scholarly journals Two Distinct α-l-Arabinofuranosidases in Caldicellulosiruptor Species Drive Degradation of Arabinose-Based Polysaccharides

2017 ◽  
Vol 83 (13) ◽  
Author(s):  
Mohammad Abu Saleh ◽  
Wen-Jie Han ◽  
Ming Lu ◽  
Bing Wang ◽  
Huayue Li ◽  
...  
Keyword(s):  
Chemical Structure ◽  
Plant Biomass ◽  
Glycoside Hydrolases ◽  
Biomass Degradation ◽  
Content Type ◽  
Complex Chemical ◽  
Key Factor ◽  
Fuels And Chemicals ◽  
Hydrolysis Of ◽  
Hydrolysis Activity

ABSTRACT Species in the extremely thermophilic genus Caldicellulosiruptor can degrade unpretreated plant biomass through the action of multimodular glycoside hydrolases. To date, most focus with these bacteria has been on hydrolysis of glucans and xylans, while the biodegradation mechanism for arabinose-based polysaccharides remains unclear. Here, putative α-l-arabinofuranosidases (AbFs) were identified in Caldicellulosiruptor species by homology to less-thermophilic versions of these enzymes. From this screen, an extracellular XynF was determined to be a key factor in hydrolyzing α-1,2-, α-1,3-, and α-1,5-l-arabinofuranosyl residues of arabinose-based polysaccharides. Combined with a GH11 xylanase (XynA), XynF increased arabinoxylan hydrolysis more than 6-fold compared to the level seen with XynA alone, likely the result of XynF removing arabinofuranosyl side chains to generate linear xylans that were readily degraded. A second AbF, the intracellular AbF51, preferentially cleaved the α-1,5-l-arabinofuranosyl glycoside bonds within sugar beet arabinan. β-Xylosidases, such as GH39 Xyl39B, facilitated the hydrolysis of arabinofuranosyl residues at the nonreducing terminus of the arabinose-branched xylo-oligosaccharides by AbF51. These results demonstrate the separate but complementary contributions of extracellular XynF and cytosolic AbF51 in processing the bioconversion of arabinose-containing oligosaccharides to fermentable monosaccharides. IMPORTANCE Degradation of hemicellulose, due to its complex chemical structure, presents a major challenge during bioconversion of lignocellulosic biomass to biobased fuels and chemicals. Degradation of arabinose-containing polysaccharides, in particular, can be a key bottleneck in this process. Among Caldicellulosiruptor species, the multimodular arabinofuranosidase XynF is present in only selected members of this genus. This enzyme exhibited high hydrolysis activity, broad specificity, and strong synergism with other hemicellulases acting on arabino-polysaccharides. An intracellular arabinofuranosidase, AbF51, occurs in all Caldicellulosiruptor species and, in conjunction with xylosidases, processes the bioconversion of arabinose-branched oligosaccharides to fermentable monosaccharides. Taken together, the data suggest that plant biomass degradation in Caldicellulosiruptor species involves extracellular XynF that acts synergistically with other hemicellulases to digest arabino-polysaccharides that are subsequently transported and degraded further by intracellular AbF51 to produce short-chain arabino sugars.

scholarly journals Functional Analysis of the Glucan Degradation Locus in Caldicellulosiruptor bescii Reveals Essential Roles of Component Glycoside Hydrolases in Plant Biomass Deconstruction

2017 ◽  
Vol 83 (24) ◽  
Author(s):  
Jonathan M. Conway ◽  
Bennett S. McKinley ◽  
Nathaniel L. Seals ◽  
Diana Hernandez ◽  
Piyum A. Khatibi ◽  
...  
Keyword(s):  
Microcrystalline Cellulose ◽  
Plant Biomass ◽  
Glycoside Hydrolases ◽  
Biomass Degradation ◽  
Content Type ◽  
Plant Biomass Degradation ◽  
Caldicellulosiruptor Bescii ◽  
Mutant Strains ◽  
Fuels And Chemicals

