514 results found
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Super Spy variants implicate flexibility in chaperone action

    Shu Quan et al.
    Lab-evolved 'super Spy' chaperones show enhanced flexibility, which allows them to bind to and stabilize proteins more effectively than natural chaperones.
    1. Biochemistry and Chemical Biology

    Adenosine diphosphate restricts the protein remodeling activity of the Hsp104 chaperone to Hsp70 assisted disaggregation

    Agnieszka Kłosowska et al.
    Hsp70 chaperone provides Hsp104 with high efficiency in disaggregation and specificity towards aggregated substrates at the, otherwise limiting, cellular concentrations of adenine nucleotides.
    1. Structural Biology and Molecular Biophysics

    Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles

    Rina Rosenzweig et al.
    Multiple chaperone binding sites on substrates suggest a mechanism by which the Hsp70 chaperone can circumvent kinetic traps in protein folding.
    1. Biochemistry and Chemical Biology
    2. Physics of Living Systems

    Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumption

    Paolo De Los Rios, Alessandro Barducci
    ATP consumption enables chaperones to exploit the different kinetic properties of their conformational states to exhibit a non-equilibrium affinity for their substrates that is orders of magnitude higher than its equilibrium value.
    1. Evolutionary Biology

    RNA chaperones buffer deleterious mutations in E. coli

    Marina Rudan et al.
    The overexpression of RNA chaperones, including several DEAD box RNA helicases, enhances the fitness of mutationally compromised E. coli strains.
    1. Cell Biology

    Proteostasis collapse, a hallmark of aging, hinders the chaperone-Start network and arrests cells in G1

    David F Moreno et al.
    Cells accumulate damaged proteins during aging and, by compromising the function of chaperones in folding newly synthesized G1 cyclins, proteostasis breakdown inhibits cell-cycle entry and drives yeast cells into senescence.
    1. Microbiology and Infectious Disease

    Mycobacterium tuberculosis SatS is a chaperone for the SecA2 protein export pathway

    Brittany K Miller et al.
    SatS of Mycobacterium tuberculosis is a new protein export chaperone with a role in exporting proteins by the specialized SecA2 pathway and a role in intracellular growth in macrophages.
    1. Structural Biology and Molecular Biophysics

    Oligomerization of a molecular chaperone modulates its activity

    Tomohide Saio et al.
    A combined NMR and kinetic study demonstrates how the dynamic transition of a molecular chaperone between different oligomerization states can modulate its activity by altering the binding kinetics and energetics of non-native proteins.
    1. Structural Biology and Molecular Biophysics

    Acidic C-terminal domains autoregulate the RNA chaperone Hfq

    Andrew Santiago-Frangos et al.
    Modeling and biophysics show that the unstructured acidic tail of the Sm protein Hfq mimics nucleic acid to auto inhibit its chaperone activity, preventing Hfq from being sequestered by inauthentic substrates and providing insight into the evolution of Hfq's chaperone function among bacterial genera.
    1. Cell Biology

    Cytosolic Hsp70 and co-chaperones constitute a novel system for tRNA import into the nucleus

    Akira Takano et al.
    A major cytoplasmic chaperone, Ssa2p, acts as a nuclear import carrier for tRNAs upon nutrient starvation in Saccharomyces cerevisiae.

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