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Importance Peptidoglycan is a key element of the bacterial cell wall to maintain the cell shape and protect the cell from bursting. Peptidoglycan degradation, by peptidoglycan hydrolysis and autolysins, occurs during growth and cell division. Since peptidoglycan hydrolases are important for virulence, envelope integrity and regulation of cell division, it is valuable to investigate their function and regulation. Notably, PcsB-like proteins such as Usp45 have been proposed as new targets for antimicrobial drugs and could also be target for the development of food-grade suicide systems. In addition, although various other expression and secretion systems have been developed for use in Lactococcus lactis, the most-used signal peptide for protein secretion in this bacterium is that of the Usp45 protein. Thus, elucidating the biological function of Usp45, and determining factors affecting its expression, would contribute to optimize several applications.Antibiotics are used to treat or prevent some types of bacterial infection. The inappropriate use of antibiotics unnecessarily promotes antibiotic resistance and increases resistant bacteria, and controlling these bacteria is difficult. While the emergence of drug-resistant bacteria is a serious problem, the behavior of drug-resistant bacteria is not fully understood. In this study, we investigated the behavior of Streptococcus mutans, a major etiological agent of dental caries that is resistant to bacitracin, which is a cell wall-targeting antibiotic, and focused on biofilm formation in the presence of bacitracin. S. click here mutans UA159 most strongly induced extracellular DNA (eDNA)-dependent biofilm formation in the presence of bacitracin at 1/8 minimum inhibitory concentration (MIC). The ΔmbrC and ΔmbrD mutant strains, which lack bacitracin resistance, also formed biofilms in the presence of bacitracin at 1/2 x MIC. This difference between the WT and the mutants was caused by the induction of atlA expression in teria have spread, it is important to understand the behavior of resistant bacteria. Streptococcus mutans is bacitracin-resistant, and the 1/8 x MIC of bacitracin, which is a cell wall-targeted antibiotic, induced eDNA-dependent biofilm formation. The ΔmbrC and ΔmbrD strains, which are not resistant to bacitracin, also formed biofilms in the presence of bacitracin at 1/2 x MIC, and both biofilms of wild and mutants promoted horizontal gene transfer. Another cell wall-targeted antibiotic, vancomycin, showed similar effects on biofilms and gene transfer as bacitracin. Thus, treatment with cell wall-targeted antibiotics may promote the spread of drug-resistant genes in biofilms. Therefore, the behavior of resistant bacteria in the presence of antibiotics at sub-MICs should be investigated when using antibiotics.Flavobacterium psychrophilum causes bacterial cold-water disease in wild and aquaculture-reared fish, and is a major problem for salmonid aquaculture. The mechanisms responsible for cold-water disease are not known. It was recently demonstrated that the related fish pathogen, Flavobacterium columnare, requires a functional type IX protein secretion system (T9SS) to cause disease. T9SSs secrete cell-surface adhesins, gliding motility proteins, peptidases, and other enzymes, any of which may be virulence factors. The F. psychrophilum genome has genes predicted to encode components of a T9SS. Here, we used a SacB-mediated gene deletion technique recently adapted for use in the Bacteroidetes to delete a core F. psychrophilum T9SS gene, gldN The ΔgldN mutant cells were deficient for secretion of many proteins in comparison to wild-type cells. Complementation of the mutant with wild-type gldN on a plasmid restored secretion. Compared to wild-type and complemented strains, the ΔgldN mutant was deficient in adhesion, gliding motility, and in extracellular proteolytic and hemolytic activities. The ΔgldN mutant exhibited reduced virulence in rainbow trout and complementation restored virulence, suggesting that the T9SS plays an important role in the disease.IMPORTANCE Bacterial cold-water disease, caused by F. psychrophilum, is a major problem for salmonid aquaculture. Little is known regarding the virulence factors involved in this disease, and control measures are inadequate. A targeted gene deletion method was adapted to F. psychrophilum and used to demonstrate the importance of the T9SS in virulence. Proteins secreted by this system are likely virulence factors, and targets for the development of control measures.Pectin deconstruction is the initial step in breaking the recalcitrance of plant biomass by using selected microorganisms that encode for pectinolytic enzymes. Pectate lyases that cleave α-1,4-galacturonosidic linkage of pectin are widely used in industries, such as paper making and fruit softening. However, reports on pectate lyases with good thermostability are few. Here, two pectate lyases (CbPL3 and CbPL9) from a hyperthermophilic bacterium Caldicellulosiruptor bescii, respectively, belonged to family 3 and family 9 polysaccharide lyases, were investigated. Biochemical properties on two CbPLs were shown similarly under optimized conditions of 80°C-85°C and pH 8-9. However, the degradation products from pectin and polygalacturonic acids (pGA) were different. A family-66 carbohydrate-binding module (CbCBM66), located in the N-terminus of two CbPLs, shares 100% amino acid identity. CbCBM66-truncated mutant of CbPL9 showed lower activities than the wild-type, whereas the CbPL3 with CbCBM66 knock-out portion werature, low optimum pH, and good thermostability at evaluated temperature. A family-66 carbohydrate binding module (CbCBM66) was identified in two CbPLs with sharing 100% amino acid identity. Deletion of CbCBM66 dramatically decreased the activity of CbPL9, but increase the activity and thermostability of CbPL3, suggesting the different roles of CbCBM66 in two enzymes. Moreover, the degradation products by two CbPLs were different. These results revealed these enzymes could represent a potential pectate lyase for applications in paper and textile industries.The broad-host-range conjugative plasmids have developed diverse adaptive mechanisms defining the range of their promiscuity. The BHR conjugative RA3 plasmid, the archetype of the IncU group, can transfer between, replicate and be maintained in representatives of Alpha-, Beta- and Gammaproteobacteria Its stability module encompasses ten ORFs apparently organized into five operons, all transcribed in the same direction from several strong promoters that are tightly regulated either by autorepressors or by global plasmid-encoded regulators. In this paper, we demonstrate that owing to an efficient RNA polymerase read-through, the transcription from the first promoter, orf02p, may continue through the whole module. Moreover, an analysis of mRNA produced from the WT stability module and its deletion variants deprived of particular internal transcription initiation sites reveals that in fact each operon may be transcribed from any upstream promoter giving rise to multicistronic transcripts of variable length creating an additional level of gene expression control by transcript dosage adjustment.
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