Structural and Biochemical Basis for Mannan Utilization by Caldanaerobius polysaccharolyticus Strain ATCC BAA-17

Chekan, Jonathan R.; Kwon, In Hyuk; Agarwal, Vinayak; Dodd, Dylan; Revindran, Vanessa; Mackie, Roderick I.; Cann, Isaac; Nair, Satish K.

doi:10.1074/jbc.m114.579904

Cited by 13 publications

(10 citation statements)

References 39 publications

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“…There are several transcriptome analysis studies that allowed the incubation of the target microorganism in the presence of inducing compounds through a short (couple of hours) [ 13 , 14 , 68 – 71 ] up to a long (24 or even 50 h) time frame [ 72 , 73 ]. In the latter studies the inducer was treated, as carbon source where extended time is required for its consumption.…”

Section: Discussionmentioning

confidence: 99%

Deciphering the signaling mechanisms of the plant cell wall degradation machinery in Aspergillus oryzae

et al. 2015

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BackgroundThe gene expression and secretion of fungal lignocellulolytic enzymes are tightly controlled at the transcription level using independent mechanisms to respond to distinct inducers from plant biomass. An advanced systems-level understanding of transcriptional regulatory networks is required to rationally engineer filamentous fungi for more efficient bioconversion of different types of biomass.ResultsIn this study we focused on ten chemically defined inducers to drive expression of cellulases, hemicellulases and accessory enzymes in the model filamentous fungus Aspergillus oryzae and shed light on the complex network of transcriptional activators required. The chemical diversity analysis of the inducers, based on 186 chemical descriptors calculated from the structure, resulted into three clusters, however, the global, metabolic and extracellular protein transcription of the A. oryzae genome were only partially explained by the chemical similarity of the enzyme inducers. Genes encoding enzymes that have attracted considerable interest such as cellobiose dehydrogenases and copper-dependent polysaccharide mono-oxygenases presented a substrate-specific induction. Several homology-model structures were derived using ab-initio multiple threading alignment in our effort to elucidate the interplay of transcription factors involved in regulating plant-deconstructing enzymes and metabolites. Systematic investigation of metabolite-protein interactions, using the 814 unique reactants involved in 2360 reactions in the genome scale metabolic network of A. oryzae, was performed through a two-step molecular docking against the binding pockets of the transcription factors AoXlnR and AoAmyR. A total of six metabolites viz., sulfite (H2SO3), sulfate (SLF), uroporphyrinogen III (UPGIII), ethanolamine phosphate (PETHM), D-glyceraldehyde 3-phosphate (T3P1) and taurine (TAUR) were found as strong binders, whereas the genes involved in the metabolic reactions that these metabolites appear were found to be significantly differentially expressed when comparing the inducers with glucose.ConclusionsBased on our observations, we believe that specific binding of sulfite to the regulator of the cellulase gene expression, AoXlnR, may be the molecular basis for the connection of sulfur metabolism and cellulase gene expression in filamentous fungi. Further characterization and manipulation of the regulatory network components identified in this study, will enable rational engineering of industrial strains for improved production of the sophisticated set of enzymes necessary to break-down chemically divergent plant biomass.Electronic supplementary materialThe online version of this article (doi:10.1186/s12918-015-0224-5) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Deciphering the signaling mechanisms of the plant cell wall degradation machinery in Aspergillus oryzae

et al. 2015

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“…In the latter, two proteins (a SusD-like protein and a surface glycan binding protein specific for mannose) are involved in mannoside recognition and sequestration (Cuskin et al, 2015b). The 3D structure of the binding element of a probable β-mannan degradation pathway in the thermophilic anaerobic bacterium Caldanaerobius polysaccharolyticus ATCC BAA-17 also has been described (Chekan et al, 2014). Here, mannobiose and mannotriose recognition involves a solute-binding component of an ATP-binding cassette (ABC) transporter.…”

Section: Recognition Of Eukaryotic Mannosides By Bacteriamentioning

confidence: 99%

“…Recently, two PUL-like systems involved in β-mannan degradation by Caldanaerobius polysaccharolyticus ATCC BAA-17, a thermophilic bacterium isolated from hot-spring sediments, have been discovered using transcriptomics (Chekan et al, 2014). These two multigenic systems together allow complete mannan metabolization.…”

