scholarly journals Feruloyl Esterase Fae1 is Required Specifically for Host Colonisation by The Rice-Blast Fungus Magnaporthe Oryzae

2021 ◽  
Author(s):  
Akhil Thaker ◽  
Khyati Mehta ◽  
Rajesh Patkar
Keyword(s):  
Cell Wall ◽  
Ferulic Acid ◽  
Plant Cell ◽  
Magnaporthe Oryzae ◽  
Plant Cell Wall ◽  
Biofuel Production ◽  
Feruloyl Esterase ◽  
Potential Candidate ◽  
Blast Fungus ◽  
Host Invasion

Abstract Plant cell wall acts as a primary barrier for microbial pathogens during infection. A cell wall degrading enzyme thus may be a crucial virulence factor, as it may aid the pathogen in successful host invasion. Nine genes coding for feruloyl esterases (Fae), likely involved in plant cell wall degradation, have been annotated in the genome of the cereal-blast fungus Magnaporthe oryzae . However, role of any Fae in pathogenicity of M. oryzae remains hitherto under explored. Here, we identified FAE1 gene (MGG_08737) that was significantly upregulated during host penetration and subsequent colonisation stages of infection. Accordingly, while deletion of FAE1 in M. oryzae did not affect the vegetative growth and asexual development, the fae1Δ mutant showed significantly reduced pathogenesis on rice plants, mainly due to impaired host invasion and colonisation. Very few (<10%) fae1Δ appressoria that formed the primary invasive hyphae, failed to elaborate from the first invaded cell to the neighboring plant cells. Interestingly, exogenously added glucose, as a simple carbon source, or ferulic acid, a product of the Fae activity, significantly supported the invasive growth of the fae1Δ mutant. We show that the Fae1-based feruloyl esterase activity, by targeting the plant cell wall, plays an important role in accumulating ferulic acid and/or sugar molecules, as a likely energy source, to enable host invasion and colonisation by M. oryzae. Given its role in plant cell wall digestion and host colonisation, M. oryzae Fae1 could be a potential candidate for a novel antifungal strategy and a biotechnological application in biofuel production.

Hydroxycinnamic acids and ferulic acid esterase in relation to biodegradation of complex plant cell walls

2005 ◽  
Vol 85 (3) ◽  
pp. 255-267 ◽  
Author(s):  
P. Yu ◽  
J. J. McKinnon ◽  
D. A. Christensen
Keyword(s):  
Cell Wall ◽  
Ferulic Acid ◽  
Plant Cell ◽  
Cell Walls ◽  
Plant Cell Wall ◽  
Structural Characteristics ◽  
Hydroxycinnamic Acid ◽  
Feruloyl Esterase ◽  
Plant Cell Walls ◽  
Ferulic Acid Esterase

Ferulic acid (3-methoxy-4-hydroxycinnamic acid), present in complex plant cell walls, is covalently cross-linked to polysaccharides by ester bonds and to components of lignin mainly by ether bonds. Ferulic acid has also been shown to occur in dimer- and trimerized forms through oxidative coupling between esterified and/or etherified ferulic acid residues. These cross-links are among the factors most inhibitory to digestion of complex plant cell walls in ruminants. Recently obtained information on ferulic acid and ferulic acid esterases in relation to complex plant cell wall biodegradation is reviewed. A focus of the review is on structural characteristics of plant cell walls associated with ferulic acid, physicochemical properties of ferulic acid esterase and synergistic interaction between ferulic acid esterase and other accessary cell wall degrading enzymes on the release of ferulic acid and plant cell wall biodegradation. Key words: Ferulic acid, hydroxycinnamic acid, feruloyl esterase, interaction effects, polysaccharide, feruloyl-polysaccharides, plant cell walls, biodegradation

Solubilisation of Ferulic Acid from Plant Cell Wall Materials in a Model Human Gut System

1996 ◽  
Vol 24 (3) ◽  
pp. 384S-384S ◽  
Author(s):  
PAUL A KROON ◽  
CRAIG B FAULDS ◽  
PETER RYDEN ◽  
GARY WILLIAMSON
Keyword(s):  
Cell Wall ◽  
Ferulic Acid ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Human Gut ◽  
Wall Materials ◽  
Cell Wall Materials

scholarly journals Regulation of the Feruloyl Esterase (faeA) Gene from Aspergillus niger

1999 ◽  
Vol 65 (12) ◽  
pp. 5500-5503 ◽  
Author(s):  
Ronald P. de Vries ◽  
Jaap Visser
Keyword(s):  
Cell Wall ◽  
Aspergillus Niger ◽  
Ferulic Acid ◽  
Methoxy Group ◽  
Plant Cell Wall ◽  
Ring Structure ◽  
Feruloyl Esterase ◽  
Cell Wall Polysaccharides ◽  
Aromatic Residues ◽  
Encoding Gene

