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Written by Dominik Paquet   
Tuesday, 12 February 2008 11:24
Eleven groups participate in this doctorate program which are concerned with various aspects of biochemical, cell biological and biomedical research. In particular these groups are:

Ludwig Maximilians-Universität München, Fakultät für Medizin

 

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Prof. Dr.med. Dr.rer.nat. Walter Neupert

Adolf-Butenandt-Institut für Physiologische Chemie der Universität München,
Butenandtstr. 5,
81377 München,
Germany
Tel.: 089-2180-77094/95,
Fax: 089-2180-77093
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  Research Interests:

Molecular characterization of mitochondrial protein translocases and morphogenesis:
There are six translocase machineries known which are responsible for the import and sorting of  precursor proteins into mitochondria. These are the TOM and the TOB complex in the outer  membrane (Group Rapaport), the Mia40-Erv1 disulfide relay system in the intermembrane space,  the TIM23 complex (Group Hell), the TIM22 complex (Group Hell) and the OXA1 complex (Group  Herrmann) in the inner membrane.   
With the help of these supramolecular complexes proteins are transported into four different  mitochondrial subcompartments: the outer membrane, the intermembrane space, the inner  membrane, and the matrix. Our lab contributed substantially towards an understanding of the  molecular composition and function of these translocase complexes. For that, baker's yeast  (Saccharomyces cerevisiae) and Neurospora crassa are mainly used as model organisms.   
In general, the individual groups of our lab deal with the molecular composition of each of these  translocase machineries, with the mechanism of membrane crossing and insertion, and with the  interaction of these complexes with each other. Furthermore, we focus on basic aspects of  morphogenesis and the structural organization of mitochondria (Group Reichert).   
With the determination of the mitochondrial proteoms of yeast, Neurospora crassa and human we  want to improve our understanding of mitochondrial function and determine its physiological  importance for human disease. 
Furthermore, we are interested in gaining a deeper understanding of molecular machines by  determining their 3D-structures (Group Groll). 
 

 

 

 

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Prof. Dr. Peter B. Becker

Adolf-Butenandt-Institut der Universität München, Abteilung für Molekularbiologie,
Schillerstr. 44,
80336 München,
Germany
Tel: 089-5996-427/428,
Fax: 089-5996-425
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  Research Interests:

Research in the Becker lab focuses on the molecular mechanisms by which modulators of  chromatin structure regulate the activity of chromosomal loci. We strive to understand the  principles that govern the targeting of regulators to specific chromatin loci, the nature of the  structural changes provoked by these factors, as well as the molecular mechanisms through which  alterations of chromatin structure affect enzymes involved in nucleic acid metabolism.  We are interested in the mechanism and regulation of ATP-dependent nucleosome remodeling by  the ISWI containing CHRomatin Accessibility Complex (CHRAC) and its functional significance in  vivo.   A second broad theme is to understand the principles that underlie the process of dosage  compensation in Drosophila, which involves enhancing the transcription of the majority of genes on  the single X male chromosome by two-fold. The acetylation of histone H4 at lysine 16 by the  acetylase MOF is causally involved in this increased transcription. MOF is targeted to the X  chromosome as part of a dosage compensation complex consisting of several ‘male-specific lethal’  proteins and non-coding roX RNA. Using a variety of biochemical, cell biological and genetic  methods we are characterising the molecular interactions that define the dosage compensation  complex and its association with X chromosomal chromatin.
 

 

 

 

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Prof. Dr. Christian Haass

Adolf-Butenandt-Institut der Universität München, Abteilung für Stoffwechselbiologe,
Schillerstr. 44,
80336 München,
Germany
Tel.: 089-5996-471/472,
Fax: 089-5996-415
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http://haass.web.med.uni-muenchen.de/
  Research Interests:

