Martin-Luther-Universität Halle-Wittenberg



Zeitplan zum Treffen des Wissenschaftlichen Beirats des Landesforschungsschwerpunkts Molekulare Biowissenschaften
Zeitplan.pdf (14,3 KB)  vom 06.02.2014


Login für Redakteure

Archiv - Landesforschungsschwerpunkt Molekulare Biowissenschaften 2011 - 2014

Der Forschungsschwerpunkt Molekulare Biowissenschaften „Proteine und ihre Funktion in der Kontrolle zellulärer Prozesse“ ist ein Verbundprojekt von Instituten der Martin-Luther-Universität Halle-Wittenberg (MLU) und der benachbarten außeruniversitären Forschungsinstitute. Wir erforschen die Struktur und Dynamik von Proteinen und ihre Funktion in supramolekularen und zellulären Zusammenhängen. Über die Grundlagenforschung hinaus streben wir auch die wirtschaftliche und medizinische Anwendung von Proteinen an.

Das Projekt wird vom Ministerium für Wissenschaft und Wirtschaft des Landes Sachsen-Anhalt durch Mittel des „Europäischen Fonds für regionale Entwicklung (EFRE) INVESTITION IN IHRE ZUKUNFT“ über den Zeitraum von zweieinhalb Jahren bis Ende 2014 gefördert.

Gefördert vom Europäischen Fonds für regionale Entwicklung (EFRE)



Jens Boch accepts job offer from the University of Hannover

Dr. Jens Boch (Genetics; Institute of Biology) has accepted an offer for a W2 professor position in Plant Biotechnology at the Institute of Plant Genetics of the Leibniz University Hannover. He will start his new job October 2015. Jens Boch, who is currently working in the group of Prof. Ulla Bonas, has been supported with funds from the research focus. His PhD student Maik Reschke, who was also supported by the research focus, will join the lab in Hannover to finish his PhD.

Another five years funding for BMBF ZIK HALOmem

The Centre for Innovation Competence (ZIK) “HALOmem - membrane protein structure & dynamics”   , a life sciences project that has been in existence since 2009, has been awarded funding for a further five years   . With this funding, the ZIK HALOmem will expand its expertise platform through the establishment of two new independent research groups    “Cryo-Electron Microscopy of Membrane Protein Complexes” and “Biophysical Characterisation of Medically Relevant Membrane Proteins”, working and collaborating within the stimulating multidisciplinary environment that has established Halle as an internationally recognised centre for pure and applied protein biochemistry, biotechnology and biophysics.

HALOmem is one of two ZIKs in Halle, the other being the materials science project “Silicon and Light: from macro to nano” (in short SiLi-nano). According to the Germany Federal Ministry of Education and Research, the ZIKs have developed into a nucleus of top-flight research within a very short period. Over the next five years, the HALOmem and SiLi-nano are set to receive around ten million euros from the federal and state governments.

Recognition of the mRNA polyadenylation signal

All eukaryotic mRNAs are processed at the 3' end, whereby an overly long precursor RNA is shortened by an endonuclease, and, in almost all cases, a poly(A) tail is added to the upstream cleavage fragment, destined to become the mature mRNA. An important signal directing the processing reaction is the hexanucleotide AAUAAA, which is located some twenty nucleotides upstream of the site of cleavage and polyadenylation. This signal is recognized by the Cleavage and Polyadenylation Specificity Factor (CPSF), which is also responsible for both the endonuclease activity and the AAUAAA-dependence of the subsequent polyadenylation reaction. CPSF, which can be considered the central component of the large 3' processing complex, is thought to consist of at least seven polypeptide subunits. By means of baculoviral expression, the group of Elmar Wahle has now reconstituted a four subunit subcomplex of CPSF that, together with recombinant poly(A) polymerase, reconstitutes AAUAAA-dependent polyadenylation. In vitro experiments as well as genome-wide cross-linking and immunoprecipitation (PAR-CLIP) experiments carried out in collaboration with Walter Keller, Mihaela Zavolan and colleagues (University of Basel,  Switzerland) showed that the WDR33 subunit plays an important role in the recognition of AAUAAA, correcting earlier publications that had assigned this function to another polypeptide. The data clarify an important aspect of a reaction fundamental for all eukaryotic cells and represent an important step towards a complete reconstitution of the 3' processing reaction.

Schönemann L, Kühn U, Martin G, Schäfer P, Gruber AR, Keller W, Zavolan M, Wahle E. Reconstitution of CPSF active in polyadenylation: Recognition of the polyadenylation signal by WDR33. Genes Dev. 28, 2381-93 (2014). doi: 10.   1101/gad.   250985.   114   

Dr. Kirsten Bacia appointed Professor of Biophysical Chemistry

Dr. Kirsten Bacia    of the interdisciplinary Centre for Innovation Competence (ZIK) “HALOmem - membrane protein structure & dynamics” has been appointed to a W2 Professorship “Biophysical Chemistry” in the Institute of Chemistry, Naturwissenschaftliche Fakultät II. “We are delighted that in culminating our tenure track procedure, we have been able keep Kirsten in Halle and HALOmem while staving off a highly competitive counter offer” stressed Professor Milton T. Stubbs, Director of the ZIK HALOmem.

