Johannes Buchner is a German biochemist and professor at the Technische Universität München, Munich, Germany.[1]

Career

Buchner obtained his PhD at the University of Regensburg, Germany, working with Rainer Rudolph and Rainer Jaenicke. He performed his postdoctoral research in the lab of Ira Pastan at the National Cancer Institute of the National Institutes of Health in Bethesda, USA, before becoming assistant professor at the University of Regensburg and subsequently full professor and Chair of Biotechnology at the TUM.

Research

Molecular chaperones are an essential class of proteins that aid other proteins to obtain their biologically active structure and inhibit off-pathway side reactions during protein maturation.[2] Buchner’s work focuses on understanding mechanisms of molecular chaperones in a quantitative and mechanistic manner. His work has contributed to our understanding of the chaperone cycle of the bacterial chaperone GroEL[3] and now lays a particular emphasis on small heat shock proteins (sHsps), the Hsp90 chaperone machinery and the role of molecular chaperones in antibody folding. Buchner’s work established sHsps as molecular chaperones[4] and has significantly contributed to our understanding of their function and mode of activation.[5] His work on antibody folding delivered important insight in the mechanisms of how antibodies fold and are scrutinized by the cellular chaperone machinery.[6] A major focus of Johannes Buchner’s lab is the Hsp90 chaperone machine. His work has provided a detailed mechanistic understanding of Hsp90 and its regulation by co-chaperones, establishing a functional chaperone cycle for Hsp90, which has become a major target in cancer therapy[7][8] Several discoveries from the Buchner lab on chaperone-mediated protein folding have been successfully translated into novel applications in biotechnology.

Memberships and awards

Buchner is a member of the Bavarian Academy of Sciences, the German Academy of Sciences and was from 2015 to 2016 president of the German Society for Biochemistry and Molecular Biology.[9] Furthermore, he is a founding member of the Rainer Rudolph foundation. His work on protein folding and molecular chaperones has received several awards, among others the Hans Neurath Award of the Protein Society[10] (2011), the Leopoldina Schleiden Medal (2015), the Albrecht-Kossel-Award (2016) and the Max Bergmann Medal (2017).

References

  1. ↑ "Startseite – Lehrstuhl für Biotechnologie". www.department.ch.tum.de. Retrieved 27 November 2021.
  2. ↑ Buchner, Johannes (2005). Protein folding handbook (in German). Weinheim: Wiley-VCH. ISBN 978-3-527-30784-5. OCLC 214281963.
  3. ↑ Schmidt, Marion; Rutkat, Kerstin; Rachel, Reinhard; Pfeifer, Günter; Jaenicke, Rainer; Viitanen, Paul; Lorimer, George; Buchner, Johannes (29 July 1994). "Symmetric Complexes of GroE Chaperonins as Part of the Functional Cycle". Science. American Association for the Advancement of Science (AAAS). 265 (5172): 656–659. Bibcode:1994Sci...265..656S. doi:10.1126/science.7913554. ISSN 0036-8075. PMID 7913554.
  4. ↑ Jakob, U; Gaestel, M; Engel, K; Buchner, J (25 January 1993). "Small heat shock proteins are molecular chaperones". The Journal of Biological Chemistry. 268 (3): 1517–20. doi:10.1016/S0021-9258(18)53882-5. ISSN 0021-9258. PMID 8093612.
  5. ↑ Haslbeck, M. (1 December 1999). "Hsp26: a temperature-regulated chaperone". The EMBO Journal. Wiley. 18 (23): 6744–6751. doi:10.1093/emboj/18.23.6744. ISSN 1460-2075. PMC 1171736. PMID 10581247.
  6. ↑ Feige, Matthias J.; Groscurth, Sandra; Marcinowski, Moritz; Shimizu, Yuichiro; Kessler, Horst; Hendershot, Linda M.; Buchner, Johannes (2009). "An Unfolded CH1 Domain Controls the Assembly and Secretion of IgG Antibodies". Molecular Cell. Elsevier BV. 34 (5): 569–579. doi:10.1016/j.molcel.2009.04.028. ISSN 1097-2765. PMC 2908990. PMID 19524537.
  7. ↑ Bose, Suchira; Weikl, Tina; Bügl, Hans; Buchner, Johannes (6 December 1996). "Chaperone Function of Hsp90-Associated Proteins". Science. American Association for the Advancement of Science (AAAS). 274 (5293): 1715–1717. Bibcode:1996Sci...274.1715B. doi:10.1126/science.274.5293.1715. ISSN 0036-8075. PMID 8939863. S2CID 31998513.
  8. ↑ Hessling, Martin; Richter, Klaus; Buchner, Johannes (22 February 2009). "Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90". Nature Structural & Molecular Biology. Springer Science and Business Media LLC. 16 (3): 287–293. doi:10.1038/nsmb.1565. ISSN 1545-9993. PMID 19234467. S2CID 25210016.
  9. ↑ CV Leopoldina
  10. ↑ "The Protein Society: The home for the international protein science community". Archived from the original on 2016-03-05. Retrieved 2016-03-03.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.