The RavA-ViaA chaperone complex modulates bacterial persistence through its association with the fumarate reductase enzyme

Bhandari, Vaibhav; Reichheld, Sean E.; Houliston, Scott; Lemak, Alexander; Arrowsmith, Cheryl H.; Sharpe, Simon; Houry, Walid A.

doi:10.1016/j.jbc.2023.105199

Cited by 2 publications

References 57 publications

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Novel amylase genes enable utilisation of resistant starch by bifidobacteria relevant to early-life microbiome development

Millar,

Abele,

Harris

et al. 2024

Preprint

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Bifidobacteriumspecies and strains are key members of the gut microbiota, appearing soon after birth and persisting into adulthood. Resistant starch is an important dietary substrate for adult-associated bifidobacteria, where its fermentation supports host health. However, little is known about how different starch structures interact with bifidobacteria across various ages and ecological niches. To address this, we carried out detailed growth kinetics screening ofBifidobacteriumreference strains and unique isolates from breast-fed infants, testing their metabolic interaction with a variety of starch structures.1H NMR metabolomics as well as analysis of CAZyme profiles from genomes were generated for eachBifidobacterium-starch combination. For a subset of resistant starch-utilising isolates, we integrated multi-omics approaches to attain further mechanistic interaction insights. Our results revealed that bifidobacterial starch hydrolysis capabilities are closely associated with their CAZyme profiles and appear to be connected to the niche they occupy. Notably, in one isolate ofBifidobacterium pseudolongum, we identified a novel gene cluster containing three multi-functional amylase enzymes complemented by several starch binding modules which were significantly upregulated in response to resistant starch. This gene cluster was also found in the genomes of bifidobacterial isolates from weaning infants and adults. These findings provide new insights into their participation in the maturation process of the infant gut microbiota. Uncovering mechanisms of metabolic interaction between starch structures and bifidobacteria underscores the importance of this ecological function and potential health implications.

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Novel amylase genes enable utilisation of resistant starch by bifidobacteria relevant to early-life microbiome development

Millar,

Abele,

Harris

et al. 2024

Preprint

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Molecular Characterization of the MoxR AAA+ ATPase of Synechococcus sp. Strain NKBG15041c

Mano,

Noi,

et al. 2024

IJMS

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We isolated a stress-tolerance-related gene from a genome library of Synechococcus sp. NKBG15041c. The expression of the gene in E. coli confers resistance against various stresses. The gene encodes a MoxR AAA+ ATPase, which was designated SyMRP since it belongs to the MRP subfamily. The recombinant SyMRP showed weak ATPase activity and protected citrate synthase from thermal aggregation. Interestingly, the chaperone activity of SyMRP is ATP-dependent. SyMRP exists as a stable hexamer, and ATP-dependent conformation changes were not detected via analytical ultracentrifugation (AUC) or small-angle X-ray scattering (SAXS). Although the hexameric structure predicted by AlphaFold 3 was the canonical flat-ring structure, the structures observed by atomic force microscopy (AFM) and transmission electron microscopy (TEM) were not the canonical ring structure. In addition, the experimental SAXS profiles did not show a peak that should exist in the symmetric-ring structure. Therefore, SyMRP seems to form a hexameric structure different from the canonical hexameric structure of AAA+ ATPase.

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The RavA-ViaA chaperone complex modulates bacterial persistence through its association with the fumarate reductase enzyme

Cited by 2 publications

References 57 publications

Novel amylase genes enable utilisation of resistant starch by bifidobacteria relevant to early-life microbiome development

Novel amylase genes enable utilisation of resistant starch by bifidobacteria relevant to early-life microbiome development

Molecular Characterization of the MoxR AAA+ ATPase of Synechococcus sp. Strain NKBG15041c

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