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Showing 1–17 of 17 results
Advanced filters: Author: Manajit K. Hayer-Hartl Clear advanced filters

    • Jonathan J. Ewbank
    • Thomas E. Creighton
    • F. Ulrich Hartl
    Comments & Opinion
    Nature Structural Biology
    Volume: 2, P: 10

  • Rubisco catalyses the conversion of atmospheric CO2 to organic compounds in photosynthetic organisms. Biochemical and structural analyses suggest that a selective sugar phosphatase found in plants and algae degrades a potent Rubisco inhibitor.

    • Andreas Bracher
    • Anurag Sharma
    • Manajit Hayer-Hartl
    Research
    Nature Plants
    Volume: 1, P: 1-7

  • The Hsp70 system prevents protein aggregation and increases folding yields, but it is unknown whether it also enhances the rate of folding. Here the authors combine refolding assays, FRET and hydrogen/deuterium exchange-mass spectrometry measurements to study the folding of firefly luciferase and find that the bacterial Hsp70 actively promotes the folding of this multi-domain protein.

    • Rahmi Imamoglu
    • David Balchin
    • F. Ulrich Hartl
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-13

  • Biochemical, biophysical and structural analysis reveals how the scaffolding protein CcmM recruits the enzymes Rubisco and carbonic anhydrase into a condensate for encapsulation into carboxysomes—microcompartments in cyanobacteria that serve to optimize CO2 assimilation.

    • Kun Zang
    • Huping Wang
    • Manajit Hayer-Hartl
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 28, P: 909-922

  • A high-resolution cryo-electron microscopy structure of a complete Tc holotoxin complex reveals the precise mechanism of Tc toxin assembly, gate opening and release of the cytotoxic enzyme into the translocation channel.

    • Christos Gatsogiannis
    • Felipe Merino
    • Stefan Raunser
    Research
    Nature
    Volume: 563, P: 209-213

  • Form I Rubisco, one of the most abundant proteins in nature, catalyses the fixation of atmospheric CO2 in photosynthesis. The limited catalytic efficiency of Rubisco has sparked extensive efforts to re-engineer the enzyme to enhance agricultural productivity. To bring this goal closer, the formation of cyanobacterial form I Rubisco is now analysed by in vitro reconstitution and cryo-electron microscopy.

    • Cuimin Liu
    • Anna L. Young
    • Manajit Hayer-Hartl
    Research
    Nature
    Volume: 463, P: 197-202

  • Fluorescently labelling trigger factor (TF) to monitor its real-time interaction with ribosome and polypeptide reveals that binding to the ribosome opens and activates TF. Rather than remaining bound to the ribosome, TF is carried away from it on the new polypeptide chain and remains associated with it for a time that depends on the propensity of the protein to aggregate.

    • Christian M. Kaiser
    • Hung-Chun Chang
    • José M. Barral
    Research
    Nature
    Volume: 444, P: 455-460

  • Crystal structures of human HSF1 DNA-binding domain in complex with DNA and of the coiled-coil domain from a fungal ortholog provide insight into the mode of interaction of this transcription factor with DNA.

    • Tobias Neudegger
    • Jacob Verghese
    • Andreas Bracher
    Research
    Nature Structural & Molecular Biology
    Volume: 23, P: 140-146

  • Biochemical and structural analyses show that Rubisco accumulation factor 1 (Raf1) stabilizes RbcL dimers, which then assemble into octamers. Raf1 is then displaced by RbcS, thus yielding the Rubisco holoenzyme.

    • Thomas Hauser
    • Javaid Y Bhat
    • Manajit Hayer-Hartl
    Research
    Nature Structural & Molecular Biology
    Volume: 22, P: 720-728

  • Although nonspecific chaperones such as GroEL can increase evolvability by helping slightly destabilized mutants, a dedicated assembly chaperone decreases evolvability of the CO2 fixation enzyme Rubisco, providing insights into Rubisco's poor catalytic power.

    • Paulo Durão
    • Harald Aigner
    • Manajit Hayer-Hartl
    Research
    Nature Chemical Biology
    Volume: 11, P: 148-155

  • Defects in the ribosome quality control (RQC) complex, which clears proteins that stalled during translation, can cause neurodegeneration; here it is shown that in RQC-defective cells a peptide tail added by the RQC subunit 2 to stalled polypeptides promotes their aggregation and the sequestration of chaperones in these aggregates, affecting normal protein quality control processes.

    • Young-Jun Choe
    • Sae-Hun Park
    • F. Ulrich Hartl
    Research
    Nature
    Volume: 531, P: 191-195

  • Rubisco plays a central role in photosynthetic carbon fixation. Form I Rubisco is composed of eight large (RbcL) and eight small (RbcS) subunits. The assembly of the RbcL octamer requires dedicated chaperone RbcX. Now the crystal structure of the RbcL core bound to RbcX reveals how the latter assists assembly of the octamer, and has implications for the role of RbcS.

    • Andreas Bracher
    • Amanda Starling-Windhof
    • Manajit Hayer-Hartl
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 875-880