ABSTRACT Feruloyl esterases can remove aromatic residues (e.g., ferulic acid) from plant cell wall polysaccharides (xylan, pectin) and are essential for complete degradation of these polysaccharides. Expression of the feruloyl esterase-encoding gene (faeA) fromAspergillus niger depends on d-xylose (expression is mediated by XlnR, the xylanolytic transcriptional activator) and on a second system that responds to aromatic compounds with a defined ring structure, such as ferulic acid and vanillic acid. Several compounds were tested, and all of the inducing compounds contained a benzene ring which had a methoxy group at C-3 and a hydroxy group at C-4 but was not substituted at C-5. Various aliphatic groups occurred at C-1. faeA expression in the presence of xylose or ferulic acid was repressed by glucose. faeA expression in the presence of ferulic acid and xylose was greater thanfaeA expression in the presence of either compound alone. The various inducing systems allow A. niger to produce feruloyl esterase not only during growth on xylan but also during growth on other ferulic acid-containing cell wall polysaccharides, such as pectin.

scholarly journals Crystal Structure and Substrate Specificity Modification of Acetyl Xylan Esterase from Aspergillus luchuensis

2017 ◽  
Vol 83 (20) ◽  
Author(s):  
Dai Komiya ◽  
Akane Hori ◽  
Takuya Ishida ◽  
Kiyohiko Igarashi ◽  
Masahiro Samejima ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Cell Wall ◽  
Substrate Specificity ◽  
Ferulic Acid ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Catalytic Triad ◽  
Acetyl Xylan Esterase ◽  
Content Type ◽  
Aspergillus Luchuensis

ABSTRACT Acetyl xylan esterase (AXE) catalyzes the hydrolysis of the acetyl bonds present in plant cell wall polysaccharides. Here, we determined the crystal structure of AXE from Aspergillus luchuensis (AlAXEA), providing the three-dimensional structure of an enzyme in the Esterase_phb family. AlAXEA shares its core α/β-hydrolase fold structure with esterases in other families, but it has an extended central β-sheet at both its ends and an extra loop. Structural comparison with a ferulic acid esterase (FAE) from Aspergillus niger indicated that AlAXEA has a conserved catalytic machinery: a catalytic triad (Ser119, His259, and Asp202) and an oxyanion hole (Cys40 and Ser120). Near the catalytic triad of AlAXEA, two aromatic residues (Tyr39 and Trp160) form small pockets at both sides. Homology models of fungal FAEs in the same Esterase_phb family have wide pockets at the corresponding sites because they have residues with smaller side chains (Pro, Ser, and Gly). Mutants with site-directed mutations at Tyr39 showed a substrate specificity similar to that of the wild-type enzyme, whereas those with mutations at Trp160 acquired an expanded substrate specificity. Interestingly, the Trp160 mutants acquired weak but significant type B-like FAE activity. Moreover, the engineered enzymes exhibited ferulic acid-releasing activity from wheat arabinoxylan. IMPORTANCE Hemicelluloses in the plant cell wall are often decorated by acetyl and ferulic acid groups. Therefore, complete and efficient degradation of plant polysaccharides requires the enzymes for cleaving the side chains of the polymer. Since the Esterase_phb family contains a wide array of fungal FAEs and AXEs from fungi and bacteria, our study will provide a structural basis for the molecular mechanism of these industrially relevant enzymes in biopolymer degradation. The structure of the Esterase_phb family also provides information for bacterial polyhydroxyalkanoate depolymerases that are involved in biodegradation of thermoplastic polymers.

scholarly journals Expanding xylose metabolism in yeast for plant cell wall conversion to biofuels

2014 ◽  
Author(s):  
Xin Li ◽  
Vivian Y Yu ◽  
Yuping Lin ◽  
Kulika Chomvong ◽  
Raíssa Estrela ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Plant Cell ◽  
First Generation ◽  
Plant Cell Wall ◽  
Biofuel Production ◽  
Xylose Metabolism ◽  
Renewable Biomass ◽  
Generation Biofuel ◽  
Utilization Pathway

Sustainable biofuel production from renewable biomass will require the efficient and complete use of all abundant sugars in the plant cell wall. Using the cellulolytic fungusNeurospora crassaas a model, we identified a xylodextrin transport and consumption pathway required for its growth on hemicellulose. Successful reconstitution of this xylodextrin utilization pathway inSaccharomyces cerevisiaerevealed that fungal xylose reductases act as xylodextrin reductases, and together with two hydrolases, generate intracellular xylose and xylitol. Xylodextrin consumption using xylodextrin reductases and tandem intracellular hydrolases greatly expands the capacity of yeasts to use plant cell wall-derived sugars, and should be adaptable to increase the efficiency of both first-generation and next-generation biofuel production.

scholarly journals Expanding xylose metabolism in yeast for plant cell wall conversion to biofuels

