Kontakt Motif

[Abigayle Laurenitis]

SmartEnabled by default, AMATI VIOLA's Smart fingering mode intelligently chooses the most realistic fingering for the notes played. As an example, when playing a chromatic passage, the Smart mode chooses to play the notes on the same string when possible, just as a real violaist would do, yielding realistic results. In contrast, when playing a motif moving around different strings in the same area of the fingerboard, fingering on different strings is preferred intelligently and realistically.

The receptor tyrosine kinase MET is essential for embryonic development of vertebrates and the healing of skin wounds in adults. In addition MET signaling is subverted during infection by the facultative intracellular pathogen Listeria monocytogenes, which induces its own uptake into non-phagocytic cells upon MET activation. The surface associated protein InlB functions as bacterial MET agonist by specifically binding to the MET extracellular domain. Structurally, InlB does not resemble the endogenous MET ligand hepatocyte growth factor/scatter factor (HGF/SF). However, the cellular response to MET stimulation by InlB is very similar to that elicited by HGF/SF.

We try to understand the mechanism of ligand-induced MET activation at the molecular level. To this end we solved crystal structures of the complex formed by InlB and the MET ectodomain. (Niemann et al. 2007). The structure revealed that the binding site for InlB does not overlap with that previously described for the β-chain of HGF/SF. MET dimerization is brought about by a small, low-affinity contact formed by the back-sides of two InlB molecules in the 2:2 complex. (Ferraris et al. 2010). As discussed in a recent review, this is reminiscent of MET activation by the HGF/SF splice variant NK1 (Niemann 2013). In cooperation with Prof. Heilemann (Frankfurt) we now use single-molecule fluorescence microscopy to study InlB mediated MET dimerization on cells. (Dietz et al. 2013).

InlB is a multi-domain protein. MET only interacts with the N-terminal internalin domain of InlB, but the other InlB domains contribute to full activation of the MET receptor. We investigate the function of the central domain of InlB called B-repeat. We solved its crystal structure revealing an ubiquitin-like β-grasp fold and we showed that the B-repeat is required for InlB to induce cell motility. (Ebbes et al. 2011). The InlB B-repeat probably binds to a host cell receptor other than MET. Currently, we try to identify this receptor.

MET is a target structure of medical importance due to its role in tissue regeneration. MET agonists could serve as protein therapeutics, e.g. to stimulate wound healing. The structure of the 2:2 InlB/MET signaling active complex, allowed the rational design of a potent MET agonist. (Ferraris et al. 2010; Kolditz et al. 2013; bottom figure).

Resembling a macromolecular syringe, type III secretion systems are multi-protein complexes used by various Gram-negative pathogens to inject effector proteins directly into the host cell cytoplasm. Hydrophobic so-called translocator proteins form the necessary pore in the host cell membrane. Within in the bacterial cytosol, these translocators bind to a chaperone, which itself is not exported. In contrast to classic chaperones, T3S chaperones do not bind or hydrolyze nucleotides.

We solved the first crystal structure of a T3S translocator chaperone, the Yersinia enterocolitica protein SycD. ( Bttner et al. 2008). SycD forms a curved structure consisting of three tetratrico peptide repeats (TPRs). A second structure of SycD in complex with a chaperone-binding peptide derived from the translocator protein YopD shows that the concave face of the curved TPR fold serves as binding site for YopD. ( Schreiner et al. 2012).

In addition to the translocators YopB and YopD, SycD binds to several other T3S proteins enabling it to exert regulatory functions. Currently, we investigate the interaction of SycD with several Y. enterocolitica T3S proteins in vitro. in vitro.

The gastric pathogen H. pylori employs a type IV secretion system (T4SS) to inject the oncogenic effector protein CagA into the stomach epithelium of its human host. The T4SS protein CagL localizes to the T4SS pilus and is essential for injection of CagA into host cells. CagL harbors a RGD motif that probably mediates binding to host cell integrins.

We solved the crystal structure of H. pylori CagL. (Barden et al. 2013). An elongated three-helix bundle forms the structural core of CagL, to which the N-terminal helix is associated only loosely. Structure comparisons suggest that CagL is a H. pylori specific protein. The RGD motif is exposed at the protein surface and thus accessible for interaction with a receptor molecule. In contrast to previously characterized RGD motifs, the RGD motif of CagL is not located in an extended or flexible loop structure but in the middle of a long helix.

We now investigate the molecular basis of the interaction between CagL and host cell receptors.

