A microbial sulfoquinovose monooxygenase pathway that enables sulfosugar assimilation

Williams, Spencer J.; Sharma, Mahima; Lingford, James P.; Petricevic, Marija; Snow, Alexander; Zhang, Yunyang; Järvå, Michael; Mui, Janice; Scott, Nichollas E.; Saunders, Eleanor; Mao, Runyu; Epa, Ruwan; Silva, Bruna da; Pires, Douglas E V; Ascher, David B.; McConville, Malcolm J.; Davies, G.J.; Goddard‐Borger, Ethan D.

doi:10.33774/chemrxiv-2021-08j01

Cited by 2 publications

(1 citation statement)

References 47 publications

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“…It forms part of an SQ-specific ABC transporter cassette found in Agrobacterium tumefaciens. 11,12 This transporter facilitates the import of SQ and SQ and its glycosides, supporting the catabolism of these sulfosugars through a sulfolysis pathway in A. tumefaciens. Similar ABC transporter cassettes, associated with other SQ sulfolysis and sulfoglycolysis pathways, have been identified in other bacteria.…”

Section: Introductionmentioning

confidence: 89%

Capture-and-release of a sulfoquinovose-binding protein on sulfoquinovose-modified agarose

Arumapperuma,

Snow,

Lee

et al. 2024

Preprint

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The solute-binding protein (SBP) components of periplasmic binding protein-dependent ATP-binding cassette (ABC)-type transporters often possess exquisite selectivity for their cognate ligands. Maltose binding protein (MBP), the best studied of these SBPs, has been extensively used as a fusion partner to enable the affinity purification of recombinant proteins. However, other SBPs and SBP-ligand based affinity systems remain underexplored. The sulfoquinovose-binding protein SmoF, is a substrate-binding protein component of the ABC transporter cassette in Agrobacterium tumefaciens involved in importing SQ and its derivatives for SQ catabolism. Here, we show that SmoF binds with high affinity to the octyl glycoside of SQ (octyl-SQ), demonstrating remarkable tolerance to extension of the anomeric substituent. The 3D X-ray structure of the SmoF•octyl-SQ complex reveals accommodation of the octyl chain, which projects to the protein surface, providing impetus for the synthesis of a linker-equipped SQ-amine using a thiol-ene reaction as a key step, and its conjugation to cyanogen bromide modified agarose. We demonstrate the successful capture and release of SmoF from SQ-agarose resin using SQ as competitive eluant, and selectivity for release versus other organosulfonates. We demonstrate that SmoF can be captured and purified from a cell lysate, demonstrating the utility of SQ-agarose in capturing SQ binding proteins from complex mixtures. The present work provides a pathway for development of ‘capture-and-release’ affinity resins for the discovery and study of SBPs.

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Section: Introductionmentioning

confidence: 89%

Capture-and-release of a sulfoquinovose-binding protein on sulfoquinovose-modified agarose

Arumapperuma,

Snow,

Lee

et al. 2024

Preprint

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Genome sequences of Arthrobacter spp. that use a modified sulfoglycolytic Embden-Meyerhof-Parnas pathway

Kaur

Peet²,

Mui³

et al. 2021

Preprint

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BackgroundSulfoglycolysis pathways enable the breakdown of the sulfosugar sulfoquinovose and environmental recycling of its carbon and sulfur content. Several pathways exist for the breakdown of sulfoquinovose that usually lead to production of C3-sulfonates (sulfolactate and 2,3-dihydroxypropanesulfonate) that are excreted and sustain secondary bacterial communities. The prototypical sulfoglycolytic pathway is a variant of the classical Embden-Meyerhof-Parnas pathway that has been described in gram-negative Escherichia coli and results in production of 2,3-dihydroxypropanesulfonate.ResultsWe used enrichment cultures to discover new sulfoglycolytic bacteria from Australian soil samples. Two gram-positive Arthrobacter spp. were isolated that produced sulfolactate as the metabolic end-product. Genome sequences identified a modified sulfoglycolytic Embden-Meyerhof-Parnas (sulfo-EMP) gene cluster that retained the core sulfoglycolysis genes encoding metabolic enzymes, but featuring the replacement of the gene encoding sulfolactaldehyde (SLA) reductase with SLA dehydrogenase, and the absence of sulfoquinovosidase and sulfoquinovose mutarotase genes. The gene clusters were broadly conserved across a range of other sequenced Actinobacteria.ConclusionsWe report the first gram-positive soil bacteria that utilize sulfo-EMP pathways to metabolize SQ. Excretion of sulfolactate is consistent with an aerobic saprophytic lifestyle. This work broadens our knowledge of the sulfo-EMP pathway to include soil bacteria.

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A microbial sulfoquinovose monooxygenase pathway that enables sulfosugar assimilation

Cited by 2 publications

References 47 publications

Capture-and-release of a sulfoquinovose-binding protein on sulfoquinovose-modified agarose

Capture-and-release of a sulfoquinovose-binding protein on sulfoquinovose-modified agarose

Genome sequences of Arthrobacter spp. that use a modified sulfoglycolytic Embden-Meyerhof-Parnas pathway

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