the organization and functional features of the channel.
PLOS ONE | 2017
Bebiana Sá-Moura; Markus Kornprobst; Satyavati Kharde; Yasar Luqman Ahmed; Gunter Stier; Ruth Kunze; Irmgard Sinning; Ed Hurt
In eukaryotes, ribosome assembly is a highly complex process that involves more than 200 assembly factors that ensure the folding, modification and processing of the different rRNA species as well as the timely association of ribosomal proteins. One of these factors, Mpp10 associates with Imp3 and Imp4 to form a complex that is essential for the normal production of the 18S rRNA. Here we report the crystal structure of a complex between Imp4 and a short helical element of Mpp10 to a resolution of 1.88 Å. Furthermore, we extend the interaction network of Mpp10 and characterize two novel interactions. Mpp10 is able to bind the ribosome biogenesis factor Utp3/Sas10 through two conserved motifs in its N-terminal region. In addition, Mpp10 interacts with the ribosomal protein S5/uS7 using a short stretch within an acidic loop region. Thus, our findings reveal that Mpp10 provides a platform for the simultaneous interaction with multiple proteins in the 90S pre-ribosome.
Nature Cell Biology | 2007
Philipp Stelter; Ruth Kunze; Dirk Flemming; Dominic Höpfner; Meikel Diepholz; Peter Philippsen; Bettina Böttcher; Ed Hurt
Journal of Biological Chemistry | 2005
Malik Lutzmann; Ruth Kunze; Karin Stangl; Philipp Stelter; Katalin Fejes Tóth; Bettina Böttcher; Ed Hurt
Molecular Cell | 2015
Philipp Stelter; Ferdinand M. Huber; Ruth Kunze; Dirk Flemming; André Hoelz; Ed Hurt
Molecular Cell | 2012
Philipp Stelter; Ruth Kunze; Monika Radwan; Emma Thomson; Karsten Thierbach; Matthias Thoms; Ed Hurt