Johannes Buchner on Muck Rack

Johannes Buchner

As seen in: BIOspektrum, Nature, Wiley Online Library, ScienceDirect, Cell Press, Cell Reports, Astronomy and Astrophysics (A&A), The Journal of Biological Chemistry, ChemistryViews
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Articles

The essential co-chaperone Sgt1 regulates client dwell time in the Hsp90 chaperone cycle

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By Sonja Engler, Florent Delhommel, Christopher Dodt, Abraham López, Ofrah Faust, Annika Elimelech, Valeria Napolitano, Grzegorz M. Popowicz, Rina Rosenzweig, Michael Sattler, Johannes Buchner
| Cell Press Verified
Keywords Sgt1 Hsp90 NMR spectroscopy co-chaperones molecular chaperones protein folding glucocorticoid receptor Aha1 Introduction Cells rely on sophisticated folding machinery to deal with the constant risk of protein misfolding and aggregation.1 A key player in this machinery is the heat shock protein 90 (Hsp90), one of the most abundant molecular chaperones in the cytosol of eukaryotic cells.
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Diphthamide synthesis is linked to the eEF2‐client chaperone machinery

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By Klaus Mayer, Raffael Schaffrath, Johannes Buchner, Lars Kaduhr
| shorturl.at
Abbreviations ACP, 3-amino-3-carboxypropyl group CCT/TriC, T-complex protein Ring Complex DPH1-8, protein/enzyme necessary for diphthamide synthesis 1–8 eEF2, eukaryotic translation elongation factor 2 HSP, heat shock protein Diphthamide on eukaryotic translation elongation factor 2 (eEF2) is important for accurate protein synthesis [[1-3]]. Ribosomes that harbor eEF2 without diphthamide can generate mistranslated proteins due to higher incidences of −1 translational frameshifts [[4-6]].
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Identification of a chaperone-code responsible for Rad51-mediated genome repair

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By Andreas Maier, Johannes Buchner
| The Journal of Biological Chemistry Verified
Abstract Posttranslational modifications of Hsp90 are known to regulate its in-vivo chaperone functions. Here we demonstrate that the lysine acetylation-deacetylation dynamics of Hsp82 is a major determinant in DNA repair mediated by Rad51. We uncover that the deacetylated lysine 27 in Hsp82 dictates the formation of the Hsp82-Aha1-Rad51 complex, which is crucial for client maturation.
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