Soliton trains in Bose-Fermi mixtures

We theoretically consider the formation of bright solitons in a mixture of Bose and Fermi degenerate gases. While we assume the forces between atoms in a pure Bose component to be effectively repulsive, their character can be changed from repulsive to attractive in the presence of fermions provided the Bose and Fermi gases attract each other strongly enough. In such a regime the Bose component becomes a gas of effectively attractive atoms. Hence, generating bright solitons in the bosonic gas is possible. Indeed, after a sudden increase of the strength of attraction between bosons and fermions (realized by using a Feshbach resonance technique or by firm radial squeezing of both samples) soliton trains appear in the Bose-Fermi mixture.Comment: 4 pages, 4 figure

Structural mechanism of GTPase-powered ribosome-tRNA movement

GTPases are regulators of cell signaling acting as molecular switches. The translational GTPase EF-G stands out, as it uses GTP hydrolysis to generate force and promote the movement of the ribosome along the mRNA. The key unresolved question is how GTP hydrolysis drives molecular movement. Here, we visualize the GTPase-powered step of ongoing translocation by time-resolved cryo-EM. EF-G in the active GDP–Pi form stabilizes the rotated conformation of ribosomal subunits and induces twisting of the sarcin-ricin loop of the 23 S rRNA. Refolding of the GTPase switch regions upon Pi release initiates a large-scale rigid-body rotation of EF-G pivoting around the sarcin-ricin loop that facilitates back rotation of the ribosomal subunits and forward swiveling of the head domain of the small subunit, ultimately driving tRNA forward movement. The findings demonstrate how a GTPase orchestrates spontaneous thermal fluctuations of a large RNA-protein complex into force-generating molecular movement

Malaria pigment hemozoin impairs gm-csf receptor expression and function by 4-hydroxynonenal

Malarial pigment hemozoin (HZ) generates the lipoperoxidation product 4-hydroxynonenal (4-HNE), which is known to cause dysregulation of the immune response in malaria. The inhibition of granulocyte macrophage colony-stimulating factor (GM-CSF)-dependent differentiation of dendritic cells (DC) by HZ and 4-HNE was previously described in vitro, and the GM-CSF receptor (GM-CSF R) was hypothesised to be a primary target of 4-HNE in monocytes. In this study, we show the functional impact of HZ on GM-CSF R in monocytes and monocyte-derived DC by (i) impairing GM-CSF binding by 50 ± 9% and 65 ± 14%, respectively (n = 3 for both cell types); (ii) decreasing the expression of GM-CSF R functional subunit (CD116) on monocyte’s surface by 36 ± 11% (n = 6) and in cell lysate by 58 ± 16% (n = 3); and (iii) binding of 4-HNE to distinct amino acid residues on CD116. The data suggest that defective DC differentiation in malaria is caused by GM-CSF R dysregulation and GM-CSF R modification by lipoperoxidation product 4-HNE via direct interaction with its CD116 subunit

Evaluation of small mammal pet supplies offered in German retail under animal welfare aspects

German retailers offer a large variety of accessories for pets. However, not all products are suitable for pet husbandry. Several articles can negatively influence the wellbeing of pets or cause injuries, but empirical studies that evaluate accessories for small pets under animal welfare aspects are rare. In the present study, we assessed articles manufactured or sold in Germany in the product categories pet cages, hay racks, running wheels, exercise balls, harnesses and leashes, tube systems, and hamster bedding. To do so, we searched 28 German websites, visited 50 pet shops and 13 home improvement and garden centers on site and afterwards examined the animal welfare compliance of the products according to various evaluation criteria. Most of the examined products were rated not suitable for pet husbandry and were animal-welfare-adverse. This result applies to 86.1% (n = 87) of the 101 assessed running wheel models, 82.7% (n = 172) of the 208 assessed pet cage models and 55.6% (n = 40) of the 72 assessed hay rack models. The articles in the product categories exercise balls, harnesses and leashes, tube systems, and hamster bedding were also found unsuitable due to animal welfare concerns. Furthermore, we found clear shortcomings regarding article declarations. In some cases, relevant product information (e.g., dimensions) were missing, or the presented information was too general (e.g., rodent cage). Improperly declared pet accessories make it difficult for pet owners to decide whether a product is suitable or unsuitable for the species they keep. A declaration duty for manufacturers of pet products could ensure that German retailers only offer properly declared pet accessories and facilitate the decision for pet owners to purchase products appropriate for the pets they keep. Furthermore, a voluntary product certification for manufacturers would allow retailers to check the animal welfare compliance of articles before including them in their assortment. If a product is unsuitable for pet husbandry because it does not meet the set requirements, it must be considered animal-welfare-adverse and removed from the assortment. As done for the Austrian “animal welfare label,” an independent, qualified third party could do the certification

Development and exploratory cluster-randomised opportunistic trial of a theory-based intervention to enhance physical activity among adolescents

Peer reviewedPostprin

Chemically monoubiquitinated PEX5 binds to the components of the peroxisomal docking and export machinery

Peroxisomal matrix proteins contain either a peroxisomal targeting sequence 1 (PTS1) or a PTS2 that are recognized by the import receptors PEX5 and PEX7, respectively. PEX5 transports the PTS1 proteins and the PEX7/PTS2 complex to the docking translocation module (DTM) at the peroxisomal membrane. After cargo release PEX5 is monoubiquitinated and extracted from the peroxisomal membrane by the receptor export machinery (REM) comprising PEX26 and the AAA ATPases PEX1 and PEX6. Here, we investigated the protein interactions of monoubiquitinated PEX5 with the docking proteins PEX13, PEX14 and the REM. “Click” chemistry was used to synthesise monoubiquitinated recombinant PEX5. We found that monoubiquitinated PEX5 binds the PEX7/PTS2 complex and restores PTS2 protein import in vivo in ¿PEX5 fibroblasts. In vitro pull-down assays revealed an interaction of recombinant PEX5 and monoubiquitinated PEX5 with PEX13, PEX14 and with the REM components PEX1, PEX6 and PEX26. The interactions with the docking proteins were independent of the PEX5 ubiquitination status whereas the interactions with the REM components were increased when PEX5 is ubiquitinated.We are grateful to Stephen J. Gould (Johns Hopkins University, Baltimore), Nancy E. Braverman (McGill University, Montreal), Wolfgang Schliebs (Ruhr University, Bochum) and Daniel Passon (EMBL, Hamburg) for providing plasmids and antibodies. Work in J.E.A. lab is funded by FEDER (Fundo Europeu de Desenvolvimento Regional), through COMPETE 2020 – Operacional Programme for Competitiveness and Internationalization (POCI), Portugal 2020, and by Portuguese funds through Fundação para a Ciência e Tecnologia (FCT)/Ministério da Ciência, Tecnologia e Inovação in the framework of the projects “Institute for Research and Innovation in Health Sciences” (POCI-01-0145-FEDER-007274) and “The molecular mechanisms of peroxisome biogenesis” (PTDC/BEXBCM/2311/2014), and through Norte 2020 – Programa Operacional Regional do Norte, under the application of the “Porto Neurosciences and Neurologic Disease Research Initiative at i3S” (NORTE-01-0145-FEDER-000008). We acknowledge support by the Open Access Publishing Fund of the University of Tübingen and the Deutsche Forschungsgemeinschaft for publishing costs