Project description:We have isolated a likely bacterial pathogen from cerebrospinal fluid from a Ugandan infant suffering from hydrocephalus. Whole-genome sequencing and assembly of the genome of the clinical isolate, as well as that of a previously deposited reference strain, identified the isolate as Paenibacillus thiaminolyticus, which has not been associated with widespread human infections.

| S-EPMC7380522 | biostudies-literature

RNA-seq analyses of phase variation-dependent genes in Paenibacillus polymyxa E681

Project description:Paenibacillus polymyxa is a root-associated plant growth-promoting rhizobacterium. It was reported that many strains of P. polymyxa naturally exhibited the phenotypic variation. In the phase variation, the characteristics of the wild-type ‘B’ and the variant ‘F’ are very different in sporulation formation, motility, antibiotic ability and so on. For better understanding of the actual physiological changes, we performed RNA-seq analyses of P. polymyxa E681 to compare genome wide patterns of gene expression. As a result, we obtained 1,062 differentially expressed genes related to flagellar assembly and transport systems.

2020-10-13 | GSE93062 | GEO

Alpha-L-fucosidase isoenzyme iso2 from Paenibacillus thiaminolyticus.

Project description:?-L-Fucosidases are enzymes involved in metabolism of ?-L-fucosylated molecules, compounds with a fundamental role in different life essential processes including immune response, fertilization and development, but also in some serious pathological events. According to the CAZy database, these enzymes belong to families 29 and 95. Some of them are also reported to be able to catalyze transglycosylation reactions, during which ?-L-fucosylated molecules, representing compounds of interest especially for pharmaceutical industry, are formed.Activity-based screening of a genomic library was used to isolate the gene encoding a novel ?-L-fucosidase. The enzyme was expressed in E.coli and affinity chromatography was used for purification of His-tagged ?-L-fucosidase. Standard activity assay was used for enzyme characterization. Thin layer chromatography and mass spectrometry were used for transglycosylation reactions evaluation.Using a genomic library of Paenibacillus thiaminolyticus, constructed in E.coli DH5? cells, nucleotide sequence of a new ?-L-fucosidase isoenzyme was determined and submitted to the EMBL database (HE654122). However, no similarity with enzymes from CAZy database families 29 and 95 was detected. This enzyme was produced in form of histidine-tagged protein in E.coli BL21 (DE3) cells and purified by metaloaffinity chromatography. Hydrolytic and transglycosylation abilities of ?-L-fucosidase iso2 were tested using different acceptor molecules.In this study, new enzyme ?-L-fucosidase iso2 originating from Paenibacillus thiaminolyticus was described and prepared in recombinant form and its hydrolytic and transglycosylation properties were characterized. As a very low amino acid sequence similarity with known ?-L-fucosidases was found, following study could be important for different biochemical disciplines involving molecular modelling.

| S-EPMC4445282 | biostudies-literature

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