ABSTRACT The ability to hydrolyze microcrystalline cellulose is an uncommon feature in the microbial world, but it can be exploited for conversion of lignocellulosic feedstocks into biobased fuels and chemicals. Understanding the physiological and biochemical mechanisms by which microorganisms deconstruct cellulosic material is key to achieving this objective. The glucan degradation locus (GDL) in the genomes of extremely thermophilic Caldicellulosiruptor species encodes polysaccharide lyases (PLs), unique cellulose binding proteins (tāpirins), and putative posttranslational modifying enzymes, in addition to multidomain, multifunctional glycoside hydrolases (GHs), thereby representing an alternative paradigm for plant biomass degradation compared to fungal or cellulosomal systems. To examine the individual and collective in vivo roles of the glycolytic enzymes, the six GH genes in the GDL of Caldicellulosiruptor bescii were systematically deleted, and the extents to which the resulting mutant strains could solubilize microcrystalline cellulose (Avicel) and plant biomass (switchgrass or poplar) were examined. Three of the GDL enzymes, Athe_1867 (CelA) (GH9-CBM3-CBM3-CBM3-GH48), Athe_1859 (GH5-CBM3-CBM3-GH44), and Athe_1857 (GH10-CBM3-CBM3-GH48), acted synergistically in vivo and accounted for 92% of naked microcrystalline cellulose (Avicel) degradation. However, the relative importance of the GDL GHs varied for the plant biomass substrates tested. Furthermore, mixed cultures of mutant strains showed that switchgrass solubilization depended on the secretome-bound enzymes collectively produced by the culture, not on the specific strain from which they came. These results demonstrate that certain GDL GHs are primarily responsible for the degradation of microcrystalline cellulose-containing substrates by C. bescii and provide new insights into the workings of a novel microbial mechanism for lignocellulose utilization. IMPORTANCE The efficient and extensive degradation of complex polysaccharides in lignocellulosic biomass, particularly microcrystalline cellulose, remains a major barrier to its use as a renewable feedstock for the production of fuels and chemicals. Extremely thermophilic bacteria from the genus Caldicellulosiruptor rapidly degrade plant biomass to fermentable sugars at temperatures of 70 to 78°C, although the specific mechanism by which this occurs is not clear. Previous comparative genomic studies identified a genomic locus found only in certain Caldicellulosiruptor species that was hypothesized to be mainly responsible for microcrystalline cellulose degradation. By systematically deleting genes in this locus in Caldicellulosiruptor bescii, the nuanced, substrate-specific in vivo roles of glycolytic enzymes in deconstructing crystalline cellulose and plant biomasses could be discerned. The results here point to synergism of three multidomain cellulases in C. bescii, working in conjunction with the aggregate secreted enzyme inventory, as the key to the plant biomass degradation ability of this extreme thermophile.

scholarly journals Transcriptional Regulation of Plant Biomass Degradation and Carbohydrate Utilization Genes in the Extreme Thermophile Caldicellulosiruptor bescii

mSystems ◽  
2021 ◽  
Author(s):  
Dmitry A. Rodionov ◽  
Irina A. Rodionova ◽  
Vladimir A. Rodionov ◽  
Aleksandr A. Arzamasov ◽  
Ke Zhang ◽  
...  
Keyword(s):  
Metabolic Engineering ◽  
Plant Biomass ◽  
Biomass Degradation ◽  
Extreme Thermophile ◽  
Comprehensive Understanding ◽  
Carbohydrate Utilization ◽  
Content Type ◽  
Metabolic Characteristics ◽  
Caldicellulosiruptor Bescii ◽  
Fuels And Chemicals

To develop functional metabolic engineering platforms for nonmodel microorganisms, a comprehensive understanding of the physiological and metabolic characteristics is critical. Caldicellulosiruptor bescii and other species in this genus have untapped potential for conversion of unpretreated plant biomass into industrial fuels and chemicals. The highly interactive and complex machinery used by C. bescii to acquire and process complex carbohydrates contained in lignocellulose was elucidated here to complement related efforts to develop a metabolic engineering platform with this bacterium.

scholarly journals Efficient Plant Biomass Degradation by Thermophilic Fungus Myceliophthora heterothallica

2012 ◽  
Vol 79 (4) ◽  
pp. 1316-1324 ◽  
Author(s):  
Joost van den Brink ◽  
Gonny C. J. van Muiswinkel ◽  
Bart Theelen ◽  
Sandra W. A. Hinz ◽  
Ronald P. de Vries
Keyword(s):  
Wheat Straw ◽  
Plant Biomass ◽  
Hydrolytic Enzymes ◽  
Reaction Times ◽  
Giant Reed ◽  
Thermophilic Fungi ◽  
Biomass Degradation ◽  
Thermostable Enzymes ◽  
Content Type

