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Showing 1–18 of 18 results
Advanced filters: Author: Jan Kosinski Clear advanced filters

  • Many biological complexes are flexible or heterogeneous. Integrative modeling using Assembline enables structure determination of these macromolecular complexes by combining data from multiple experimental sources, including electron microscopy maps.

    • Vasileios Rantos
    • Kai Karius
    • Jan Kosinski
    Protocols
    Nature Protocols
    Volume: 17, P: 152-176

  • In-cell structural studies in Saccharomyces cerevisiae reveal that the configuration of the Nup159 complex is a key determinant of the mRNA export function of the nuclear pore complex, and suggest a model in which nuclear pore complexes are degraded via the autophagy machinery.

    • Matteo Allegretti
    • Christian E. Zimmerli
    • Martin Beck
    Research
    Nature
    Volume: 586, P: 796-800

  • While the architecture of vertebrate nuclear pore complexes (NPCs) is well understood, the extent of its evolutionary conservation is still unclear. Here, the authors analyze the in situ architecture of an algal NPC, revealing distinct structural features that provide insights into NPC evolution.

    • Shyamal Mosalaganti
    • Jan Kosinski
    • Martin Beck
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-8

  • Motile cells must navigate complex environments. Here the authors use state-of-the-art imaging, coarse-grained MD simulations and experimental biophysics to show that cells sense their plasma membrane curvature to circumvent obstacles.

    • Ewa Sitarska
    • Silvia Dias Almeida
    • Alba Diz-Muñoz
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-15

  • The peptide/histidine transporter 1, PHT1 (SLC15A4), is required for TLR-IRF5 activation via the adaptor protein TASL. Here, the authors determined the structure of PHT1 in the outward-open conformation and present a model of the PHT1-TASL complex where the first 16 residues of TASL bind into the central cavity of PHT1.

    • Tânia F. Custódio
    • Maxime Killer
    • Christian Löw
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-12

  • The proteome-wide characterization of proteostasis depends on robust approaches to determine protein half-lives. Here, the authors improve the accuracy and precision of mass spectrometry-based quantification, enabling reliable protein half-life determination in several non-dividing cell types.

    • Toby Mathieson
    • Holger Franken
    • Mikhail M. Savitski
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-10

  • Transcription factor TFIIIC plays roles in Pol III transcription and in chromatin organization. CryoEM structure of the yeast TFIIIC subcomplex τA, a negative stain reconstruction of τA bound to the TFIIIB subunits Brf1 and TBP and accompanying biochemistry suggest how τA achieves positioning of TFIIIB upstream of the TSS and remodeling of the TFIIIC complex during assembly of TFIIIB.

    • Matthias K. Vorländer
    • Anna Jungblut
    • Christoph W. Müller
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-12

  • Microtubules are a ubiquitous eukaryotic cytoskeletal element typically consisting of 13 protofilaments arranged in a hollow cylinder. Using CryoEM and subvolume averaging, Ferreira and Pražák et al. show that Plasmodium does not adhere to a single microtubule structure. Instead, the cytoskeleton changes substantially to produce a unique, fit for purpose structure and organisation at each stage of its life cycle.

    • Josie L. Ferreira
    • Vojtěch Pražák
    • Kay Grünewald
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-17

  • Importins are known to facilitate nucleocytoplasmic transport and cytoplasmic chaperoning of some proteins. Here, the authors uncover that these proteins also act as co-translational chaperones for specific sets of proteins, for example ribonucleic acid binding factors.

    • Maximilian Seidel
    • Natalie Romanov
    • Martin Beck
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-15

  • RNA polymerase III (Pol III), the largest eukaryote polymerase yet characterized, transcribes structured small non-coding RNAs; here cryo-electron microscopy structures of budding yeast Pol III allow building of an atomic-level model of the complete 17-subunit complex, both unbound and while elongating RNA.

    • Niklas A. Hoffmann
    • Arjen J. Jakobi
    • Christoph W. Müller
    Research
    Nature
    Volume: 528, P: 231-236

  • The Nup82–Nup159–Nsp1 complex, which plays a key role in mRNA export, is recruited late during the process of nuclear pore complex (NPC) assembly. Here the authors combine crosslinking mass spectrometry, biochemical reconstitution and molecular modeling to gain insights into the mechanism of Nup82 recruitment to the NPC.

    • Roman Teimer
    • Jan Kosinski
    • Ed Hurt
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-11

  • The most comprehensive architectural model to date of the nuclear pore complex reveals previously unknown local interactions, and a role for nucleoporin 358 in Y-complex oligomerization.

    • Alexander von Appen
    • Jan Kosinski
    • Martin Beck
    Research
    Nature
    Volume: 526, P: 140-143

  • Ribosome recycling orchestrated by ABCE1 connects translation termination and mRNA surveillance mechanisms with re-initiation. Using a cross-linking and mass spectrometry approach, Kiosze-Becker et al. provide new information on the large conformational rearrangements that occur during ribosome recycling.

    • Kristin Kiosze-Becker
    • Alessandro Ori
    • Robert Tampé
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-9

  • Pazicky et al. describe the structures of glideosome trimeric complexes consisting of myosin A, essential light chain (ELC) and myosin light chain in T. gondii and P. falciparum. They show that ELCs enhance MyoA performance by inducing secondary structure in MyoA, stiffening its lever arm and calcium binding has no influence on ELC structure. These findings provide insight into this important virulence machinery.

    • Samuel Pazicky
    • Karthikeyan Dhamotharan
    • Christian Löw
    ResearchOpen Access
    Communications Biology
    Volume: 3, P: 1-14