FMP Publications

Our publications are recorded in a searchable database since 2010, updates will be added regularly.

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The mechanism of denaturation and the unfolded state of the alpha-helical membrane-associated protein Mistic
Jacso, T., Bardiaux, B., Broecker(*), J., Fiedler(*), S., Baerwinkel(*), T., Mainz, A., Fink, U., Vargas(*), C., Oschkinat, H., Keller(*), S.; Reif, B.
J Am Chem Soc, 135:18884-18891

Tags: Solid-State NMR Spectroscopy (Reif), NMR-Supported Structure Biology (Oschkinat)

Abstract: In vitro protein-folding studies using chemical denaturants such as urea are indispensible in elucidating the forces and mechanisms determining the stability, structure, and dynamics of water-soluble proteins. By contrast, alpha-helical membrane-associated proteins largely evade such approaches because they are resilient to extensive unfolding. We have used optical and NMR spectroscopy to provide an atomistic-level dissection of the effects of urea on the structure and dynamics of the alpha-helical membrane-associated protein Mistic as well as its interactions with detergent and solvent molecules. In the presence of the zwitterionic detergent lauryl dimethylamine oxide, increasing concentrations of urea result in a complex sequence of conformational changes that go beyond simple two-state unfolding. Exploiting this finding, we report the first high-resolution structural models of the urea denaturation process of an alpha-helical membrane-associated protein and its completely unfolded state, which contains almost no regular secondary structure but nevertheless retains a topology close to that of the folded state.

Mapping discontinuous protein-binding sites via structure-based peptide libraries: combining in silico and in vitro approaches
Jaeger(*), I. S., Kretzschmar(*), I., Körner, J., Weiser(*), A. A., Mahrenholz(*), C. C., Potty(*), A., Kourentzi(*), K., Willson(*), R. C., Volkmer(*), R.; Preissner(*), R.
J Mol Recognit, 26:23-31

Tags: NMR-Supported Structural Biology (Oschkinat)

Abstract: To perform their various functions, protein surfaces often have to interact with each other in a specific way. Usually, only parts of a protein are accessible and can act as binding sites. Because proteins consist of polypeptide chains that fold into complex three-dimensional shapes, binding sites can be divided into two different types: linear sites that follow the primary amino acid sequence and discontinuous binding sites, which are made up of short peptide fragments that are adjacent in spatial proximity. Such discontinuous binding sites dominate proteinprotein interactions, but are difficult to identify. To meet this challenge, we combined a computational, structure-based approach and an experimental, high-throughput method. SUPERFICIAL is a program that uses protein structures as input and generates peptide libraries to represent the protein's surface. A large number of the predicted peptides can be simultaneously synthesised applying the SPOT technology. The results of a binding assay subsequently help to elucidate proteinprotein interactions; the approach is applicable to any kind of protein. The crystal structure of the complex of hen egg lysozyme with the well-characterised murine IgG1 antibody HyHEL-5 is available, and the complex is known to have a discontinuous binding site. Using SUPERFICIAL, the entire surface of lysozyme was translated into a peptide library that was synthesised on a cellulose membrane using the SPOT technology and tested against the HyHEL-5 antibody. In this way, it was possible to identify two peptides (longest common sequence and peptide 19) that represented the discontinuous epitope of lysozyme. Copyright (c) 2012 John Wiley & Sons, Ltd.

A Floquet description of phase alternated sequences for efficient homonuclear recoupling in solid perdeuterated systems
Jayanthi(*), S., Akbey, Ü., Uluca(*), B., Oschkinat, H.; Vega(*), S.
Journal of Magnetic Resonance, 234:10-20

Tags: NMR-Supported Structural Biology (Oschkinat)

Abstract: A Floquet description of a phase alternated homonuclear recoupling scheme for perdeuterated systems is presented. As a result, we demonstrate improvements in the recoupling efficiency of the DOuble Nucleus Enhanced Recoupling [DONER; J. Am. Chem. Soc. 131 (2009) 170541 technique by utilizing Phase Alternated Recoupling Irradiation Schemes [PARIS; Chem. Phys. Lett. 469 (2009) 342]. The effect of proton and deuterium radio frequency irradiation during recoupling has been systematically studied and theoretical observations have been verified experimentally using a deuterated model compound, L-Alanine, at 10 and 20 kHz magic angle spinning frequency. Experimental results are well in agreement with theoretical observations, thereby significantly increasing the recoupling efficiency of conventional DONER in perdeuterated systems. (C) 2013 Elsevier Inc. All rights reserved.

From mice to man: chloride transport in leukoencephalopathy
Jentsch, T. J.
Lancet Neurol, 12:626-628

Tags: Physiology and Pathology of Ion Transport (Jentsch)

The Bacterial Translocon SecYEG Opens upon Ribosome Binding
Knyazev(*), D. G., Lents(*), A., Krause, E., Ollinger(*), N., Siligan(*), C., Papinski(*), D., Winter(*), L., Horner(*), A.; Pohl(*), P.
Journal of Biological Chemistry, 288:17941-17946

Tags: Mass Spectrometry (Krause, E.)