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Xin Li ◽  
Vivian Yaci Yu ◽  
Yuping Lin ◽  
Kulika Chomvong ◽  
Raíssa Estrela ◽  
...  
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
First Generation ◽  
Plant Cell Wall ◽  
Biofuel Production ◽  
Xylose Metabolism ◽  
Metabolic Intermediates ◽  
Renewable Biomass ◽  
Generation Biofuel ◽  
Utilization Pathway

Sustainable biofuel production from renewable biomass will require the efficient and complete use of all abundant sugars in the plant cell wall. Using the cellulolytic fungus Neurospora crassa as a model, we identified a xylodextrin transport and consumption pathway required for its growth on hemicellulose. Reconstitution of this xylodextrin utilization pathway in Saccharomyces cerevisiae revealed that fungal xylose reductases act as xylodextrin reductases, producing xylosyl-xylitol oligomers as metabolic intermediates. These xylosyl-xylitol intermediates are generated by diverse fungi and bacteria, indicating that xylodextrin reduction is widespread in nature. Xylodextrins and xylosyl-xylitol oligomers are then hydrolyzed by two hydrolases to generate intracellular xylose and xylitol. Xylodextrin consumption using a xylodextrin transporter, xylodextrin reductases and tandem intracellular hydrolases in cofermentations with sucrose and glucose greatly expands the capacity of yeast to use plant cell wall-derived sugars and has the potential to increase the efficiency of both first-generation and next-generation biofuel production.

scholarly journals Phenolic compounds as cross-links of plant derived polysaccharides

2004 ◽  
Vol 22 (SI - Chem. Reactions in Foods V) ◽  
pp. S64-S67 ◽  
Author(s):  
M. Bunzel ◽  
J. Ralph ◽  
H. Steinhart
Keyword(s):  
Cell Wall ◽  
Phenolic Compounds ◽  
Ferulic Acid ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Sinapic Acid ◽  
Cell Wall Polysaccharides ◽  
The Past ◽  
Maize Bran ◽  
Cross Links

Plant cell wall polysaccharides are partially cross-linked via phenolic compounds. As shown in the past, the most important phenolic compounds to cross-link plant cell-wall polysaccharides are ester-linked ferulic acid dimers, but p-coumarate dimers were also shown to be potential cross-linking compounds. Recently, ferulic acid dimers were identified and quantified in a range of cereal grains. The isolation of 8-O-4-dehydrodiferulic aciddiarabinoside from maize bran shows that diferulic acids are able to form intermolecular cross-links between arabinoxylans. The more recently identified sinapic acid dehydrodimers and ferulic acid dehydrotrimers provide additional contributions to building up a strong network of plant cell wall polysaccharides.

scholarly journals Biochemical Analyses of Multiple Endoxylanases from the Rumen Bacterium Ruminococcus albus 8 and Their Synergistic Activities with Accessory Hemicellulose-Degrading Enzymes

2011 ◽  
Vol 77 (15) ◽  
pp. 5157-5169 ◽  
Author(s):  
Young Hwan Moon ◽  
Michael Iakiviak ◽  
Stefan Bauer ◽  
Roderick I. Mackie ◽  
Isaac K. O. Cann
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Biofuel Production ◽  
Rumen Bacterium ◽  
Ruminococcus Albus ◽  
Content Type ◽  
Chemical Complexity ◽  
Degrading Enzymes ◽  
Modular Architectures

ABSTRACTRuminococcus albus8 is a ruminal bacterium capable of metabolizing hemicellulose and cellulose, the major components of the plant cell wall. The enzymes that allow this bacterium to capture energy from the two polysaccharides, therefore, have potential application in plant cell wall depolymerization, a process critical to biofuel production. For this purpose, a partial genome sequence ofR. albus8 was generated. The genomic data depicted a bacterium endowed with multiple forms of plant cell wall-degrading enzymes. The endoxylanases ofR. albus8 exhibited diverse modular architectures, including incorporation of a catalytic module, a carbohydrate binding module, and a carbohydrate esterase module in a single polypeptide. The accessory enzymes of xylan degradation were a β-xylosidase, an α-l-arabinofuranosidase, and an α-glucuronidase. We hypothesized that due to the chemical complexity of the hemicellulose encountered in the rumen, the bacterium uses multiple endoxylanases, with subtle differences in substrate specificities, to attack the substrate, while the accessory enzymes hydrolyze the products to simple sugars for metabolism. To test this hypothesis, the genes encoding the predicted endoxylanases were expressed, and the proteins were biochemically characterized either alone or in combination with accessory enzymes. The different endoxylanase families exhibited different patterns of product release, with the family 11 endoxylanases releasing more products in synergy with the accessory enzymes from the more complex substrates. Aside from the insights into hemicellulose degradation byR. albus8, this report should enhance our knowledge on designing effective enzyme cocktails for release of fermentable sugars in the biofuel industry.

Sign in / Sign up

Export Citation Format

Share Document