Abnormal c-Fos expression in TetTag mice containing fos-EGFP.

Molecular and genetic techniques now allow selective tagging and manipulation of the population of neurons, often referred to as "engram cells," that were active during a specific experience. One common approach to labeling these cells is to use the transgenic mouse (TetTag). In addition to tagging cells active during learning, it is common to examine the reactivation of these cells using immediate early gene (IEG) expression as an index of neural activity.

Measuring Bacterial Flagellar Motor Dynamics via a Bead Assay.

The bacterial flagellar motor (BFM) is a rotary molecular machine that drives critical bacterial processes including motility, chemotaxis, biofilm formation, and infection. For over two decades, the bead assay, which measures the rotation of a microparticle attached to the flagellum of a surface-attached bacterium, has been instrumental in deciphering the motor's biophysical mechanisms. This technique has not only quantified the rotational speed and frequency of directional switching as a function of the viscous load on the flagellum but has also revealed the BFM's capacity for mechanosensitive speed modulation, adapting to environmental conditions.

Combinatorial transcription factor binding encodes cis-regulatory wiring of mouse forebrain GABAergic neurogenesis.

Transcription factors (TFs) bind combinatorially to cis-regulatory elements, orchestrating transcriptional programs. Although studies of chromatin state and chromosomal interactions have demonstrated dynamic neurodevelopmental cis-regulatory landscapes, parallel understanding of TF interactions lags. To elucidate combinatorial TF binding driving mouse basal ganglia development, we integrated chromatin immunoprecipitation sequencing (ChIP-seq) for twelve TFs, H3K4me3-associated enhancer-promoter interactions, chromatin and gene expression data, and functional enhancer assays.

Molecular model of a bacterial flagellar motor reveals a "parts-list" of protein adaptations to increase torque.

One hurdle to understanding how molecular machines work, and how they evolve, is our inability to see their structures . Here we describe a minicell system that enables cryogenic electron microscopy imaging and single particle analysis to investigate the structure of an iconic molecular machine, the bacterial flagellar motor, which spins a helical propeller for propulsion. We determine the structure of the high-torque motor including the subnanometre-resolution structure of the periplasmic scaffold, an adaptation essential to high torque.