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Gnidovec, L.

Publications and source records attributed to Gnidovec, L..

2 recordsLinked to original sources

Competence repression by the SPβ prophage in Bacillus subtilis revealed by transcriptomics across culture conditions

Prophages are near-ubiquitous in bacterial genomes, yet their effects on host physiology are typically assayed under a narrow range of laboratory conditions, mostly involving DNA-damaging agents or physical and chemical stress. This leaves open the question of which ecological and physiological conditions trigger prophage-host interaction, and whether the outcome benefits the host or the prophage. Here, we used publicly available transcriptomic data to investigate conditions promoting prophage-host interaction in Bacillus subtilis. This analysis identified that competence strongly induces prophage gene expression. To further investigate the role of competence, we used two sets of B. subtilis strains: a natural SP{beta} lysogen strain and its cured counterpart, and a natural non-lysogenic strain and the same strain lysogenised with SP{beta}. Under competence-inducing conditions, both lysogen strains showed lower expression of the competence genes compared with their non-lysogenic counterparts. This result was corroborated by transformation assays that showed consistently lower transformation efficiency in the lysogen strains, and by fluorescence microscopy using a transcriptional reporter for the late competence gene. Because competence is a principal route for horizontal gene transfer in B. subtilis, prophage repression of the competence programme constrains host DNA uptake and evolvability. More broadly, these results show that mining public transcriptomes for condition effects can guide experimental effort towards prophage-host phenotypes that conventional laboratory conditions would miss.

microbiology↗

CONDENSATES OF SYNAPTIC VESICLES AND SYNAPSIN ARE MOLECULAR BEACONS FOR ACTIN SEQUESTERING AND POLYMERIZATION

Neuronal communication relies on precisely maintained synaptic vesicle (SV) clusters, which assemble via liquid-liquid phase separation (LLPS). This process requires synapsins, the major synaptic phosphoproteins, which are known to bind actin. The reorganization of SVs, synapsins and actin is a hallmark of synaptic activity, but their interplay is still unclear. Here, we combined the reconstitution approaches, expansion microscopy, super-resolution imaging and cryo-electron tomography to dissect the roles of synapsin-SV condensates in the organization of the presynaptic actin cytoskeleton. Our data indicate that LLPS of synapsin initiates actin polymerization, allowing for SV:synapsin:actin assemblies to facilitate the mesoscale organization of SV clusters along axons mimicking the native presynaptic organization in both lamprey and mammalian synapses. Understanding the relationship between the actin network and synapsin-SVs condensates is an essential building block on a roadmap to unravel how coordinated neurotransmission along the axon enables circuit function and behavior.

cell biology↗