In the 'Laboratory of Alzheimer's and Parkinson's Disease Research' we study pathogenic processes, which lead to neurodegenerative dieseases.
We focus on the generation of a deadly peptide, the Amyloid ß-peptide (Aß), which accumulates during aging in our brains, and becomes deposited as insoluble aggregates called amyloid plaques. Since Aß has a central role in AD pathology, we investigated the mechanisms behind its generation. It quickly became clear that Aß is generated by proteolytic processing involving two types of proteases, ß-, and γ-secretase. Both secretases are major drug targets, since their inhibition should slow down the age related neuropathology caused by aggregating Aß.
Our work on γ-secretase focuses on its identification, function, assembly, and reconstitution. By identifying the active sites of the γ-secretase activity in presenilins, we were able to define a completely novel class of aspartyl proteases. By using C. elegans and zebrafish as a model system in combination with biochemical and cell biological technologies, we could demonstrate that presenilins not only play a role in Aß generation but are also directly involved in the Notch signaling pathway, which is important in development of higher organisms. However, Presinilins alone could not perform proteolysis and we could demonstrate that a complex composed of four different proteins is required to reconstitute γ-secretase activity in yeast . Currently we are investigating the assembly of the γ-secretase complex and the interaction sites of the individual components. Similar complexes involved in analogous signaling pathways are functionally investigated in the zebrafish model. In addition we are searching for mechanisms, which could affect the precision of the γ-secretase cleavage during aging and thus lead to enhanced aggregation and deposition of Aß.   
In parallel we are studying the function and regulation of ß-secretase. Here we are specifically interested in regulative mechanisms, which may be responsible for the increased ß-secretase activity during aging. First evidence suggests a posttranscriptional mechanism via the 5' untranslated region of the ß-secretase mRNA. The function of ß-secretase and its homologues is investigated in zebrafish.
Zebrafish is also used to generate a vertebrate model system for the investigation of age related Aß neurotoxicity. Based on such a model we currently prepare a mutagenesis screen to identify enhancers and inhibitors of Aß mediated cell death in vivo.
Our work on the molecular mechanisms of AD pathology is complemented by the investigation of similar age dependent diseases such as Parkinson's disease (PD) and Prion disorders. Transgenic mouse models for PD pathology have been generated and are currently used to identify small compounds, which are able to prevent α-synuclein mediated neuropathology. The pathological and biological function of genes associated with early onset PD is investigated in zebrafish.
The 'Laboratory of Alzheimer's and Parkinson's Disease Research' uses a wide range of biochemical and molecular biological methods as well as standard and confocal microscopy to analyze our cell culture and in vivo models of neurodegenerative diseases.
 

 

 

 

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Prof. Dr. Manfred Schliwa

Adolf-Butenandt-Institut der Universität München, Abteilung für Zellbiologie,
Schillerstr. 42,
80336 München,
Germany
Tel.: 089-5996-884/4,
Fax: 089-5996-882
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http://zellbio.web.med.uni-muenchen.de/
  Research Interests:

Our group is interested in the molecular und cellular properties of the motor protein Kinesin.  
Molecular motors are a force-generating enzymes which convert the free energy of the phosphate bond  of ATP into mechanical work. This work is used to power the transport of intracellular organelles along  microtubules. The development of in vitro motility assays for studying motors has yielded new insights  into the mechanical workings of motor proteins.   
Kinesin - driven motility can be directly monitored in cell-free assays by observing, under the  microscope, the gliding of individual fluorescently marked microtubules across glass surfaces  coated with purified kinesin. By using a TIRF microscope, we can also visualize single  fluorescently labeled kinesin motors and analyze their motility. We are able to observe single  fluorophores moving along microtubules and measure their velocity and run length.
Another focus of our research is the centrosome of Dictyostelium discoideum. PD. Dr. Ralph Gräf  developed a method to purify centrosomes free of microtubules in our lab. Additionally, we adapted  Tandem Affinity Purification for this organism to find centrosomal and microtubule associated  protein interactors.   
In summary, our scientific expertise includes: 
  • Microtubule-dependent intracellular motility 
  • Protein biochemistry of cytoskeletal proteins 
  • Kinesin motor proteins 
  • Confocal microscopy 
  • TIRF microscopy
    • In vitro motility assays   
      • Multiple-motor assays    
      • Single-motor assays based on fluorescently labeled motors  
    • In vivo motility in Neurospora crassa and Dictyostelium discoideum  
  • Steady state and pre-steady state kinetics of the kinesin-microtubule ATPase   
 

 

 

 

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Prof. Dr. Michael Schleicher

Adolf-Butenandt-Institut der Universität München, Abteilung für Zellbiologie,
Schillerstr. 42,
80366 München,
Germany
Tel.: 089-2180-75876;
Fax: 089-2180-75004
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http://zellbio.web.med.uni-muenchen.de/
  Research Interests:

The molecules that are involved in the actin cytoskeleton remodelling are the focus of our group. Dynamic actin cytoskeleton is a key member of cell migration, which is the basis of processes ranging from cell division to development. To get an insight into the actin dynamics we characterize the role of actin-binding and regulating proteins like formins and Ste20- like kinases respectively. A combination of cell biology (gene knock-out), biochemistry (in vitro actin polymerization) and microscopy (confocal, Reflection Interference Contrast Microscope –RICM and Total Internal Reflection Fluorescence –TIRF) techniques are primarily used as tools in our research. Dictyostelium discoideum is the model system we use for the study as this simple haploid organism allows us to investigate cell motility at the single cell and multicellular stage with biochemical and molecular methods.
 

 

 


Ludwig Maximilians-Universität München, Fakultät für Biologie

 

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Prof. Dr. Jürgen Soll

Institut für Botanik,
Menzingerstr. 68,
80638 München
Tel.: 089-17861-244/245
Fax: 089-17861-185
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Research Interests:

Protein transport processes of chloroplasts    

Research in the group of Prof. Dr. J. Soll focuses on transport processes across the two envelope  membranes of chloroplasts.  