After receiving her doctorate in Dresden in 2005, Kirsten Bacia joined the lab of Nobel laureate Randy Schekman in Berkeley as a postdoctoral researcher. In 2009, she became a founding member of ZIK HALOmem, heading the junior research group “Biophysical Chemistry of Membranes”. Research in her lab is aimed at understanding the structure and function of the cellular machinery that sorts and packages proteins into membrane-enclosed vesicles for transport between intracellular compartments. The group uses a combination of biochemical and biophysical methods for the difficult task of reconstituting and characterizing the interplay between membrane proteins and lipid bilayers outside the living cell. State-of-the art equipment introducing a fluorescence correlation spectroscopy (FCS) setup is used to study the physico-chemical properties of protein and lipid assemblies in native biological membranes and artificial membrane mimetics.

New Group Leader in Genetics

Dr. Christian Eckmann, who previously worked at the Max-Planck-Institute of Molecular Cell Biology and Genetics in Dresden, has joined the Institute of Biology as a new research group leader. Christian Eckmann holds a Heisenberg fellowship of the DFG. He is interested in mechanisms of posttranscriptional control of cell fate decisions during germline development, using the genetic model organism Caenorhabditis elegans. His work is supported by funds from the research focus.

Green Light for the Charles Tanford Center

Today, February 12 2014, the finance committee of the parliament of the State of Sachsen-Anhalt has given the go-ahead for the construction of the Charles Tanford Center (see below). Completion of the building, which is expected towards the end of 2016, will significantly improve the infrastructure for protein research in Halle.

Meeting of the Scientific Advisory Board

The Scientific Advisory Board of the research focus will meet in Halle March 10, 2014. The research focus will present itself with several talks and with posters. The Keynote Lecture will be delivered by Dr. Frank Sobott, Antwerpen, on 'Native ion mobility-mass spectrometry: from flexible proteins to ion channels'. The complete program of the meeting can be found here.

The meeting is open to the public, but registration is required, and a modest fee will be collected to cover the costs of catering. If you want to participate, please contact

The Scientific Advisory Board has the following members: Prof. Annette Beck-Sickinger, Leipzig; Prof. Erwin Grill, Munich; Dr. Ulrike Fiedler, Halle; Prof. Utz Fischer, Würzburg Dr. Ortrun Mittelsten Scheid, Vienna; Prof. Uwe Sonnewald, Erlangen.

In vitro reconstitution and structure elucidation of a membrane protein complex

The COPII membrane protein complex is responsible for the  formation of intracellular transport vesicles at the Endoplasmic  Reticulum (ER). The group of Dr. Kirsten Bacia investigates the  structure and function of this protein complex by in vitro reconstitution in a project that started when she was a postdoc in the  laboratory of Dr. Randy Schekman at the University of California,  Berkeley. Yeast COPII proteins are purified and combined with giant  liposomes, which serve as a model for the ER membrane. In a  collaboration with Dr. Giulia Zanetti (UC Berkeley and Birkbeck  University, London) and Dr. John Briggs and co-workers (EMBL Heidelberg), the structure of the membrane-anchored COPII coat was elucidated on tubular-shaped  membranes by cryo- electron tomography, producing a detailed view of  both an inner and an outer coat layer. The structural insight  facilitates future functional studies and advances our understanding of  intracellular cargo transport.

Zanetti G, Prinz S, Daum S, Meister A, Schekman R, Bacia K, Briggs JAG, The structure of the COPII transport-vesicle coat assembled on membranes, eLife 2013;2:e00951,   

Hugo-Junkers Innovation Award 2013:
3rd prize in the Basic Research Category goes to HALOmem Junior Researchers

The Hugo Junkers Award of the State of Sachsen-Anhalt was awarded to HALOmem researchers Dr. Kirsten Bacia, Dr. Mikio Tanabe, Dr. Caroline Haupt, Stefan Werner, Peter Simeonov and Daniela Krüger for demonstrating that dual-color fluorescence cross-correlation spectroscopy (dcFCCS) constitutes an efficient method for optimizing membrane protein reconstitution.

A large number of membrane proteins, such as receptors, ion channels and transporters, are important targets for drug discovery. Reconstituting purified membrane proteins into liposomes facilitates preservation of their native conformation and functioning. The HALOmem researchers showed that dual-color fluorescence cross-correlation spectroscopy allows to monitor the reconstitution process by means of rapid measurements that require only minute amounts of material, while providing highly specific information on diffusing lipoprotein particles. Their approach hence facilitates optimization of experimental conditions for membrane protein reconstitution.