ABSTRACTRapid and efficient enzymatic degradation of plant biomass into fermentable sugars is a major challenge for the sustainable production of biochemicals and biofuels. Enzymes that are more thermostable (up to 70°C) use shorter reaction times for the complete saccharification of plant polysaccharides compared to hydrolytic enzymes of mesophilic fungi such asTrichodermaandAspergillusspecies. The genusMyceliophthoracontains four thermophilic fungi producing industrially relevant thermostable enzymes. Within this genus, isolates belonging toM. heterothallicawere recently separated from the well-described speciesM. thermophila. We evaluate here the potential ofM. heterothallicaisolates to produce efficient enzyme mixtures for biomass degradation. Compared to the other thermophilicMyceliophthoraspecies, isolates belonging toM. heterothallicaandM. thermophilagrew faster on pretreated spruce, wheat straw, and giant reed. According to their protein profiles andin vitroassays after growth on wheat straw, (hemi-)cellulolytic activities differed strongly betweenM. thermophilaandM. heterothallicaisolates. Compared toM. thermophila,M. heterothallicaisolates were better in releasing sugars from mildly pretreated wheat straw (with 5% HCl) with a high content of xylan. The high levels of residual xylobiose revealed that enzyme mixtures ofMyceliophthoraspecies lack sufficient β-xylosidase activity. Sexual crossing of twoM. heterothallicashowed that progenies had a large genetic and physiological diversity. In the future, this will allow further improvement of the plant biomass-degrading enzyme mixtures ofM. heterothallica.

scholarly journals A Novel Cys2His2 Zinc Finger Homolog of AZF1 Modulates Holocellulase Expression in Trichoderma reesei

mSystems ◽  
2019 ◽  
Vol 4 (4) ◽  
Author(s):  
Amanda Cristina Campos Antonieto ◽  
Karoline Maria Vieira Nogueira ◽  
Renato Graciano de Paula ◽  
Luísa Czamanski Nora ◽  
Murilo Henrique Anzolini Cassiano ◽  
...  
Keyword(s):  
Trichoderma Reesei ◽  
Filamentous Fungi ◽  
Plant Cell Wall ◽  
Plant Biomass ◽  
Regulatory Elements ◽  
Biomass Degradation ◽  
Control Of Gene Expression ◽  
Content Type ◽  
Encoding Genes

ABSTRACT Filamentous fungi are remarkable producers of enzymes dedicated to the degradation of sugar polymers found in the plant cell wall. Here, we integrated transcriptomic data to identify novel transcription factors (TFs) related to the control of gene expression of lignocellulosic hydrolases in Trichoderma reesei and Aspergillus nidulans. Using various sets of differentially expressed genes, we identified some putative cis-regulatory elements that were related to known binding sites for Saccharomyces cerevisiae TFs. Comparative genomics allowed the identification of six transcriptional factors in filamentous fungi that have corresponding S. cerevisiae homologs. Additionally, a knockout strain of T. reesei lacking one of these TFs (S. cerevisiae AZF1 homolog) displayed strong reductions in the levels of expression of several cellulase-encoding genes in response to both Avicel and sugarcane bagasse, revealing a new player in the complex regulatory network operating in filamentous fungi during plant biomass degradation. Finally, RNA sequencing (RNA-seq) analysis showed the scope of the AZF1 homologue in regulating a number of processes in T. reesei, and chromatin immunoprecipitation-quantitative PCR (ChIP-qPCR) provided evidence for the direct interaction of this TF in the promoter regions of cel7a, cel45a, and swo. Therefore, we identified here a novel TF which plays a positive effect in the expression of cellulase-encoding genes in T. reesei. IMPORTANCE In this work, we used a systems biology approach to map new regulatory interactions in Trichoderma reesei controlling the expression of genes encoding cellulase and hemicellulase. By integrating transcriptomics related to complex biomass degradation, we were able to identify a novel transcriptional regulator which is able to activate the expression of these genes in response to two different cellulose sources. In vivo experimental validation confirmed the role of this new regulator in several other processes related to carbon source utilization and nutrient transport. Therefore, this work revealed novel forms of regulatory interaction in this model system for plant biomass deconstruction and also represented a new approach that could be easy applied to other organisms.