The first aspect concerns the posttranslational import of preproteins and characterized several  subunits of the Toc and Tic import machinery. By reconstitution into proteoliposomes the role of  single subunits of the Toc complex as well as the regulation of import receptors by GTP as driving  force across the outer membrane have been described.  

Additionally, electrophysiological methods were used to characterize the channel properties of both  the outer and inner envelope localized protein import pore. All collected data from the lab  demonstrated that the import machinery of transport is unique compared to other organelles like  mitochondria (Group Boelter and Schleiff).    

The second aspect concerns solute transport across the chloroplast outer envelope. Like the  prokaryotic ancestors chloroplasts have retained multiple ion channels, which act as a selective  molecular sieve for metabolite transport in and out of the organelle. Outer envelope solute  channels clearly regulate metabolic networks in the plant cell and fulfill essential functions in  chloroplast differentiation (Group Philippar).    

A third project of the group deals with the processes involved in the biogenesis and differentiation  of chloroplasts and their prokaryotic progenitor cyanobacteria. In particular the distribution of  protein translocons in chloroplasts and cyanobacteria as well as their contribution to the formation  of thylakoids, inner envelope and plasma membranes are studied (Group Huenken).     

Focus of the fourth project is the biochemical and molecular characterization of components involved in  thylakoid biogenesis and how this process is regulated in correlation with the metabolic needs of the  surrounding cell (Group Vothknecht).    

Methods used in the lab include (among others) the use of GFP fusions together with confocal  laser scanning microscopy to localize proteins within the chloroplast.  BN-PAGE as well as lipid  chromatography and negative-stain EM are also employed to study complex formation between  proteins.    

Model organisms used in the group are:   

  • higher plants like Arabidopsis thaliana, Nicotiana tabacum and Pisum sativum, 
  • the moss Physcomitrella patens, 
  • the green algae Chlamydomonas reinhardtii   and 
  • Cyanobacteria like Synechocystis and Anabaena 
   

Ludwig Maximilians-Universität München, Fakultät für Chemie

 

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Prof. Dr. Patrick Cramer

Institut für Biochemie und Genzentrum der Universität München,
Feodor-Lynen-Str. 25,
81377 München,
Germany
Tel.: 089-2180-76953,
Fax: 089-2180-76999 
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http://www.lmb.uni-muenchen.de/cramer/index.html
  Research Interests:

Gene expression in eukaryotes is mainly regulated at the level of mRNA transcription by RNA  polymerase II. Over the last years we could elucidate many aspects of the transcription mechanism  by determining three-dimensional structures of RNA polymerase II alone and in various functional  complexes that reflect snapshots of the transcription cycle. Our work demonstrated the feasibility of  X-ray crystallographic analysis of large and transient multiprotein complexes, and is a great  starting point for further mechanistic analysis of gene transcription. Over the next years, we want to  work towards the structures of even larger and more transient multicomponent transcription  complexes. We want to elucidate protein-protein, protein-peptide, and protein-nucleic acid  interactions that underlie gene transcription and its regulation. Our main experimental tool will  remain X-ray crystallography, supported by a variety of biochemical and molecular biology  techniques in a modern interdisciplinary research setup. Our long-term goal is a mechanistic  understanding of gene regulation by structure-function analysis of RNA polymerase II. We wish to  obtain a detailed three-dimensional movie of the mRNA transcription machinery passing through  the transcription cycle. 
 

 

 

 

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Prof. Dr. Ralf-Peter Jansen

Genzentrum und Institut für Biochemie der Universität München,
Feodor Lynen Str. 25,
81377 München,
Germany
Tel.: 089-218076903,
Fax.: 089-218076949
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  Research Interests:

Protein synthesis in the cytoplasm can be temporally and spatially controlled by mRNA localization  and translational regulation. RNA localization has been described in a variety of organisms ranging  from fungi to plants, invertebrates, and vertebrates. We would like to understand how localized  RNAs are exported from the nucleus, how they are transported through the cytoplasm, and how  they are anchored at their target position.    In order to understand these mechanisms, we are using budding yeast as a model system. In  yeast, several mRNAs are localized to the bud cortex during mitotic growth, including some that  control cell fate, cell cycle and signalling. The major factors of the machinery that targets them to  the bud have been genetically identified and characterized. They include a myosin motor protein, a  myosin-specific chaperone, several RNA-binding proteins and additional associated proteins.    To date it is unknown how all these components act in concert and how the translation of mRNAs  is repressed during trafficking. In addition, it is not understood where ribonucleoprotein complexes  that move a localized RNA assemble and how they disassemble at the target site. Using a  combination of immuno-fluorescence, FISH, life imaging and biochemical methods we want to  understand the molecular mechanism of cytoplasmic RNA trafficking and how it is linked to other  aspects of RNA metabolism like processing, translation and RNA decay.
 

