Description

Short- and medium-term objectives

The following structural objectives are meant to strengthen existing excellent groups and to complement them with new groups that add new technologies, experimental systems, and contribute related biological questions. The objectives also allow for a completion of the ongoing restructuring process of the LMU Gene Center by 2009.

  • Objective 1. Establish a high-end cryo-electron microscopic facility at the LMU (2007)

  • Objective 2. Establish an advanced bioanalytics platform (2007)

  • Objective 3. Establish a HTP crystallization and visualization facility (2007)

  • Objective 4. Recruit W2 tenure-track Professor in structural biology hybrid methods (2007)

  • Objective 5. Establish a yeast functional genomics platform (2007)

  • Objective 6. Establish course in advanced structural network biology (2008)

  • Objective 7. Recruit W3-Professor “Organismic biochemistry” (2007–2008)

  • Objective 8. Establish the Advanced biological NMR platform (2007–2008)

  • Objective 9. Take over 30% of the Swiss Light Source (SLS) beamline PX2 (2009)

  • Objective 10. Establish mail-in crystallography at the SLS beamline PX2 (2009)

  • Objective 11. Actively participate in the foundation of a joint “Munich Center for Molecular Systems Biology” (MPG, LMU, TUM)

 

Goals of innovation

  • Goal 1. To establish how the multiprotein machineries for gene transcription recognize their promoters in the genome, and how they are activated and repressed during gene regulation, using a combined structural and functional approach (Cramer and collaboration with Carell)

  • Goal 2. To unravel how DNA repair machineries work and communicate with other protein assemblies on chromatin, using a combined structural and biochemical approach (Hopfner in collaboration with Carell)

  • Goal 3. To elucidate how the ribosomal machinery for protein biosynthesis communicates with associated factors to orchestrate protein synthesis with protein folding and targeting, using cellular biochemistry and electron microscopy (Beckmann)

  • Goal 4. To use and improve NMR spectroscopic techniques to study biological recognition and its dynamics in the p53/Hsp90 network (Kessler) and in RNA-based and metabolite-induced gene regulation (coordinator: Sattler)

  • Goal 5. To unravel the structural basis for regulated RNA turnover in eukaryotes by X-ray crystallography and functional analysis (Conti)

  • Goal 6. To map molecular landscapes in the cell, in particular large protein assemblies and their interactions, and to study the time-space structure of the proteome (Baumeister)

  • Goal 7. To identify functional networks between key players in bacterial stress response by a combined microbiological, biochemical, and computational approach (Jung)

  • Goal 8. To study how gene regulatory protein networks govern differentiation and development in model organisms, using a combined experimental and bioinformatics approach (N.N W3 Organismic biochemistry)

  • Goal 9. To use functional genomics and biochemistry to study molecular networks for protein modification and regulated degradation in yeast (Jentsch)

  • Goal 10. To study by advanced mass spectroscopy the changes in protein networks and the protein distribution between cellular compartments upon external stimuli (Mann, collaboration with groups of area E working on the development of chemical tools for proteomics research)

  • Goal 11. To use biochemistry, proteomics, genetics, biophysics, and modelling to study behaviour of halophilic organisms on a quantitative systemic level (Oesterhelt)

  • Goal 12. To use a combined structural, genetic, and biochemical approach to decipher protein networks involved in coupled and RNA-regulated gene expression pathways (Niessing, Sträßer, Foerstemann)

Research groups

Principal investigators

  • Patrick Cramer, LMU Gene Center, X-ray structure of multiprotein transcription complexes

  • Karl-Peter Hopfner, LMU Gene Center, X-ray structure of DNA repair machineries

  • Roland Beckmann, LMU Gene Center, cryo-electron microscopy of protein targeting

  • Kirsten Jung, LMU BioCenter, signalling protein networks in E. coli

  • Designated successor of Horst Kessler, TUM Garching, biological NMR spectroscopy

  • Michael Sattler, TUM Garching, NMR studies of protein domain functional complexes

 

Associated members

  • Elena Conti, MPI for Biochemistry, X-ray crystallographic analysis of RNA turnover

  • Wolfgang Baumeister, MPI for Biochemistry, electron tomography of cells

  • Stefan Jentsch, MPI for Biochemistry, signalling protein networks in yeast

  • Matthias Mann, MPI for Biochemistry, mass spectrometry and proteomics

 

Junior and tenure-track groups

  • Dierk Niessing, LMU Gene Center and GSF, X-ray structure of transport protein complexes

  • Katja Sträßer, LMU Gene Center, protein networks in coupled yeast gene expression

  • Klaus Förstemann, LMU Gene Center, networks in gene regulation by RNA

 

Senior group

  • Dieter Oesterhelt, MPI for Biochemistry, protein networks and systems biology

 

Researchers in this area form an internationally unique set of scientists who are leading in X-ray crystallography (Cramer, Hopfner, Conti), cryo-electron microscopy (Beckmann, Baumeister), electron tomography (Baumeister), NMR (Kessler, Sattler), mass spectrometry and proteomics (Mann), yeast genetics and biochemistry (Jentsch), and bacterial systems biology (Jung, Oesterhelt).

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