Simeonov P, Werner S, Haupt C, Tanabe M, Bacia K, Membrane Protein Reconstitution into Liposomes Guided by Dual-Color Fluorescence Cross-Correlation Spectroscopy, Biophys. Chem.,   

New faculty member at the Institute of Biochemistry and Biotechnology

Prof. Thomas Kiefhaber, Technical University of Munich, has accepted a  position as Professor of Protein Biochemistry at the Institute of  Biochemistry and Biotechnology as of April 1, 2014.

The group of  Prof. Kiefhaber is working on folding, dynamics and stability of  proteins. They focus on spectroscopic investigations of the dynamics of  different protein states in the nanosecond to millisecond range and also  study protein folding reactions that are coupled to the binding of  specific interaction partners.

The work of Prof. Kiefhaber is supported with funds from the research focus.

A new cryo electron microscope for Halle

As a result of a 2.5 million Euro BMBF strategic investment in ZIK HALOmem (   ), a high end cryo-electron microscope is to be installed on the Weinberg Campus at the end of 2013, together with a solid state direct detector. The establishment of cryo electron microscopy, which bridges the ‘resolution gap’ between the near atomic methods of crystallography and NMR on the one hand and optical microscopy on the other hand, will allow structural analysis of macromolecular complexes currently not accessible by the available high resolution techniques.

New faculty member joining the Institute of Pharmacy

Prof. Ralf Benndorf, University of Würzburg, has accepted a position as Professor of Clinical Pharmacy at the Institute of Pharmacy.

Prof. Benndorf is pursuing clinical and experimental studies concerning the influence of angiotensin II receptors and associated vascular mediators on the function of the vascular endothelium and angiogenesis. He is also interested in pharmacogenetic aspects of the interaction between antagonists of the type I angiotensin II receptor and drug transporters.

The work of Prof. Benndorf is supported with funds from the research focus.

New faculty member in the Institute of Pharmacy

Dr. Björn Junker, previously at the Institute of plant genetics and crop plant research in Gatersleben, has accepted a professor position for 'Biosynthesis and Metabolism of Pharmaceutically Active Substances' in the Institute of Pharmacy and is in the process of moving his lab to the University  of Halle.

Using methods of systems biology and bioinformatics as well as analytical approaches, Prof. Junker's group investigates plant metabolism resulting in the synthesis of pharmaceutically active substances. Data derived from mass spectrometry are fed into mathematical models of plant metabolism. The aims are a better understanding of the biosynthesis of pharmaceutical agents and the identification of possibilities to improve yields or composition of substances.

Prof. Junker's work is supported with funds from the research focus.

New professor in the Medical Faculty

Dr. Stephan M. Feller, currently research lecturer at the University  of Oxford, has accepted a professorship for 'Gastrointestinal Tumor  Biology' in the Medical Faculty of the University of Halle.

Prof.  Feller's work focuses on the topic of signal computation and signaling  defect hetereogeneity in gastrointestinal cancers. Most human cancers  are very difficult or impossible to cure, in no small part because each  cancer essentially presents a unique disease at the molecular level. The  group uses advanced chemoproteomic and cell biology methods to gain  insight into the diversity of cancer-driving kinases of  gastrointestinal cancers, since these enzymes can be effectively  targeted using existing drug discovery technology. A second focus is on  understanding how complex signals in cancer cells are computed to drive  important cell actions like proliferation, migration and invasion. This  research employs various biophysical, biochemical and cell biological  tools. The group has recently developed an entirely novel and  internationally much recognized hypothesis of how complex signal  computation is accomplished on large and structurally disordered  platform proteins, and how it may potentially be targeted by novel types  of drugs.

Prof. Feller's research will reinforce ties between  clinically oriented research and protein biochemistry in Halle. His  group is one of several from the Medical Faculty that will move into the  new protein research center that is currently being planned.

Research building 'Proteinzentrum Halle'

Following a competition between teams involving both architects and  engineers, Henn Architekten Berlin have been commissioned to plan a new  research building 'Proteinzentrum Halle'. Construction on the Weinberg  Campus will begin in 2014, and the building is expected to be finished  by the end of 2016. Funding for the building was approved late in 2010  in a competitive procedure on the basis of an application submitted by  scientists from the University of Halle. The costs will be shared  between the federal and the state government. Approximately 5 500 square  meters of office and lab space will house twelve research groups from  the Institutes of Biochemistry and Biotechnology, of Pharmacy, and of  Chemistry as well as from the Medical Faculty.

The new building  will be dedicated to the memory of Charles Tanford, one of the pioneers  of the biophysical chemistry of proteins. Tanford was born in Halle in  1921 under the name of Karl Tannenbaum. Together with his family, he  left Germany in 1929.

Foto: HENN Architekten, Alexanderstraße 7, 10178 Berlin

Foto: HENN Architekten, Alexanderstraße 7, 10178 Berlin

Foto: HENN Architekten, Alexanderstraße 7, 10178 Berlin

Zum Seitenanfang