Protein Folding, Unfolding and Degradation

Banner - Cellular Protein Folding and Unfolding: Chaperonins and AAA ATPases
Project Leader: Jörg Martin
Department:Protein Evolution - Lupas
Assistant: Karin Lehmann
Phone:+49 7071 601-340
Fax:+49 7071 601-349
Staff:Alphabetical List

Introduction

In the early life of a protein, proper folding is commonly required to arrive at a functional and active state. At the end of the road, a protein’s fate is degradation, typically preceded by dissociation of oligomeric complexes and unfolding of the polypeptide chain. Using a variety of biochemistry, biophysics and microbiology techniques, we focus on two experimental systems to better understand these intricate processes. To learn more about protein folding, we investigate and compare the molecular properties of bacterial and archaeal chaperonins. To learn more about protein degradation, we study an ancestral archaeal ubiquitination system and prokaryotic versions of the proteasome. In the long run, we aim to understand how different protein folding and degradation machineries evolved in bacteria and archaea.

Selected Publications

Fuchs, A.C.D., Maldoner, L., Wojtynek, M., Hartmann, M.D. and Martin, J. (2018). Rpn11-mediated ubiquitin processing in an ancestral ubiquitination system. Nat. Commun. 9, 2696.

Fuchs, A.C.D., Maldoner, L., Hipp, K., Hartmann, M.D. and Martin, J. (2018). Structural characterization of the bacterial proteasome homolog BPH reveals a tetradecameric double-ring complex with unique inner-cavity properties. J. Biol. Chem. 293, 920-930.

Fuchs, A.C.D, Alva, V., Maldoner, L., Albrecht, R., Hartmann, M.D. and Martin, J. (2017). The architecture of the Anbu complex reflects an evolutionary intermediate at the origin of the proteasome system. Structure 25, 834-845.

Shah, R., Large, A.T., Ursinus, A., Lin, B., Gowrinathan, P., Martin, J. and Lund, P. (2016). Replacement of GroEL in Escherichia coli by the group II chaperonin from the archaeon Methanococcus maripaludis. J. Bact. 198, 2692-2700.

Scharfenberg, F., Serek-Heuberger, J., Coles, M., Hartmann, M.D., Habeck, M., Martin, J., Lupas, A.N. and Alva, V. (2015). Structure and evolution of N-domains in AAA metalloproteases. J. Mol. Biol. 427, 910-923.

Forouzan, D., Ammelburg, M., Hobel, C., Ströh, L., Martin, J. and Lupas, A.N. (2012). The archaeal proteasome is regulated by a network of AAA ATPases. J. Biol. Chem. 287, 39254-39262.

Djuranovic, S., Hartmann, M.D., Habeck, M., Ursinus, A., Zwickl , P., Martin, J., Lupas, A.N. and Zeth, K. (2009). Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases. Mol. Cell 34, 580-590.

Open Positions

We always welcome applications from motivated students with a strong biochemistry background to carry out research projects at various levels (Bachelor, Master, PhD).

To apply or to get more information, please send a cover letter and your curriculum vitae to joerg.martin@tuebingen.mpg.de