Researchers led by Professor Gerd Ulrich Nienhaus from the KIT have developed a new fluorescent marker protein. The photoactivatable fluorescent protein mIrisFP enables reversible photoswitching between fluorescent and nonfluorescent state as well as conversion from a green-emitting to a red-emitting form. The protein is suitable for carrying out dynamic investigations on cells and organisms and opens up new opportunities in cell biological and molecular medical research.
Prof. Dr. Andrei Lupas is a molecular biologist and director of the Department of Protein Evolution at the Max Planck Institute (MPI) for Developmental Biology in Tübingen. He became fascinated by the incredible complexity of proteins early on during his scientific career. His work focuses on the use of laboratory and computational methods to solve the question as to how a simple amino acid chain becomes a protein ‘nanomachine’. Lupas and his fellow scientists have developed model systems to study the folding of proteins and their transition into complex systems. Lupas regards the repetition of the basic building blocks as an essential principle without which the complexity of proteins would not be possible.
Proteins are the active part of cells. They recognise sequences transport nutrients and information as well as getting rid of waste. Proteins that go from one side of a membrane through to the other serve as transporters and channels and help molecules across membranes. Dr. Thomas Becker and his colleagues from the Institute for Biochemistry and Molecular Biology at the University of Freiburg are studying these complex processes. They are particularly interested in how transmembrane proteins are integrated into the mitochondrial membranes of yeast cells the protein complexes involved and whether the lipid composition of the membranes plays a role in this process.
Around thirty per cent of all cellular proteins are located in or on a biological membrane. Numerous diseases are associated with defects in these proteins. It is estimated that around 50 per cent of all drugs developed by the pharmaceutical industry in the future will target the different membranes of cells. However it is quite difficult to biochemically investigate biological membranes. These are the many reasons why many research groups and biotechnology companies are looking closely at cellular membranes.
Fifteen years ago, molecular biologist Frauke Melchior discovered a new mechanism of posttranslational protein modification that controls a variety of processes in eukaryotic cells. A small protein called SUMO is covalently bound to target proteins by specific enzymes and cleaved by other enzymes. This discovery has shaped Melchior’s scientific career.
Changes in a short protein domain can alter a whole signaling network involved in organ development – this is the key result of a comparative study of the development of the egg laying organ in two species of nematodes. However, the outward appearance of the organ remains the same in both species.
MicroRNAs are essential regulators of the genetic program in multicellular organisms. Because of their potent effects the production of these small regulators has itself to be tightly controlled. That is the key finding of a new study performed by Tübingen scientists at the Max Planck Institute for Developmental Biology. They identified a new component that modulates the production of microRNAs in thale cress by the removal of phosphate residues from a microRNA-biogenesis enzyme.
Bioinformatics methods are important tools for the classification of protein sequences. Prof. Dr. Tancred Frickey, Professor of Applied Bioinformatics at the University of Konstanz, has developed a programme that enabled him to classify the AAA ATPase protein family. CLANS software can also be used to visualise the similarities between film actors who have played roles in the same genre category.
The production of pure crystals is a method that is normally used for the determination of the spatial structure of a protein using X-ray defraction. Crystalline proteins have a very regular structure, meaning that contaminations can to a large extent be excluded. Therefore, protein crystals only contain a small number of foreign substances, which makes them a lot more stable in solution than proteins are. Due to the aforementioned properties, crystallisation opens up a broad range of applications in industrial protein purification processes. For example, the method can be used for the purification, formulation or storage stabilisation of proteins.
“In order to fully understand an organism, it is necessary to consider it as a whole,” said Dr. Uwe Schulte, biochemist and CEO of Logopharm GmbH in Freiburg. A growing number of scientists hold the same view, and there is a growing inclination to research the big picture. This is reflected in the continuously increasing number of projects looking into systems biology research.
Prof. Dr. Irmgard Sinning, biochemist and structural biologist at the University of Heidelberg, will be awarded the 2014 Leibniz Prize from the German Research Foundation (DFG) for her work on the structure and function of complexes that transport different membrane proteins to the correct cellular compartments in the appropriate target membranes. Her research is primarily focussed on the co-translational SRP pathway mediated by signal recognition particles and on the GET pathway, which ensures the post-translational insertion of membrane proteins.
RNA is a family of biological molecules with multiple roles, including the transmission of information and the catalysis of chemical reactions in a similar way to enzyme action. Ribozymes (ribonucleic acid enzymes) of this kind function for example within the ribosome where they link amino acids during protein synthesis. Professor Jörg Hartig from the University of Konstanz has developed a new ribozyme-based method that enables him to control the incorporation of specific amino acids during translation. The use of RNA switches, so-called riboswitches, have several advantages over traditional methods in controlling gene expression.
