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Showing 1–12 of 12 results
Advanced filters: Author: Jochen Reinstein Clear advanced filters

  • SNAP-tag is a widespread tool for labeling protein for bioimaging. Now, Kühn et al. report SNAP-tag2 with increased labeling kinetics and brightness, which translates into a better performance in live-cell super-resolution imaging.

    • Stefanie Kühn
    • Veselin Nasufovic
    • Kai Johnsson
    ResearchOpen Access
    Nature Chemical Biology
    P: 1-8

  • Bacteriorhodopsin (bR) is a light-driven proton pump. Here the authors combine time-resolved crystallography at a free-electron laser, ultrafast spectroscopy and quantum chemistry to study the structural changes following multiphoton photoexcitation of bR and find that they occur within 300 fs not only in the light-absorbing chromophore but also in the surrounding protein.

    • Gabriela Nass Kovacs
    • Jacques-Philippe Colletier
    • Ilme Schlichting
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-17

  • The role of co-chaperone and Hsp90 activator Aha1 is now examined in conjunction with other co-chaperones in vivo and in vitro, to reveal how they regulate the progression of the Hsp90 cycle. Aha1 and Cpr6 interact with and activate Hsp90 in a synergistic manner and displace the inhibitory co-chaperone Sti1. Aha1 is eventually released from Hsp90 by p23.

    • Jing Li
    • Klaus Richter
    • Johannes Buchner
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 326-331

  • The ER-resident Hsp70 BiP is regulated by NEF Bap. The interactions between BiP and Bap are now dissected using biochemistry, molecular modeling and smFRET approaches, revealing that Bap affects both domains of BiP, to coordinate release of substrate and nucleotide.

    • Mathias Rosam
    • Daniela Krader
    • Johannes Buchner
    Research
    Nature Structural & Molecular Biology
    Volume: 25, P: 90-100

  • The repressor–antirepressor complex AppA–PpsR is a transcriptional regulator that permits Rhodobacter to switch between photosynthesis and respiration in response to light and oxygen. A combination of crystallography, hydrogen/deuterium-exchange MS and binding assays shows how illumination reduces the affinity of the complex for DNA and provides insight into the mechanism of signal transduction by photoreceptors.

    • Andreas Winkler
    • Udo Heintz
    • Ilme Schlichting
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 859-867

  • Although structures of single-domain BLUF proteins—a photoreceptor protein domain that senses blue light—have been determined, there have been no reports of the structure of a BLUF protein containing a functional output domain; for this reason, the mechanism of light activation has remained enigmatic. The first biochemical, structural and mechanistic characterization of a full-length, active photoreceptor containing a BLUF sensor domain and a phosphodiesterase EAL output domain is now reported.

    • Thomas R. M. Barends
    • Elisabeth Hartmann
    • Ilme Schlichting
    Research
    Nature
    Volume: 459, P: 1015-1018