Welcome to the Bange Lab 

The Bange Lab is located at the Philipps-University-Marburg - one of the most traditional places for natural sciences in Germany.

We are part of the interdisciplinary LOEWE Center for Synthetic Microbiology (Synmikro) and the Faculty of Chemistry.

Microorganisms provide the greatest diversity within the biosphere and conquered every possible niche ranging from hot springs to the human gut. 

Key to the evolutionary success is their fast adaptability leading to specific features attributed to novel environmental settings. 

Given their rather small genomes, microorganisms must exhibit an enormous molecular plasticity allowing the robust adaptation of their cellular constituents and regulatory networks to new environmental requirements during the course of evolution.

 

The mission of the AG Bange is to understand the molecular inventory of microbes and its adaptation through the course of evolution by combining high-resolution techniques with systems- and cell biology approaches. 

Latest Infos

 

The Deutsche Forschungsgemeinschaft (DFG) supports the foundation of the:

"Marburg core facility for Interaction, Dynamics and Assembly of biomolecular Structures". Great News!

Read more ...

 

The Deutsche Forschungsgemeinschaft (DFG) supports the foundation of Collaborative Research Center between Marburg, Giessen und Munich (TRR174). Within this great consortium, the Bange lab will unravel how bacteria regulate place and number of their flagella. Read more ...

 

Current Opinion in Chemical Biology with a focus on Synthetic Biology

Guest Editors: Gert Bange and Torsten Wladminghaus

Editorial Overview: From understanding to engineering biology and back

Curr Opin in Chem Biol. 2016, 34:151–153

Regulation of the Shine-Dalgarno binding protein CsrA by the flagellar regulator FliW.

 

CsrA proteins are repressors of translation that target the Shine–Dalgarno sequence of the ribosome-binding site. Here we present the first crystal structure of protein FliW, which allosterically regulates CsrA in a highly specific manner. Read more ...

 

PNASdoi: 10.1073/pnas.1602425113

 

 

Magic dance of bacterial second messengers: The multiple conformations of (p)ppGpp.

 

Wieland wrote a review for Molecular Microbiology discussing the structural biology of the alarmones (p)ppGpp.

Please follow this link to directly access to article: "The magic dance of the alarmones (p)ppGpp."

 

Molecular Microbiology, DOI: 10.1111/mmi.13412

 

 

On the cover!

 

Florian wrote a review dealing with open questions on the assembly of our favourite nanomachine: the flagellum.

 

Altegoer F, Bange G (2015).

Undiscovered regions on the molecular landscape of flagellar assembly.

Current Opinion in Microbiology, DOI: 10.1016/j.mib.2015.08.011

The nutritional alarmones (p)ppGpp play essential roles during the response and adaptation of bacteria to stress conditions and environmental changes. Here we provide in-depth biochemical and structural view on catalytic mechanism&regulation underlying the synthesis of (p)ppGpp.

 

​​Steinchen W, Schuhmacher J, Altegoer F, Fage C, Srinivasan V, Linne U, Marahiel M, Bange G*  (2015).

Catalytic mechanism and allosteric regulation of an oligomeric (p)ppGpp synthetase by an alarmone.

PNAS, doi: 10.1073/pnas.1505271112

How do bacteria establish specific-localization and numeric-regulation of their flagella? Flagella are molecular motors that enable bacteria to be mobile. Place and number of flagella at the bacterial surface are subject to distinct molecular mechanisms. Recent progress and open questions in our understanding can be found in:

Schuhmacher J, Thormann KM and Bange G (2015). How bacteria maintain location and number of flagella.

FEMS Reviews Microbiology, 39(6):812-22

 

Schuhmacher JS, Rossmann F, Dempwolff F, Knauer C, Altegoer F, Steinchen W,Dörrich A, Klingl A, Stephan M, Linne U, Thormann K and Bange G (2015).

The MinD-like ATPase FlhG effects location and number of bacterial flagella during C-ring assembly.

PNAS, 112 (10), 3092-7

Ribosome biogenesis requires assembly factors guiding newly synthesized ribosomal proteins (r-proteins) to nascent ribosomes. This study shows the r-proteins are captured by their chaperones as early as during their synthesis. This work also provides insights into the development of ribosome stress-related diseases such as the Blackfan-Diamond Anemia. 

 

Pausch P, Singh U, Ahmed YL, Pillet B, Murat G, Altegoer F, Stier G, Thoms M, Hurt E, Sinning, I, Bange, G*, Kressler D* (2015).

Co-translational capturing of nascent ribosomal proteins by their dedicated chaperones.

Nature Communicationsdoi: 10.1038/ncomms8494 , *corresponding authors

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