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Welsch, N.

Publications and source records attributed to Welsch, N..

2 recordsLinked to original sources

A novel membrane-spanning one-component system controls β-glucan utilization in marine Bacteroidota

One of the most prevalent and bioavailable glycans in marine systems is the {beta}-glucan laminarin. Members of the phylum Bacteroidota are particularly well adapted to degrade this and other polysaccharides. Here, we describe a membrane-spanning one-component system that regulates laminarin utilization in marine Bacteroidota. We analyzed this {beta}-glucan utilization regulator (BguR) type in the marine model bacterium Formosa agariphila KMM3901T. Deletion of the regulator gene abolishes growth on laminarin, whereas the wild type exhibits more than 80-fold induction of the associated genomic gene cluster, indicating the regulators role as a transcriptional activator for laminarin utilization. Structural predictions show that its periplasmic sensor domain resembles those of hybrid two-component systems (HTCSs), although the absence of phosphorylation domains and distinct architecture indicate a completely different, ATP-independent mode-of-action. Comparative genomics show that this regulator is widespread among Bacteroidota, exhibiting lineage-specific distribution patterns similar to hallmark features such as tandem SusCD-like pairs. BguR is frequently found in close proximity to {beta}-glucan-targeting PULs in the genome, implying a defined substrate preference that extends beyond laminarin. These findings suggest a previously unrecognized regulatory mechanism for glycan sensing in marine bacteria, shedding light on an important facet of the marine carbon cycle. IMPORTANCEAlthough recent research has provided detailed insights into the enzymatic breakdown of algal glycans by marine bacteria, the regulatory mechanisms that govern specific carbohydrate utilization strategies remain largely unexplored. This study reveals a novel regulatory mechanism for {beta}-glucan use by marine Bacteroidota. We identified a membrane-embedded one-component regulator that directly links sensing and utilization of laminarin, a major algal polysaccharide in the oceans. Unlike traditional two-component systems, the new regulator operates without phosphorelays. The regulator and its associated laminarin PULs are widely conserved across diverse marine bacteria and even linked to other {beta}-glucan types, indicating a shared regulatory strategy for carbon acquisition from structurally related substrates. These findings advance our understanding of how key ocean microbes coordinate polysaccharide breakdown.

microbiology↗

Novel laminarin-binding CBMs in multimodular proteins of marine Bacteroidota feature prominently in phytoplankton blooms

The {beta}-(1,3)-glucan laminarin functions as storage polysaccharide in marine stramenophiles such as diatoms. Laminarin is abundant, water-soluble and structured simply, making it an attractive substrate for marine bacteria. As a consequence, many marine bacteria have developed competitive strategies to scavenge and decompose laminarin, which involves carbohydrate-binding modules (CBMs) as key players. We therefore functionally and structurally characterized two yet unassigned domains as laminarin-binding CBMs in multimodular proteins from our model bacterium Christiangramia forsetii KT0803T, hereby unveiling the novel laminarin-binding CBM families CBMxx and CBMyy (official CAZy numbering will be provided upon acceptance of the manuscript in a peer-reviewed journal). We discovered four CBMxx repeats in a surface glycan-binding protein (SGBP) and a single CBMyy combined with a glycoside hydrolase module from family 16 (GH16_3). Our analyses revealed that both modular proteins have an elongated shape, and that the GH16_3 displayed a higher flexibility than the SGBP. While motility of both polypeptide chains may facilitate recognition and/or degradation of laminarin, constraints in the SGBP may support docking of laminarin onto the bacterial surface. The exploration of bacterial metagenome-assembled genomes (MAGs) from phytoplankton blooms in the North Sea revealed that both laminarin-binding CBM families are widely distributed among marine Bacteroidota, illustrating the high adaptability of modularity in sugar-binding and -degrading proteins. High expression of CBMxx- and CBMyy-containing proteins during phytoplankton blooms further underpins their importance in marine laminarin usage.

biochemistry↗