scholarly journals Genus-Wide Assessment of Lignocellulose Utilization in the Extremely Thermophilic GenusCaldicellulosiruptorby Genomic, Pangenomic, and Metagenomic Analyses

2018 ◽  
Vol 84 (9) ◽  
Author(s):  
Laura L. Lee ◽  
Sara E. Blumer-Schuette ◽  
Javier A. Izquierdo ◽  
Jeffrey V. Zurawski ◽  
Andrew J. Loder ◽  
...  
Keyword(s):  
Microcrystalline Cellulose ◽  
Plant Biomass ◽  
Thermophilic Bacteria ◽  
Cellulose Degradation ◽  
Glycoside Hydrolases ◽  
Metagenomic Data ◽  
Lignocellulose Degradation ◽  
Sequence Information ◽  
Metagenomic Sequence ◽  
Content Type

ABSTRACTMetagenomic data from Obsidian Pool (Yellowstone National Park, USA) and 13 genome sequences were used to reassess genus-wide biodiversity for the extremely thermophilicCaldicellulosiruptor. The updated core genome contains 1,401 ortholog groups (average genome size for 13 species = 2,516 genes). The pangenome, which remains open with a revised total of 3,493 ortholog groups, encodes a variety of multidomain glycoside hydrolases (GHs). These include three cellulases with GH48 domains that are colocated in the glucan degradation locus (GDL) and are specific determinants for microcrystalline cellulose utilization. Three recently sequenced species,Caldicellulosiruptorsp. strain Rt8.B8 (renamed hereCaldicellulosiruptor morganii),Thermoanaerobacter cellulolyticusstrain NA10 (renamed hereCaldicellulosiruptor naganoensis), andCaldicellulosiruptorsp. strain Wai35.B1 (renamed hereCaldicellulosiruptor danielii), degraded Avicel and lignocellulose (switchgrass).C. morganiiwas more efficient thanCaldicellulosiruptor besciiin this regard and differed from the other 12 species examined, both based on genome content and organization and in the specific domain features of conserved GHs. Metagenomic analysis of lignocellulose-enriched samples from Obsidian Pool revealed limited new information on genus biodiversity. Enrichments yielded genomic signatures closely related to that ofCaldicellulosiruptor obsidiansis, but there was also evidence for other thermophilic fermentative anaerobes (Caldanaerobacter,Fervidobacterium,Caloramator, andClostridium). One enrichment, containing 89.8%Caldicellulosiruptorand 9.7%Caloramator, had a capacity for switchgrass solubilization comparable to that ofC. bescii. These results refine the known biodiversity ofCaldicellulosiruptorand indicate that microcrystalline cellulose degradation at temperatures above 70°C, based on current information, is limited to certain members of this genus that produce GH48 domain-containing enzymes.IMPORTANCEThe genusCaldicellulosiruptorcontains the most thermophilic bacteria capable of lignocellulose deconstruction, which are promising candidates for consolidated bioprocessing for the production of biofuels and bio-based chemicals. The focus here is on the extant capability of this genus for plant biomass degradation and the extent to which this can be inferred from the core and pangenomes, based on analysis of 13 species and metagenomic sequence information from environmental samples. Key to microcrystalline hydrolysis is the content of the glucan degradation locus (GDL), a set of genes encoding glycoside hydrolases (GHs), several of which have GH48 and family 3 carbohydrate binding module domains, that function as primary cellulases. Resolving the relationship between the GDL and lignocellulose degradation will inform efforts to identify more prolific members of the genus and to develop metabolic engineering strategies to improve this characteristic.

scholarly journals Microbial Glucuronoyl Esterases: 10 Years after Discovery

2016 ◽  
Vol 82 (24) ◽  
pp. 7014-7018 ◽  
Author(s):  
Peter Biely
Keyword(s):  
Plant Biomass ◽  
Current Knowledge ◽  
Schizophyllum Commune ◽  
Enzymatic Saccharification ◽  
Artificial Substrates ◽  
Content Type ◽  
New Family ◽  
Biomass Processing ◽  
Hydrolysis Of ◽  
Positive Effect