Section: (2) Soil and Spring Bacteriamentioning

confidence: 99%

Mannoside recognition and degradation by bacteria

et al. 2016

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Mannosides constitute a vast group of glycans widely distributed in nature. Produced by almost all organisms, these carbohydrates are involved in numerous cellular processes, such as cell structuration, protein maturation and signalling, mediation of protein-protein interactions and cell recognition. The ubiquitous presence of mannosides in the environment means they are a reliable source of carbon and energy for bacteria, which have developed complex strategies to harvest them. This review focuses on the various mannosides that can be found in nature and details their structure. It underlines their involvement in cellular interactions and finally describes the latest discoveries regarding the catalytic machinery and metabolic pathways that bacteria have developed to metabolize them.

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“…The newly created GT108 family only contains six characterized members, all acting on mannogen, a linear β-1,2polymannoside. In contrast, the GH130 family is much more polyspecific, with 18 characterized members, of which 3 are β-1,2mannosidases [12,13] and 14 are glycoside phosphorylases acting on a large variety of substrates, such asβ-1,4-mannooligosaccharides [14][15][16][17][18], β-1,4mannosyl-N-acetyl-glucosamine [19],β-1,4mannosyl-N,N'-diacetylchitobiose [20],β-1,2-mannobiose [21,22],β-1,2-oligomannans [21] andβ-1,3-mannobiose [23]. Their large diversity of specificities, the tolerance of some enzymes towards acceptors, and their ability to generate αMan1P through phosphorolysis of cheap substrates for the synthesis of various heteromannosides, makes GH130 glycoside phosphorylases attractive enzymes for the in vitro synthesis of β-mannosidic linkages, which are considered to be some of the most challenging glycosidic linkages in synthetic carbohydrate chemistry [24].…”

Section: Introductionmentioning

confidence: 99%

Analysis of the diversity of the glycoside hydrolase family 130 in mammal gut microbiomes reveals a novel mannoside-phosphorylase function

Laville

Tarquis

et al. 2020

Microbial Genomics

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Mannoside phosphorylases are involved in the intracellular metabolization of mannooligosaccharides, and are also useful enzymes for the in vitro synthesis of oligosaccharides. They are found in glycoside hydrolase family GH130. Here we report on an analysis of 6308 GH130 sequences, including 4714 from the human, bovine, porcine and murine microbiomes. Using sequence similarity networks, we divided the diversity of sequences into 15 mostly isofunctional meta-nodes; of these, 9 contained no experimentally characterized member. By examining the multiple sequence alignments in each meta-node, we predicted the determinants of the phosphorolytic mechanism and linkage specificity. We thus hypothesized that eight uncharacterized meta-nodes would be phosphorylases. These sequences are characterized by the absence of signal peptides and of the catalytic base. Those sequences with the conserved E/K, E/R and Y/R pairs of residues involved in substrate binding would target β-1,2-, β-1,3- and β-1,4-linked mannosyl residues, respectively. These predictions were tested by characterizing members of three of the uncharacterized meta-nodes from gut bacteria. We discovered the first known β-1,4-mannosyl-glucuronic acid phosphorylase, which targets a motif of the Shigella lipopolysaccharide O-antigen. This work uncovers a reliable strategy for the discovery of novel mannoside-phosphorylases, reveals possible interactions between gut bacteria, and identifies a biotechnological tool for the synthesis of antigenic oligosaccharides.

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Structural and Biochemical Basis for Mannan Utilization by Caldanaerobius polysaccharolyticus Strain ATCC BAA-17

Cited by 13 publications

References 39 publications

Deciphering the signaling mechanisms of the plant cell wall degradation machinery in Aspergillus oryzae

Deciphering the signaling mechanisms of the plant cell wall degradation machinery in Aspergillus oryzae

Mannoside recognition and degradation by bacteria

Analysis of the diversity of the glycoside hydrolase family 130 in mammal gut microbiomes reveals a novel mannoside-phosphorylase function

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