Must sowing density of intercropping be half of the two sole crops density for providing good performance? (ReMIX Practice abstract)

Outcome: According to some given abiotic and biotic factors and general rules, farmers can create and evaluate the matching OSD for their fields. Practical recommendations: • OSD is influenced by different factors such as soil, vegetation period/climate conditions, choice of species and cultivars, organic vs. conventional system, weeds/pests/diseases control, technical equipment and type of intercropping. • Proportion in yield can vary largely from sowing proportion. Total yield should be higher than the average of sole crops. In a cereal-legume-intercropping, legumes are responsible for a high protein content and cereals have a high plasticity for tillering/compensation. They suppress weeds but also tend to suppress their mixture partner. For central Europe, 80 % of sole crop sowing rate of legumes and 40 % of cereals can be used as a first start (Dierauer et al., 2017). Practical testing/ Farmers’ experiences: Farmers should try out the optimal mixture ratio. Start a small-scale trial with different sowing densities. Replicate more than one year

Ligand chain length drives activation of lipid G protein-coupled receptors

Sphingosine-1-phosphate (S1P) is a lipid mediator that can activate five cell membrane G protein-coupled receptors (GPCRs) which carry a variety of essential functions and are promising drug targets. S1P is composed of a polar zwitterionic head-group and a hydrophobic alkyl chain. This implies an activation mechanism of its cognate receptor that must be significantly different from what is known for prototypical GPCRs (ie receptor to small hydrophilic ligands). Here we aim to identify the structural features responsible for S1P agonism by combining molecular dynamics simulations and functional assays using S1P analogs of different alkyl chain lengths. We propose that high affinity binding involves polar interactions between the lipid head-group and receptor side chains while activation is due to hydrophobic interactions between the lipid tail and residues in a distinct binding site. We observe that ligand efficacy is directly related to alkyl chain length but also varies with receptor subtypes in correlation with the size of this binding pocket. Integrating experimental and computational data, we propose an activation mechanism for the S1P receptors involving agonist-induced conformational events that are conserved throughout class A GPCRs.SCOPUS: ar.jinfo:eu-repo/semantics/publishe

Nucleolar targeting: the hub of the matter

The nucleolus is a dynamic structure that has roles in various processes, from ribosome biogenesis to regulation of the cell cycle and the cellular stress response. Such functions are frequently mediated by the sequestration or release of nucleolar proteins. Our understanding of protein targeting to the nucleolus is much less complete than our knowledge of membrane-spanning translocation systems—such as those involved in nuclear targeting—and the experimental evidence reveals that few parallels exist with these better-characterized systems. Here, we discuss the current understanding of nucleolar targeting, explore the types of sequence that control the localization of a protein to the nucleolus, and speculate that certain subsets of nucleolar proteins might act as hub proteins that are able to bind to multiple protein targets. In parallel to other subnuclear structures, such as PML bodies, the proteins that are involved in the formation and maintenance of the nucleolus are inexorably linked to nucleolar trafficking

Ligand chain length drives activation of lipid G protein-coupled receptors

Sphingosine-1-phosphate (S1P) is a lipid mediator that can activate five cell membrane G proteincoupled receptors (GPCRs) which carry a variety of essential functions and are promising drug targets. S1P is composed of a polar zwitterionic head-group and a hydrophobic alkyl chain. This implies an activation mechanism of its cognate receptor that must be significantly different from what is known for prototypical GPCRs (ie receptor to small hydrophilic ligands). Here we aim to identify the structural features responsible for S1P agonism by combining molecular dynamics simulations and functional assays using S1P analogs of different alkyl chain lengths. We propose that high affinity binding involves polar interactions between the lipid head-group and receptor side chains while activation is due to hydrophobic interactions between the lipid tail and residues in a distinct binding site. We observe that ligand efficacy is directly related to alkyl chain length but also varies with receptor subtypes in correlation with the size of this binding pocket. Integrating experimental and computational data, we propose an activation mechanism for the S1P receptors involving agonist-induced conformational events that are conserved throughout class A GPCRs