Physiologists have for a long time regarded the communication between cells as a purely “external” process. However, research carried out by Dr. Nikolaj Klöcker and his team at the Freiburg University Medical Centre now shows that the cells do not exclusively regulate their electrical properties directly at the cell membrane. They also found a range of molecular switches in neurons and epithelial cells that are able to control the cells’ electrical properties. These switches not only influence the synthesis, but also the intracellular transport and degradation of receptors and ion channels that enable the exchange of information on the cell surface.
Researchers from the Proteome Center at the University of Tübingen have identified a previously unknown type of ubiquitin a regulatory protein that functions in numerous cellular processes including inflammatory processes.
Scientists at the Institute for Biological Interfaces IBG at the KIT - Karlsruhe Institute of Technology have succeeded in identifying highly effective protein chains which have the potential of being used as part of an anti-inflammatory protection layer on implants.
Sausage casings made of collagen can be used as an alternative to natural intestine casings as they give a similar sensation when biting into knockwursts or boiled sausages. Scientists involved in the German Federal Ministry of Education and Research funded project "Biotechnological process development for novel membranes based on collagen", are seeking to optimise the process of collagen processing using environmentally friendly biotechnology methods.
Proteins that are involved in the development of an organism must be activated at the right time and then inactivated if no longer required. Scientists in Tübingen investigate the specific degradation of these proteins through specialised and highly selective systems of the cell.
Heidelberg research institute EML Research is pleased to announce that as of July 15, Dr. Frauke Gräter will be group leader of a newly established research group called “Molecular Biomechanics“. The 32 year old chemist has been junior research group leader jointly at the Bioquant, University of Heidelberg, and the MPG-CAS Partner Institute for Computational Biology (PICB), Shanghai, since 2007. Before that, she had worked at Columbia University, N.Y., and at the Max Planck Institute for Biophysical Chemistry in Göttingen. The new research group at EML Research will consist of 10 people, six of them coming from Shanghai to the Neckar.
While the role of the amyloid precursor protein (APP) in the development of amyloid plaques that are characteristic of Alzheimer’s disease is well known, the physiological role of this protein in the brain has remained elusive. However, the molecular biologist Professor Dr. Ulrike Müller from Heidelberg has now shown in mouse models that components of the APP gene family play a major role in synaptic plasticity, learning and memory.
A large number of cellular proteins are located in or on a membrane. Dr. Dirk Schneider from the University of Freiburg believes that biochemists who investigate such proteins must be a little crazy, as the methods required to isolate the molecules from their exotic environment, i.e. from the lipid bilayer, are extremely difficult and complicated. Research has long focused on water-soluble proteins. Schneider and his team have now taken on the challenge of finding out how proteins fold and assemble into complexes.
The cellular protein machinery is a marvel of nature and produces umpteen different proteins. Most of these proteins pass through a stack of membrane-enclosed discs, known as the Golgi apparatus, a miniature reaction chamber where the finishing touch is progressively added to the proteins. Rudolf Hausmann, professor and head of the Department of Bioprocess Engineering at the University of Hohenheim, is developing membranes based on the Golgi model to facilitate production of proteins outside the cells.
Cells possess a large number of chaperones which make sure that proteins behave correctly and do not cause damage. Scientists at the Centre for Molecular Biology in Heidelberg are investigating the mechanisms used by the complex network of chaperones to control the proper folding of cellular proteins.
Biotechnologically manufactured pharmaceuticals represent the most innovative type of new medications to respond to challenges in the fields of oncology immunodeficiency and metabolism. The research group led by Prof. Dr. Jürgen Hubbuch from the Karlsruhe Institute of Technology KIT is developing methods that enable the processing and crystallisation of biological molecules and turning them into biologically viable forms.
Clumped proteins can be dissolved with the aid of cellular repair systems a process of critical importance for cell survival especially under conditions of stress. Heidelberg researchers have now decrypted the fundamental mechanism for dissolving protein aggregates that involves specific molecular chaperones.
The research group led by Prof. Ralf Reski is a moss specialist and has now, for the first time, succeeded in producing a human protein in a moss bioreactor – the complement factor H. The lack of this protein leads to age-related macular degeneration in about 50 million people worldwide. The complement factor H has been assigned ‘orphan drug’ status by the respective EU authorities.