Felix Willmund
Professor
Department of Biology
State Research Center for Optics and Material Sciences
United States of America
Biography
since October 2014: Juniorprofessor for Molecular Genetics of Eukaryotes, University of Kaiserslautern (Germany) 04/2013 - 09/2014: Group Leader at the TU Kaiserslautern (Germany) - DAAD fellow 02/2008 - 02/2013: Postdoctoral Fellow, Stanford University, CA, USA-EMBO fellow 08/2007 - 01/2008: Postdoc, University of Freiburg, Germany 04/2004 - 07/2007: PhD student in the group of Dr. Michael Schroda, University of Freiburg, Germany 1998 - 2004: Studies of Biology (Major Biochemistry) at University of Freiburg, Germany 2001: Exchange year with BSc degree at the Brock University, St. Catharines, Canada
Research Interest
My group investigates the pathways of protein folding and quality control in the chloroplast of photosynthetic active eukaryotes. During protein biogenesis chloroplast proteomes face a highly challenging task of integrating proteins encoded by the nuclear genome and proteins encoded by the small chloroplast genome. Chloroplasts, as well as other cellular compartments, posses a family of diverse proteins- termed molecular chaperones- that assist newly synthesized proteins during maturation. We apply molecular biological, biochemical and systems-biology approaches to understand the function of these chaperones. In addition we are interested in understanding the molecular consequences of abiotic stress (i.e. heat stress) for proteome homeostasis of green alga. We examine how stress-induced aggregates are formed and how cells manage to clear these aggregates.
Publications
-
Willmund F, Dorn KV, Schulz-Raffelt M, Schroda M(2008)The chloroplast DnaJ homolog CDJ1 of Chlamydomonas reinhardtii is part of a multi-chaperone complex containing HSP70B, CGE1, and HSP90C. Plant Physiology 148: 2070-2082.
-
Willmund F, del Alamo M, Pechmann S, Chen T, Albanèse V, Dammer EB (2013) The cotranslational function of ribosome-associated Hsp70 in eukaryotic protein homeostasis. Cell 152:196-209.