 

 


Max-Planck-Institut für Biochemie/Martinsried

 

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Prof. Dr. Wolfgang Baumeister

MPI für Biochemie,
Abt. Mol. Strukturbiologie
Am Klopferspitz,
82152 Martinsried,
Germany
Tel.: 089-8578-2652/2642 (Sekr.),
Fax: 089-8578-2641
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http://www.biochem.mpg.de/baumeister/
  Research Interests:

With the advent of computer-controlled electron microscopes and the automation of data  acquisition it became possible to obtain molecular-resolution (2-4 nm) tomograms of structures as  large as organelles or whole cells. Non-invasive three-dimensional (3-D) imaging of vitrified cells is  where cryoelectron tomography promises to make unique contributions by closing the gap between  the cellular and the molecular world. The emerging picture of the cell is one of a giant and highly  dynamic supramolecular assembly – hitherto a largely uncharted territory. Tomograms of cells at  molecular resolution are essentially 3-D images of the cell’s entire proteome and they reveal the  spatial relationships of macromolecules in the cytoplasm, the ‘interactome’. In order to exploit the  imposing amount of information contained in a cellular tomogram sophisticated pattern recognition  techniques must be used capable of detecting and identifying molecules in tomograms with a low  signal-to-noise ratio through their structural signature. The ultimate goal is to obtain through a  combined proteomics – electron tomography approach a comprehensive 3-D molecular atlas of  cells and organelles and to reveal the principles of supramolecular organization which provides the  basis for higher cellular functions. 
 

 

 

 

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Prof. Dr. Franz-Ulrich Hartl

Am Klopferspitz 18a,
82152 Martinsried,
Germany
Tel.: 089-8578 2233
Fax: 089-8578 2211
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http://www.biochem.mpg.de/hartl/
  Research Interests:

The Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, is investigating the mechanisms of protein folding in the cell. Protein folding is required for the realization of genetic information at the level of functional proteins and as such is one of the most fundamental reactions in all of biology. The long-term goal is to reach a complete understanding, at the structural and functional level, of how the machinery of molecular chaperones assists in co- and posttranslational protein folding. Of special interest are the folding pathways in the cytosol of prokaryotes and eukaryotes. Using a range of methods from biophysical to cell biology, the Department ultimately seeks to decipher the rules by which the thousands of different proteins in the cytosol utilize the chaperone machinery for de novo folding and assembly. A second focus of research concerns the molecular mechanisms underlying neurodegenerative disorders, such as prion diseases and polyglutamine diseases, which are caused by aberrant protein folding and are associated with the formation of protein aggregates. Here the wish is to understand how protein misfolding causes cytotoxicity and how molecular chaperones act as protective modulators. It is planned to harness the power of the chaperone machinery for applications in biotechnological protein production and in combating disease.
 

 

 


Technische Universität München, Fakultät für Chemie

 

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Prof. Dr. Johannes Buchner

Institut für Organische Chemie und Biochemie, Lehrstuhl für Biotechnologie der TU München
Lichtenbergstr. 4,
85747 Garching,
Germany
Tel.: 089-289-133-41
Sekr.: 089-289-133-40
Fax: 089-289-133-45
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http://www.chemie.tu-muenchen.de/biotech
  Research Interests:

Proteins adopt their three-dimensional structure in a spontaneous reaction, determined by the noncovalent interactions of amino acid side chains. In the case of cysteine residues, covalent linkages  may contribute to the stability of the three dimensional structure.  In vivo, a set of helper proteins, called molecular chaperones, exists which assists protein folding.  Many members of this functionally related group belong to the so-called heat shock proteins. In  addition, folding catalysts for slow reactions, such as disulfide bond formation, exist. One of the key  functions of these folding helper proteins is to prevent unproductive side reactions such as the  unspecific interaction of (un)folding polypeptide chains which lead to the formation of aggregates,  e.g. inclusion bodies upon overexpression of recombinant proteins in biotechnological processes.  Our research interests can be divided in two major areas: 1. Understanding the principles and  limitations of the folding of multidomain proteins. One of the model proteins studied are antibodies.  The structure formation process of these proteins includes folding, formation of disulfide bonds,  prolyl isomerization, and domain association. 2. Analysis of the molecular mechanisms of  chaperone proteins. We study the major classes of molecular chaperones with a focuson the  Hsp90 family and small heat shock proteins. This involves the analysis of the structure function  relationship and the dynamics of conformational changes upon ATP hydrolysis. 
 

 

 

 

 


Last Updated on Monday, 25 August 2008 22:07