Ruprecht-Karls-Universität Heidelberg

Prof. Bernd Bukau

ZMBH, Im Neuenheimer Feld 282
69120 Heidelberg, Germany
Tel.: + 49-6221 54 6795
Fax.: +49-6221 54 5894

SFB 1036 managing office /
SFB 1036 - Geschäftsstelle

Veronika Helm
ZMBH, Im Neuenheimer Feld 282
69120 Heidelberg, Germany
Tel.: + 49-6221 54 8102

Welcome to the SFB 1036


As a consequence of the intrinsic biochemical fragility of molecules and limited robustness and precision of cellular processes, cells must routinely deal with faulty or damaged molecules and perturbations of cell physiology. Damage and erroneous processes may be tolerable or even result in some advantage eventually contributing to evolutionary diversification, but may otherwise have catastrophic consequences. Some types of damage can become encoded in the genome, and manifest as inherited or acquired diseases. Others may perturb cellular homeostasis and result in malfunction, degeneration and ageing of cells and organisms. Damage and errors are aggravated by a multitude of internal and environmental insults (stresses). Consequently, all cells, from bacteria to human, have developed a powerful network of systems, acting at multiple levels on macromolecules, cellular compartments, whole cells and entire organs, to minimize and reverse the damage that would ensue if mistakes and abnormal molecules went by unmonitored and uncorrected. The medical dimension of surveillance and damage response pathways becomes apparent when these pathways lose effective function, since this usually results in disease.

The long-term goal of this Collaborative Research Center (Sonderforschungsbereich, SFB) entitled "Cellular surveillance and damage control" is to elucidate the molecular mechanisms driving and coordinating damage control systems. In 17 research projects (TP) and 2 service projects (Z) the question of how the quality of gene function is monitored and how damage signals are integrated to elicit appropriate responses will be analyzed. This should provide a comprehensive understanding of how cells react to damage and establish and maintain homeostasis. Towards this goal the SFB will investigate:

Safeguarding systems that avert potential errors and damage by ensuring proper performance of cellular processes such as DNA replication, translation, and those underpinning homeostatic environments (e.g. iron homeostasis or redox state).

Damage repair systems which detect damaged or abnormal macromolecules (DNA, RNA, proteins) and provide repair and/or regulated elimination.

Stress response pathways that increase cellular capacity to cope with specific or global stress (e.g. heat shock, oxidative stress, protein overload in the endoplasmic reticulum). With the planned research on surveillance mechanisms and damage responses we are aiming at providing a comprehensive understanding of how cells react to damage and establish and maintain homeostasis.

News & Seminars

June 7, 2018
4 p.m.

Irene Chiolo (University of Southern California, Los Angeles, US)
"Highways for Repair: Nuclear Myosins and Actin Filaments Relocalize Heterochromatic DNA Breaks"
ZMBH seminar room 001 | INF 282 (pdf)
June 12, 2018
1 p.m.

Christian Kaiser (Dept. of Biology, Johns Hopkins University, Baltimore, US)
"Multi-domain protein folding: The ribosome and a chaperone keep nascent chains on track"
ZMBH seminar room 001 | INF 282 (pdf)

The SFB congratulates Frauke Melchior on 2018 FEBS | EMBO Women in Science Award!

Treble by the SFB - in the recent issue of Molecular Cell on protein quality control, there were three contributions by our Collaborative Research Center:

Article by Kityk et al. on the structure of the J-domain of a co-chaperone in complex with Hsp70, review by Mogk et al. on the mechanism of action of different protein disaggregation machines, and last but not least a preview by Avci and Lemberg on an exciting ERAD paper by the Hampton laboratory.