ABSTRACTA carbohydrate esterase called glucuronoyl esterase (GE) was discovered 10 years ago in a cellulolytic system of the wood-rotting fungusSchizophyllum commune. Genes coding for GEs were subsequently found in a number of microbial genomes, and a new family of carbohydrate esterases (CE15) has been established. The multidomain structures of GEs, together with their catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass, led to the view that the esterases evolved for hydrolysis of the ester linkages between 4-O-methyl-d-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. This idea of the function of GEs is further supported by the effects of cloning of fungal GEs in plants and by very recently reported evidence for changes in the size of isolated lignin-carbohydrate complexes due to uronic acid de-esterification. These facts make GEs interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants. This article is a brief summary of current knowledge of these relatively recent and unexplored esterases.

scholarly journals Two SusD-Like Proteins Encoded within a Polysaccharide Utilization Locus of an Uncultured Ruminant Bacteroidetes Phylotype Bind Strongly to Cellulose

2012 ◽  
Vol 78 (16) ◽  
pp. 5935-5937 ◽  
Author(s):  
A. K. Mackenzie ◽  
P. B. Pope ◽  
H. L. Pedersen ◽  
R. Gupta ◽  
M. Morrison ◽  
...  
Keyword(s):  
Cell Walls ◽  
Plant Biomass ◽  
Primary Cell ◽  
Biomass Degradation ◽  
Content Type ◽  
Plant Biomass Degradation ◽  
Polysaccharide Utilization Locus ◽  
Plant Primary Cell Walls

ABSTRACTWe demonstrate that two characteristic Sus-like proteins encoded within a polysaccharide utilization locus (PUL) bind strongly to cellulosic substrates and interact with plant primary cell walls. This shows associations between unculturedBacteroidetes-affiliated lineages and cellulose in the rumen and thus presents new PUL-derived targets to pursue regarding plant biomass degradation.

scholarly journals Investigating the Function of an Arabinan Utilization Locus Isolated from a Termite Gut Community

2014 ◽  
Vol 81 (1) ◽  
pp. 31-39 ◽  
Author(s):  
Grégory Arnal ◽  
Géraldine Bastien ◽  
Nelly Monties ◽  
Anne Abot ◽  
Véronique Anton Leberre ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Plant Biomass ◽  
Bioinformatic Analysis ◽  
Open Reading Frames ◽  
Glycoside Hydrolases ◽  
Functional Screening ◽  
Content Type ◽  
Termite Gut ◽  
Pentose Sugar

ABSTRACTBiocatalysts are essential for the development of bioprocesses efficient for plant biomass degradation. Previously, a metagenomic clone containing DNA from termite gut microbiota was pinpointed in a functional screening that revealed the presence of arabinofuranosidase activity. Subsequent genetic and bioinformatic analysis revealed that the DNA fragment belonged to a member of the genusBacteroidesand encoded 19 open reading frames (ORFs), and annotation suggested the presence of hypothetical transporter and regulator proteins and others involved in the catabolism of pentose sugar. In this respect and considering the phenotype of the metagenomic clone, it was noted that among the ORFs, there are four putative arabinose-specific glycoside hydrolases, two from family GH43 and two from GH51. In this study, a thorough bioinformatics analysis of the metagenomic clone gene cluster has been performed and the four aforementioned glycoside hydrolases have been characterized. Together, the results provide evidence that the gene cluster is a polysaccharide utilization locus dedicated to the breakdown of the arabinan component in pectin and related substrates. Characterization of the two GH43 and the two GH51 glycoside hydrolases has revealed that each of these enzymes displays specific catalytic capabilities and that when these are combined the enzymes act synergistically, increasing the efficiency of arabinan degradation.

scholarly journals Comparative Analysis of Extremely Thermophilic Caldicellulosiruptor Species Reveals Common and Unique Cellular Strategies for Plant Biomass Utilization

2015 ◽  
Vol 81 (20) ◽  
pp. 7159-7170 ◽  
Author(s):  
Jeffrey V. Zurawski ◽  
Jonathan M. Conway ◽  
Laura L. Lee ◽  
Hunter J. Simpson ◽  
Javier A. Izquierdo ◽  
...  
Keyword(s):  
Panicum Virgatum ◽  
Plant Biomass ◽  
Thermal Control ◽  
Glycoside Hydrolases ◽  
Crystalline Cellulose ◽  
Content Type ◽  
Genes Encoding ◽  
Conserved Genes ◽  
Flagellum Biosynthesis ◽  
Chemotaxis System

