Abstract
Phylogenetic reconstruction revealed that most Actinobacterial orthologs of S. coelicolor SCO2837, encoding a metal-dependent galactose oxidase-like protein, are found within Streptomyces and were probably acquired by horizontal gene transfer from fungi. Disruption of SCO2837 (glxA) caused a conditional bld phenotype that could not be reversed by extracellular complementation. Studies aimed at characterising the regulation of expression of glxA showed that it is not a target for other bld genes. We provide evidence that glxA is required for osmotic adaptation, although independently from the known osmotic stress response element SigB. glxA has been predicted to be part of an operon with the transcription unit comprising the upstream cslA gene and glxA. However, both phenotypic and expression studies indicate that it is also expressed from an independent promoter region internal to cslA. GlxA displays an in situ localisation pattern similar to that one observed for CslA at hyphal tips, but localisation of the former is independent of the latter. The functional role of GlxA in relation to CslA is discussed.
Highlights
Galactose oxidase proteins have captivated biochemists due to the peculiar mechanism with which this family of proteins catalyze alcohol oxidation
The related family of glyoxal oxidase proteins shares many of the structural features of galactose oxidase, the presence of ‘kelch’ motifs and the active site structure, its catalytic activity concerns the oxidation of aldehydes into carboxylic acids and is not necessarily functionally homologous to galactose oxidase
To address this and contribute to the very limited knowledge concerning bacterial galactose oxidase-like genes, in this paper we present data describing the functional role of SCO2837, the only putative galactose oxidase encoded by S. coelicolor
Summary
Galactose oxidase proteins have captivated biochemists due to the peculiar mechanism with which this family of proteins catalyze alcohol oxidation. The requirement for a functional CslA during aerial development indicates that its cognate galactose oxidase-like encoding gene may play a role during differentiation To address this and contribute to the very limited knowledge concerning bacterial galactose oxidase-like genes, in this paper we present data describing the functional role of SCO2837, the only putative galactose oxidase encoded by S. coelicolor. We showed that this protein is required for aerial development and its expression is independent from known developmental or stress related regulatory genes.
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