Abstract: In co-translational translocation, the ribosome funnel and the channel of the protein translocation complex SecYEG are aligned. For the nascent chain to enter the channel immediately after synthesis, a yet unidentified signal triggers displacement of the SecYEG sealing plug from the pore. Here, we show that ribosome binding to the resting SecYEG channel triggers this conformational transition. The purified and reconstituted SecYEG channel opens to form a large ion-conducting channel, which has the conductivity of the plug deletion mutant. The number of ion-conducting channels inserted into the planar bilayer per fusion event roughly equals the number of SecYEG channels counted by fluorescence correlation spectroscopy in a single proteoliposome. Thus, the open probability of the channel must be close to unity. To prevent the otherwise lethal proton leak, a closed post-translational conformation of the SecYEG complex bound to a ribosome must exist.

Synaptic requiem: a duet for Piccolo and Bassoon
Kononenko, N., Pechstein, A.; Haucke, V.
EMBO J, 32:920-922

Tags: Molecular Pharmacology and Cell Biology (Haucke)

Compromised fidelity of endocytic synaptic vesicle protein sorting in the absence of stonin 2
Kononenko, N. L., Diril(*), M. K., Puchkov, D., Kintscher(*), M., Koo(*), S. J., Pfuhl(*), G., Winter(*), Y., Wienisch(*), M., Klingauf(*), J., Breustedt(*), J., Schmitz(*), D., Maritzen, T.; Haucke, V.
Proc Natl Acad Sci U S A, 110:E526-535

Tags: Molecular Pharmacology and Cell Biology (Haucke),Membrane Traffic and Cell Motility (Maritzen)

Abstract: Neurotransmission depends on the exocytic fusion of synaptic vesicles (SVs) and their subsequent reformation either by clathrin-mediated endocytosis or budding from bulk endosomes. How synapses are able to rapidly recycle SVs to maintain SV pool size, yet preserve their compositional identity, is poorly understood. We demonstrate that deletion of the endocytic adaptor stonin 2 (Stn2) in mice compromises the fidelity of SV protein sorting, whereas the apparent speed of SV retrieval is increased. Loss of Stn2 leads to selective missorting of synaptotagmin 1 to the neuronal surface, an elevated SV pool size, and accelerated SV protein endocytosis. The latter phenotype is mimicked by overexpression of endocytosis-defective variants of synaptotagmin 1. Increased speed of SV protein retrieval in the absence of Stn2 correlates with an up-regulation of SV reformation from bulk endosomes. Our results are consistent with a model whereby Stn2 is required to preserve SV protein composition but is dispensable for maintaining the speed of SV recycling.

The tortoise and the hare revisited
Kononenko, N. L., Pechstein, A.; Haucke, V.
Elife, 2:e01233

Tags: Molecular Pharmacology and Cell Biology (Haucke)

Abstract: Optogenetics and electron microscopy reveal an ultrafast mode of synaptic vesicle recycling, adding a new twist to a 40-year-old controversy.

CRIS-A Novel cAMP-Binding Protein Controlling Spermiogenesis and the Development of Flagellar Bending
Krähling(*), A. M., Alvarez(*), L., Debowski(*), K., Van(*), Q., Gunkel(*), M., Irsen(*), S., Al-Amoudi(*), A., Strünker(*), T., Kremmer(*), E., Krause, E., Voigt(*), I., Wortge(*), S., Waisman(*), A., Weyand(*), I., Seifert(*), R., Kaupp(*), U. B.; Wachten(*), D.
Plos Genet, 9

Tags: Mass Spectrometry (Krause, E.)

Abstract: The second messengers cAMP and cGMP activate their target proteins by binding to a conserved cyclic nucleotide-binding domain (CNBD). Here, we identify and characterize an entirely novel CNBD-containing protein called CRIS (cyclic nucleotide receptor involved in sperm function) that is unrelated to any of the other members of this protein family. CRIS is exclusively expressed in sperm precursor cells. Cris-deficient male mice are either infertile due to a lack of sperm resulting from spermatogenic arrest, or subfertile due to impaired sperm motility. The motility defect is caused by altered Ca2+ regulation of flagellar beat asymmetry, leading to a beating pattern that is reminiscent of sperm hyperactivation. Our results suggest that CRIS interacts during spermiogenesis with Ca2+-regulated proteins that-in mature sperm-are involved in flagellar bending.

Extended and structurally supported insights into extracellular mechanisms of the thyrotropin receptor
Krause, G., Kreuchwig, A.; Kleinau(*), G.
Exp Clin Endocr Diab, 121

Tags: Structural Bioinformatics and Protein Design (Krause, G.)

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Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP)
Campus Berlin-Buch
Robert-Roessle-Str. 10
13125 Berlin, Germany
+4930 94793 - 100 
+4930 94793 - 109 (Fax)

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