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Celma, L.

Publications and source records attributed to Celma, L..

2 recordsLinked to original sources

c-di-GMP-Dependent Regulation of Motility by comFB and comFC

ComFB is encoded in the comF operon of Bacillus subtilis, situated between the genes for ComFA and ComFC. The latter two proteins are essential for natural transformation, whereas ComFB is dispensable. We show here that ComFB binds specifically and with high affinity to the second messenger c-di-GMP and that ComFB acts as a c-di-GMP receptor to inhibit swarming and swimming motility, apparently by interfering with flagellar activity. We show further that in the absence of ComFC, swarming is completely abrogated by a mechanism that requires FB. These results reveal a new c-di-GMP regulatory system that controls motility independently of MotI. IMPORTANCEBacterial motility is subject to tight regulation, and the second messenger c-di-GMP is often involved in the production and activity of flagella. Revealing the mechanisms of these regulatory pathways is broadly important for understanding bacterial motility and of c-di-GMP-related processes. We show that ComFB is a specific, high-affinity receptor for c-di-GMP that decreases the activity of flagella to control swarming and swimming motility in Bacillus subtilis.

microbiology↗

ComF is a key mediator in single-stranded DNA transport and handling during natural transformation

Natural transformation plays a major role in the spreading of antibiotic resistances and virulence factors. Whilst bacterial species display specificities in the molecular machineries allowing transforming DNA capture and integration into their genome, the ComF(C) protein is essential for natural transformation in all Gram-positive and - negative species studied. Despite this, its role remains largely unknown. Here, we show that Helicobacter pylori ComF is not only involved in DNA transport through the cell membrane, but it also required for the handling of the ssDNA once it is delivered into the cytoplasm. ComF crystal structure revealed the presence of a zinc-finger motif and a putative phosphoribosyl transferase domain, both necessary for its in vivo activity. ComF is a membrane-associated protein with affinity for single-stranded DNA. Collectively, our results suggest that ComF provides the link between the transport of the transforming DNA into the cytoplasm and its handling by the recombination machinery.

microbiology↗