Lehmann, K., Hause, B., Altmann, D. und Kck, M. (2001) Tomato ribonuclease LX with the functional ER retention motif HDEF is expressed during physiological cell death processes including xylem differentiation, germination and senescence. Plant Physiology 127: 436-449.

Motivation: Accurate prediction of RNA subcellular localization plays an important role in understanding cellular processes and functions. Although post-transcriptional processes are governed by trans-acting RNA binding proteins (RBPs) through interaction with cis-regulatory RNA motifs, current methods do not incorporate RBP-binding information. Results: In this article, we propose DeepLocRNA, an interpretable deep-learning model that leverages a pre-trained multi-task RBP-binding prediction model to predict the subcellular localization of RNA molecules via fine-tuning. We constructed DeepLocRNA using a comprehensive dataset with variant RNA types and evaluated it on the held-out dataset. Our model achieved state-of-the-art performance in predicting RNA subcellular localization in mRNA and miRNA. It has also demonstrated great generalization capabilities, performing well on both human and mouse RNA. Additionally, a motif analysis was performed to enhance the interpretability of the model, highlighting signal factors that contributed to the predictions. The proposed model provides general and powerful prediction abilities for different RNA types and species, offering valuable insights into the localization patterns of RNA molecules and contributing to our understanding of cellular processes at the molecular level. A user-friendly web server is available at:

Premature shedding of flowers, seeds and fruits results significantly reduced yields (5-20%) in important crops (e.g. oilseed rape); flower and petal abscission reduces the sales value in ornamentals. Thus the understanding of cell separation processes is important for competitive horticulture, and for sustainable agriculture that makes optimal use of the arable land available for food and feed production.

IDA encodes a small protein with a N-terminal secretory signal peptide. Arabidopsis plants with mutation in the IDA gene retain their floral organs indefinitely, while overexpression of IDA induces earlier abscission, as well as ectopic shedding of whole flowers, cauline leaves and branches, organs that normally do not abscise in Arabidopsis.

This overexpression phenotype is dependent on the leucine-rich-repeat receptor-like kinases (LRR-RLKs) HAESA (HAE) and HAESA-LIKE2 (HSL2) HAE and HSL2 genes, and is not found in hae hsl2 mutant background, consistent with IDA being the ligand of these receptors.

The active part of IDA is confined within a peptide (EPIP) of 20 amino acids in the C-terminal end. this C-terminal motif is conserved in protein encoded by IDL genes. IDL genes are expressied at sites were cell separation events occur suggesting that IDL peptides also may be involved in cell separation processes. We are presently identifying the receptors of the IDL peptides and elucidating their function.

To reduce your wait at the Jewish Museum Berlin to a minimum, we recommend reserving a time slot ticket from our online ticket shop in advance. However, walk-in tickets are also available at the ticket desk.

The Jewish Museum Berlin will be opening a major exhibition on the GOLEM on September 22. The myth of someone who can create artificial life is the focus of this extensive thematic exhibition. To this day, this well-known legendary Jewish figure continues to inspire generations of artists and writers. Whether as homunculi, cyborgs, robots, or androids: the golem is presented in the exhibition from its creation from a ritual in Jewish mysticism through to popular narrative material in film and literature and its continuation in artistic and digital worlds.

A figure molded from inanimate matter such as dust or clay is brought to life by means of ritual incantations and a specific combination of Hebrew letters. Created by a human and possessing immense physical strength, the soulless creature becomes a helper, a companion, or a rescuer of a Jewish community in danger. There is no setting more closely tied to the story of the golem than Prague. According to legend, Rabbi Judah Loew created a golem out of clay in order to protect the Jewish ghetto from persecution. As in many golem stories, however, the creation gets out of control and becomes a threat even to its creator.

In every epoch, the golem symbolizes the threat scenarios and hopes for redemption of its time. As a figure of thought and a projection screen, the golem combines faith in progress and hope for rescue with the fear of an unleashed power. In seven rooms, the exhibition fathoms the wide range of material on the theme as it has been presented in medieval manuscripts, multifaceted narratives, silent film, and the fine arts over the last two centuries. With more than 120 objects displayed on almost 10,000 sq. feet of exhibition space, subjects such as creativity, creation, power, and redemption are examined. The thematic spectrum ranges from Jewish mysticism to the legend of Prague to the motifs of transformation and doppelgngers. The epilog brings visitors back to the present: Whether as a comic superhero, characters in a computer game, or a cyborg, the golem lives, and with it the question as to what it means to be a human being.

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