Project Members

Dr. Simon Trowitzsch
Group Leader
phone +49-(0)69-798-29273

Dr. Elina Nürenberg
Postdoctoral Fellow
phone: +49-(0)-69-798-29471

Dr. Lukas Susac
Postdoctoral Fellow
phone: +49-(0)-69-798-29274

Bianca Hetzert
PhD Student
phone: +49-(0)-69-798-29471

Holger Heinemann
PhD Student
phone: +49-(0)-69-798-29470

Ribosome Recycling and mRNA Surveillance

The twin ATP-binding cassette (ABC) protein ABCE1 is one of the most conserved proteins in evolution, ubiquitously found in Archaea and Eukarya and essential for life. Ribosomes are split via an ATP dependent power stroke by ABCE1 after translation termination, in mRNA surveillance and ribosome biogenesis. In addition, ABCE1 provides the functional link between translation termination and re-initiation. However, the molecular mechanism and RNA interaction sites in these key cellular processes still remain to be discovered.

In our RNA team ABCE1 is used as a model for the study of ABC proteins in archaea and yeast organisms by a combination of biochemical, biophysical and cell biological approaches. We focus on the ATPase cycle of the splitting process and the post-splitting complex as a platform for initiation factors. The methodical portfolio includes classical biochemistry, structural studies by cryo-EM reconstruction and crystallization, single-molecule FRET, cross-link mass spectrometry and in vivo mutational studies with ribosome profile analysis.

External link to a published movie about the closing of ABCE1 and the 40S-ABCE1 post-splitting complex formation (Heuer & Gerovac 2017 NSMB).


Gerovac M, Tampé R.
Control of mRNA Translation by Versatile ATP-Driven Machines

Trends Biochem Sci. 2019 Feb;44(2):167-180. doi: 10.1016/j.tibs.2018.11.003. Epub 2018 Dec 7.

Elina Nürenberg-Goloub, Holger Heinemann, Milan Gerovac, Robert Tampé. 
Ribosome recycling is coordinated by processive events in two asymmetric ATP sites of ABCE1
Life Sci Alliance. 2018 Jun 14;1(3). pii: e201800095. doi: 10.26508/lsa.201800095.

Heuer A, Gerovac M, Schmidt C, Trowitzsch S, Preis A, Kötter P, Berninghausen O, Becker T, Beckmann R, Tampé R.
Structure of the 40S-ABCE1 post-splitting complex in ribosome recycling and translation initiation.
Nat Struct Mol Biol. 2017 May;24(5):453-460. doi: 10.1038/nsmb.3396. Epub 2017 Apr 3.

Kiosze-Becker K, Ori A, Gerovac M, Heuer A, Nürenberg-Goloub E, Jan Rashid U,
Becker T, Beckmann R, Beck M, Tampé R,
Structure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometry
Nat Commun. 2016 Nov 8;7:13248. doi: 10.1038/ncomms13248.

Nürenberg E, Tampé R.
Tying up loose ends: ribosome recycling in eukaryotes and archaea.
Trends Biochem Sci. 2013 Feb;38(2):64-74. doi: 10.1016/j.tibs.2012.11.003. Epub 2012 Dec 19. 

Barthelme D, Dinkelaker S, Albers SV, Londei P, Ermler U, Tampé R.
Ribosome recycling depends on a mechanistic link between the FeS cluster domain and a conformational switch of the twin-ATPase ABCE1.
Proc Natl Acad Sci U S A. 2011 Feb 22;108(8):3228-33. doi: 10.1073/pnas.1015953108. Epub 2011 Feb 3.

Barthelme, D., Scheele, U., Dinkelaker, S., Janoschka, A., MacMillan, F., Albers, S.-V., Driessen, A.J.M., Salamone-Stagni, M., Bill, E., Meyer-Klaucke, W., Schünemann, V., & Tampé, R.
Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette protein ABCE1.
J Biol Chem. 2007 May 11;282(19):14598-607. Epub 2007 Mar 12.