ABSTRACTMicrobiological, genomic and transcriptomic analyses were used to examine three species from the bacterial genusCaldicellulosiruptorwith respect to their capacity to convert the carbohydrate content of lignocellulosic biomass at 70°C to simple sugars, acetate, lactate, CO2, and H2.Caldicellulosiruptor bescii,C. kronotskyensis, andC. saccharolyticussolubilized 38%, 36%, and 29% (by weight) of unpretreated switchgrass (Panicum virgatum) (5 g/liter), respectively, which was about half of the amount of crystalline cellulose (Avicel; 5 g/liter) that was solubilized under the same conditions. The lower yields withC. saccharolyticus, not appreciably greater than the thermal control for switchgrass, were unexpected, given that its genome encodes the same glycoside hydrolase 9 (GH9)-GH48 multidomain cellulase (CelA) found in the other two species. However, the genome ofC. saccharolyticuslacks two other cellulases with GH48 domains, which could be responsible for its lower levels of solubilization. Transcriptomes for growth of each species comparing cellulose to switchgrass showed that many carbohydrate ABC transporters and multidomain extracellular glycoside hydrolases were differentially regulated, reflecting the heterogeneity of lignocellulose. However, significant differences in transcription levels for conserved genes among the three species were noted, indicating unexpectedly diverse regulatory strategies for deconstruction for these closely related bacteria. Genes encoding the Che-type chemotaxis system and flagellum biosynthesis were upregulated inC. kronotskyensisandC. besciiduring growth on cellulose, implicating motility in substrate utilization. The results here show that capacity for plant biomass deconstruction varies acrossCaldicellulosiruptorspecies and depends in a complex way on GH genome inventory, substrate composition, and gene regulation.

scholarly journals Leucoagaricus gongylophorus Produces Diverse Enzymes for the Degradation of Recalcitrant Plant Polymers in Leaf-Cutter Ant Fungus Gardens

2013 ◽  
Vol 79 (12) ◽  
pp. 3770-3778 ◽  
Author(s):  
Frank O. Aylward ◽  
Kristin E. Burnum-Johnson ◽  
Susannah G. Tringe ◽  
Clotilde Teiling ◽  
Daniel M. Tremmel ◽  
...  
Keyword(s):  
Plant Biomass ◽  
Draft Genome ◽  
Lignocellulose Degradation ◽  
Biomass Degradation ◽  
Large Reservoir ◽  
Content Type ◽  
Plant Biomass Degradation ◽  
Basidiomycetous Fungus ◽  
Leucoagaricus Gongylophorus ◽  
Ant Fungus

ABSTRACTPlants represent a large reservoir of organic carbon comprised primarily of recalcitrant polymers that most metazoans are unable to deconstruct. Many herbivores gain access to nutrients in this material indirectly by associating with microbial symbionts, and leaf-cutter ants are a paradigmatic example. These ants use fresh foliar biomass as manure to cultivate gardens composed primarily ofLeucoagaricus gongylophorus, a basidiomycetous fungus that produces specialized hyphal swellings that serve as a food source for the host ant colony. Although leaf-cutter ants are conspicuous herbivores that contribute substantially to carbon turnover in Neotropical ecosystems, the process through which plant biomass is degraded in their fungus gardens is not well understood. Here we present the first draft genome ofL. gongylophorus, and, using genomic and metaproteomic tools, we investigate its role in lignocellulose degradation in the gardens of bothAtta cephalotesandAcromyrmex echinatiorleaf-cutter ants. We show thatL. gongylophorusproduces a diversity of lignocellulases in ant gardens and is likely the primary driver of plant biomass degradation in these ecosystems. We also show that this fungus produces distinct sets of lignocellulases throughout the different stages of biomass degradation, including numerous cellulases and laccases that likely play an important role in lignocellulose degradation. Our study provides a detailed analysis of plant biomass degradation in leaf-cutter ant fungus gardens and insight into the enzymes underlying the symbiosis between these dominant herbivores and their obligate fungal cultivar.

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