Adam Ostrowski

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Biofilms represent the predominant mode of microbial growth in the natural environment. Bacillus subtilis is a ubiquitous Gram-positive soil bacterium that functions as an effective plant growth-promoting agent. The biofilm matrix is composed of an exopolysaccharide and an amyloid fiber-forming protein, TasA, and assembles with the aid of a small secreted(More)
In the natural environment bacteria predominantly live adhered to a surface as part of a biofilm. While many of the components needed for biofilm assembly are known, the mechanism by which microbes sense and respond to contact with a surface is poorly understood. Bacillus subtilis is a Gram-positive model for biofilm formation. The DegS-DegU two-component(More)
Protein O-GlcNAcylation is an abundant, dynamic and reversible type of protein post-translational modification in animals that has been implicated in signalling processes linked to innate immunity, stress response, growth factor response, transcription, translation and proteosomal degradation. Only two enzymes, O-GlcNAc (O-linked N-acetylglucosamine)(More)
Two hundred participants, 50 in each of 4 age ranges (19-29 years, 30-49 years, 50-69 years, 70-90 years) were tested for short-term working memory, speed of processing, and online processing of 3 types of sentences in which an initially assigned syntactic structure and/or semantic interpretation had to be revised. Self-paced reading times were longer for(More)
The assembly of the bacterial flagellum is exquisitely controlled. Flagellar biosynthesis is underpinned by a specialized type III secretion system that allows export of proteins from the cytoplasm to the nascent structure. Bacillus subtilis regulates flagellar assembly using both conserved and species-specific mechanisms. Here, we show that YvyG is(More)
Post-translational modification of proteins is a ubiquitous mechanism of signal transduction in all kingdoms of life. One such modification is addition of O-linked N-acetylglucosamine to serine or threonine residues, known as O-GlcNAcylation. This unusual type of glycosylation is thought to be restricted to nucleocytoplasmic proteins of eukaryotes and is(More)
Background: Protein O-GlcNAcylation is essential for function and stability of many proteins in metazoa and is essential for development. Results: Thermobaculum terrenum encodes a functional O-GlcNAc hydrolase and a conserved O-GlcNAc-transferase. Conclusion: T. terrenum is the first known bacterium to possess the components for a functional O-GlcNAc(More)
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