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Long-term social memory of mate copying in Drosophila melanogaster is localized in mushroom bodies
Abstract Long-term social memory (LTSM) is a key feature to elicit the cultural inheritance of behaviour independently of genetics. However, the neurobiological basis of LTSM remains largely unknown. We previously used the Drosophila animal model, which is known to perform mate copying through observational learning of the mate choice of conspecifics to show that the expression of the rutabaga gene, a calcium/calmodulin-dependent adenylyl cyclase (AC-Rut+) that acts as a coincidence detector enabling associative learning, is necessary and sufficient in the γ-Kenyon cells (KCs) of the mushroom bodies (MBs). Here, we show that the expression of AC-Rut+ in both the γ- and the α/β-KCs is required for LTSM involving de novo protein synthesis in a mate-copying context, whether using demonstrations involving real flies or involving pictures of copulating conspecifics. Thus, pathways of short- and long-term memory show considerable overlap in the MBs across social vs. asocial learning contexts.
Efficient Methanol Oxidation Kinetics Enabled by an Ordered Heterocatalyst with Dual Electric Fields
Optimal cultivation concentration of duckweed for pollutant removal from biogas slurry
Unveiling New Reactivities in Complex Mixtures: Synthesis of Tricyclic Pyridinium Derivatives
Crystal structure of the plasmid-encoded R67 dihydrofolate reductase complexed with Congo red an amyloid binding dye
Abstract Plasmid-encoded bacterial R67 dihydrofolate reductase (DHFR) catalyzes the same reaction as the chromosomal counterpart but is highly resistant to the widely used antibiotic Trimethoprim (TMP) unlike the chromosomal enzyme. The structure of Q67H mutant of R67 DHFR complexed with a non-specific inhibitor Congo red (CGR) has been determined at 1.15 Å resolution. In the F o -F c map, one of the two naphthalene moieties in CGR is clearly observed, however, the biphenyl linker and the other naphthalene moiety are not seen owing to flexibility. CGR does not utilize its twofold axis to align with any of the three crystallographic twofold axes of the tetrameric protein instead, it binds like the asymmetrical folate and NADP+ at any one of the four symmetry-related positions in the active site pore. The naphthalene moiety with exocyclic sulphonate ion and amino group, interacts with residues 66–68 from all four protomers via metal-based ionic, van der Waals, stacking, and hydrogen bonding interactions. Preliminary modeling studies suggest variant fragments of CGR targeting one or both Lys32 residues at the site of enlarging pore may yield specific and potent inhibitors. Based on the CGR – protein interactions in the present work, we propose a putative model for the binding of CGR to cross-β amyloid.