Plant cell wall degrading enzymes of Septoria nodorum

Lehtinen, Ulla

doi:10.1006/pmpp.1993.1045

Cited by 47 publications

(40 citation statements)

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“…in minimal medium supplemented with 1 % (w/v) carbon sources as required. Wheat cell-wall material, used as a potential inducer of CWDE gene expression, was prepared from leaves of CDC Teal by the method described by Lehtinen (1993).…”

Section: Methodsmentioning

confidence: 99%

A secreted lipase encoded by LIP1 is necessary for efficient use of saturated triglyceride lipids in Fusarium graminearum

et al. 2005

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A triglyceride lipase gene LIP1 was identified in the genome of Fusarium graminearum strain PH-1. The predicted protein encoded by LIP1 contains 591 amino acid residues with a putative N-terminal signal peptide and shows 57 and 40-44 % identity to a Botrytis cinerea lipase and five Candida rugosa lipases, respectively. Yeast cells overexpressing LIP1 showed lipolytic activity against a broad range of triglyceride substrates. Northern blot analyses revealed that expression of LIP1 was activated in planta during the fungal infection process. LIP1 expression was strongly induced in minimal medium supplemented with wheatgerm oil, but only weakly induced by olive oil and triolein. In contrast, supplementation with other carbon sources, including glucose, sucrose, apple pectin and wheat cell-wall material, did not induce LIP1 expression. Saturated fatty acids were the strongest inducers for LIP1 expression and this induction was suppressed proportionally by the presence of the unsaturated fatty acid. To determine the potential function of LIP1, gene replacement was conducted on strain PH-1. When compared with wild-type PH-1, DLIP1 mutants showed greatly reduced lipolytic activities at the early stage of incubation on minimal medium supplemented with either saturated or unsaturated lipid as the substrate, indicating that LIP1 encodes a secreted lipase for exogenous lipid hydrolysis. Moreover, the DLIP1 mutants exhibited growth deficiency on both liquid and solid minimal media supplemented with the saturated triglyceride tristearin as the sole carbon source, suggesting that LIP1 is required for utilization of this substance. Despite these differences, no variation in disease symptoms between the DLIP1 mutants and the wild-type strain was observed on susceptible cereal hosts.

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Section: Methodsmentioning

confidence: 99%

A secreted lipase encoded by LIP1 is necessary for efficient use of saturated triglyceride lipids in Fusarium graminearum

et al. 2005

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“…It is generally acknowledged that many plant-pathogenic fungi can produce a variety of CWDEs that are involved in plant pathogenesis (Lalaoui et al, 2000;Lehtinen, 1993). These enzymes are particularly important for so-called 'rot' pathogens when attacking their hosts by breaking down host tissue (Lehtinen, 1993).…”

Section: Impact Of Fsr1 On Selected Cwdes In F Verticillioidesmentioning

confidence: 99%

“…These enzymes are particularly important for so-called 'rot' pathogens when attacking their hosts by breaking down host tissue (Lehtinen, 1993). Consequently, we examined whether mutations in FSR1 affect the expression of genes that encode CWDEs in F. verticillioides.…”

Section: Impact Of Fsr1 On Selected Cwdes In F Verticillioidesmentioning

confidence: 99%

The coiled-coil protein-binding motif in Fusarium verticillioides Fsr1 is essential for maize stalk rot virulence

Yamamura

Shim

2008

Microbiology

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Fusarium verticillioides (Sacc.) Nirenberg (teleomorph Gibberella moniliformis Wineland) is one of the key pathogens of maize stalk rot disease. However, a clear understanding of stalk rot pathogenesis is still lacking. Previously, we identified the F. verticillioides FSR1 gene, which plays a key role in fungal virulence and sexual mating. The predicted Fsr1 protein contains multiple protein-binding domains, namely a caveolin-binding domain, a coiled-coil structure, and a calmodulin-binding motif at the N terminus and a WD40 repeat domain at the C terminus. Fsr1 shares significant similarity to a family of striatin proteins that play a critical role in cellular mechanisms that regulate a variety of developmental processes. Significantly, FSR1 function is conserved in Fusarium graminearum, where it also plays a direct role in pathogenesis. In this study, our goal was to determine the motif(s) in Fsr1 that are directly associated with fungal virulence. We complemented the FSR1 knockout (Dfsr1) strain with mutated versions of the FSR1 gene, and determined that the Fsr1 C-terminal WD40 repeat domain is dispensable for vegetative growth and maize stalk rot virulence. We also examined the potential link between FSR1-mediated virulence and cell wall-degrading enzyme (a-amylase, pectinase and cellulase) activities. Further characterization of the N-terminal region revealed that the coiled-coil structure is essential for virulence in F. verticillioides. The coiled-coil domain is involved in a variety of protein-protein interactions in eukaryotic systems, and thus we hypothesize that the interaction between Fsr1 and the putative Fsr1-binding protein triggers downstream gene signalling that is associated with F. verticillioides virulence.

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“…For instance, bacterial strains of Erwinia chrysanthemi that infect maize have been found to secrete more endoxylanase activity than strains that infect only dicotyledonous plants (Braun and Rodrigues 1993). Similarly, fungal pathogens, such as Septoria nodorum, that infect graminaceous monocotyledons have been reported to secrete more xylan-degrading enzymes than pectinases (Cooper et al 1988;Lehtinen 1993). Fusarium-infected barley has also been found to contain considerable amounts of endoxylanase (Schwarz et al 2002).…”

Section: Resultsmentioning

confidence: 96%

Hydrolysis of fungal and plant cell walls by enzymatic complexes from cultures of Fusarium isolates with different aggressiveness to rye (Secale cereale)

Jaroszuk-Ściseł

Kurek

2012

Arch Microbiol

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The efficiency of hydrolysis of fungal (Fusarium spp.) cell wall and rye root cell wall by crude enzymatic complexes from (42-day-old) cultures of three F. culmorum isolates, a plant growth-promoting rhizosphere isolate (PGPF) DEMFc2, a deleterious rhizosphere isolate (DRMO) DEMFc5, and a pathogenic isolate DEMFc37, as well as two other, pathogenic isolates belonging to F. oxysporum and F. graminearum species was studied. In the enzymatic complexes originating from the Fusarium spp. cultures, the activities of the following cell wall-degrading enzymes were identified: glucanases, chitinases, xylanases, endocellulases, exocellulases, pectinases, and polygalacturonases. The preparation originating from a culture of the PGPF isolate was the least efficient in plant cell wall (PCW) hydrolysis. There were no significant differences in the efficiency of PCW hydrolysis between preparations from cultures of the DRMO and the pathogenic isolates. PGPF was the most efficient in liberating reducing sugars and N-acetylglucosamine (GlcNAc) from fungal cell walls (FCW). Xylanase activities of the enzymatic complexes were strongly positively (R > +0.9) correlated with their efficiency in hydrolyzing PCW, whereas chitinase activities were correlated with the efficiency in FCW hydrolysis.

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Plant cell wall degrading enzymes of Septoria nodorum

Cited by 47 publications

References 0 publications

A secreted lipase encoded by LIP1 is necessary for efficient use of saturated triglyceride lipids in Fusarium graminearum

A secreted lipase encoded by LIP1 is necessary for efficient use of saturated triglyceride lipids in Fusarium graminearum

The coiled-coil protein-binding motif in Fusarium verticillioides Fsr1 is essential for maize stalk rot virulence

Hydrolysis of fungal and plant cell walls by enzymatic complexes from cultures of Fusarium isolates with different aggressiveness to rye (Secale cereale)

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