Überlebensstrategien: Heidelberger Lebens­wissen­schaften im Gespräch

Überlebensstrategien ist ein gemeinsames Projekt der lebens-wissenschaftlichen Sonderforschungsbereiche der Universität Heidelberg mit der Rhein-Neckar-Zeitung (RNZ). Die Redakteure der Stadtredaktion Heidelberg begleiten jeweils eine Veranstaltung mit ihren persönlichen Fragen zu den vorgestellten Forschungsthemen, den beteiligten Wissenschaftlern und den Methoden. Dieses Format der Moderation soll eine lebendige Brücke zum Publikum bilden, das in den Dialog einbezogen wird. In zwanglosem Rahmen im Karlstorbahnhof und mit musikalischer Begleitung durch Mitglieder des Collegium Musicum stellen die Sonderforschungs-bereiche ihre Fragestellungen und langfristigen Ziele vor. (click here for poster, flyer).

Photographs of Events

photos from the kick-off meeting 2013 photos from the PhD and PostDoc retreat 2013
photos from the SFB 1036 retreat at Flehingen Castle, 2014 Impressions of the SFB Congress in November 2014
group photo of the SFB members at retreat in Bad Wimpfen, October 7/8, 2015 End of year party 2015 & inauguration seminars by
Claudio Joazeiro and H. Kaessmann
Kick-off meeting 2016
The SFB members at the retreat in Leinsweiler, October 19/20, 2017

Recent publications

Ahmed, Y.L., Schleich, S., Bohlen, J., Mandel, N., Simon, B., Sinning, I., Teleman, A.A. (2018). DENR·MCTS1 heterodimerization and tRNA recruitment are required for translation reinitiation. PLoS Biology (In Press).

Acevedo, J.M., Hoermann, B., Schlimbach, T., Teleman, A.A. (2018). Changes in global translation elongation or initiation rates shape the proteome via the Kozak sequence. Sci Rep. 8:4018. doi: 10.1038/s41598-018-22330-9. (Abstract).

Moraru, A., Wiederstein, J., Pfaff, D., Fleming, T., Miller, A.K., Nawroth, P., Teleman, A.A. (2018). Elevated levels of the reactive metabolite methylglyoxal recapitulate progression of Type 2 Diabetes. Cell Metab. 27:926-934. doi: 10.1016/j.cmet.2018.02.003. (Abstract).

Grousl, T., Ungelenk, S., Miller, S., Ho, C.T., Khokhrina, M., Mayer, M.P., Bukau, B., Mogk, A. (2018). A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins. J. Cell Biol. 217:1269-1285. pii: jcb.201708116. doi: 10.1083/jcb.201708116.1. (Abstract).

Avci, D., Lemberg, M.K. (2018). Membrane Protein Dislocation by the Rhomboid Pseudoprotease Dfm1: No Pore Needed? Mol. Cell 69:161-162. doi: 10.1016/j.molcel.2017.12.031. (Abstract).

Mogk, A., Bukau, B., Kampinga, H.H. (2018). Molecular Mechanism of J-Domain-Triggered ATP Hydrolysis by Hsp70 Chaperones. Mol. Cell 214-226. doi: 10.1016/j.molcel.2018.01.004. (Abstract).

Kityk, R., Kopp, J., Mayer, M.P. (2018). Molecular Mechanism of J-Domain-Triggered ATP Hydrolysis by Hsp70 Chaperones. Mol. Cell 69:227-237.e4. doi: 10.1016/j.molcel.2017.12.003. (Abstract).

Stöcker, S., Maurer, M., Ruppert, T., Dick, T.P. (2018). A role for 2-Cys peroxiredoxins in facilitating cytosolic protein thiol oxidation. Nat. Chem. Biol. 14:148-155. doi:10.1038/nchembio.2536. (Abstract).

Heppner, D.E., Hristova, M., Ida, T., Mijuskovic, A., Dustin, C.M., Bogdandi, V., Fukuto, J.M., Dick, T.P., Nagy, P., Li, J., Akaike, T., van der Vliet, A. (2018). Cysteine perthiosulfenic acid (Cys-SSOH): A novel intermediate in thiol-based redox signaling? Redox biology 14, 379-385, doi:10.1016/j.redox.2017.10.006. (Abstract).

The SFB 1036 is funded by the