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2 edition of Cutinase of Fusarium solani f. sp. pisi found in the catalog.

Cutinase of Fusarium solani f. sp. pisi

Charles Peter Woloshuk

Cutinase of Fusarium solani f. sp. pisi

mechanism of induction and relatedness to other Fusarium species

by Charles Peter Woloshuk

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Published .
Written in English

    Subjects:
  • Fusarium solani.

  • Edition Notes

    Statementby Charles Peter Woloshuk.
    The Physical Object
    Paginationxi, 73 leaves, bound :
    Number of Pages73
    ID Numbers
    Open LibraryOL16587436M

    @article{osti_, title = {Cutinase of Fusarium solani F. sp. pisi: mechanism of induction and relatedness to other Fusarium species}, author = {Woloshuk, C P}, abstractNote = {Three studies were made on the extracellular cutinase of the phytopathogenic fungus Fusarium solani f. sp. pisi. I. The production of cutinase was found to be induced in spores of F. solani f. sp. pisi, strain T Fusarium solani f sp pisi (Nectria haematococca) isolate with one cutinase gene produced 10 to 20% of the cutinase produced by isolate T-8 that has multiple cutinase genes, whereas cutinase gene-disrupted mutant of isolate did not produce cutinase. On the surface of pea stem seg .

    Spores of the phytopathogenic fungus Fusarium solani f. sp. pisi were shown to produce the extracellular enzyme, cutinase, only when cutin or cutin hydrolysate was added to the spore suspension. Dihydroxy-C/sub 16/ acid and trihydroxy-C/sub 18/ acid, which are unique cutin monomers, showed the greatest cutinase-inducing activity. We report here the three-dimensional structure of a recombinant cutinase from F. solani pisi, expressed in Escherichia coli9, Cutinase is an α–β protein; the active site is composed of the.

    induce cutinase, F. solani f. sp. pisi wasgrown in a medium containing % glucose as the carbon source and % chemically prepared hydrolysate ofcutin. Growthofthe fungus did not appear to be affected by the presence of cutin hydrolysate. The extracellular fluid was examined for cutinase activity using a model substrate, PNB, which is.   Fernando G, Zimmermann W, Kollatukudy PE () Suberin-grown Fusarium solani f. sp. pisi generates a cutinase-like esterase which depolymerizes the aliphatic components of suberin. Physiol Plant Pathol –


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Cutinase of Fusarium solani f. sp. pisi by Charles Peter Woloshuk Download PDF EPUB FB2

1. Introduction. Cutinase from the phytopathogenic fungus Fusarium solani pisi is an example of a small carboxylic ester hydrolase that bridges functional properties between lipases and esterases.

Cutinases are named after their ability to degrade cutin polymers, but additionally a large variety of short and long chain triacylglycerols (TAGs) are rapidly by: Fusarium venenatum A3/5 was transformed using the Aspergillus niger expression plasmid, pIGF, in which the coding sequence for the F.

solani f. pisi cutinase gene had been inserted in frame, with a KEX2 cleavage site, with the truncated A. niger glucoamylase gene under control of the A. niger glucoamylase by: 5. Fusarium solani f sp pisi (Nectria haematococca) isolate with one cutinase gene produced 10 to 20% of the cutinase produced by isolate T-8 that has multiple cutinase genes, whereas cutinase gene-disrupted mutant of isolate did not produce by: Koichi Yoneyama, Masahiro Natsume, in Comprehensive Natural Products II, Germination inducers of phytopathogens.

Flavonoids stimulate spore germination in the soilborne phytopathogenic fungus Fusarium germination of F. solani f. pisi, which causes disease in pea, is stimulated by flavanone hesperetin (), flavone apigenin (), the pterocarpan.

Cutin hydrolysate induced the production of an extracellular cutinase by glucose-grown Fusarium solani f. pisi. The rate of production depended on the amount of cutin hydrolysate added up to 80 μg/ml, and saturation was attained at this level.

Glucose was found to be a repressor of cutinase by: Induction of a biopolyester hydrolase (cutinase) by low levels of cutin monomers in Fusarium solani pisi.

J Bacteriol. Feb; (2)– [PMC free article] Martinez C, De Geus P, Lauwereys M, Matthyssens G, Cambillau C. Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent.

Nature. We compared wild-type strains and a cutinase-negative gene replacement mutant strain of Fusarium solani f. pisi (D. Stahl and W. Schäfer, Plant Cell) and a wild-type strain of Fusarium moniliforme to show that Fusarium cutinase is a PCL depolymerase.

Studies using antibodies to cutinase (Maiti and Kolattukudy ) or pectate lyase (Crawford and Kolattukudy ) suggested that cell wall degrading enzymes are important for pathogenicity of F.

solani f. pisi. Transformation of a cutinase gene from F. solani into a strain of Mycosphaerella that could infect papaya fruit only through. Cutin hydrolysate induced the production of an extracellular cutinase by glucose-grown Fusarium solani f.

pisi. The rate of production depended on the amount of cutin hydrolysate added up to 80 μg/ml, and saturation was attained at this level.

Glucose was found to be a repressor of cutinase production. A radial immunodiffusion assay for cutinase was developed, and the induction of. High-level extracellular production of Fusarium solani cutinase was achieved using a Pichia pastoris expression system.

The cutinase-encoding gene was cloned into pPICZαA with the Saccharomyces cerevisiae α-factor signal sequence and methanol-inducible alcohol oxidase promoter by two different ways.

The additional sequences of the c-myc epitope and (His) 6-tag of the vector were. Enzymatic degradation of BBP by cutinase and esterase. Purified cutinase from F. oxysporum f. pisi (kindly provided by C. Sagt, Utrecht University, Utrecht, The Netherlands) and commercial Candida cylindracea esterase (Boehringer Mannheim GmbH, Mannheim, Germany) were dissolved in Tris-HCl buffer (10 mM, pH ), and the enzyme concentration was adjusted to 10 or.

These originated from different sources, including fungi (e.g. Fusarium solani f. pisi, Magnaportha grisea, and Colletotrichum gloeosporioides), Enhanced degradation of an endocrine-disrupting chemical, butyl benzyl phthalate, by Fusarium oxysporum f.

pisi cutinase. Fusarium solani f sp pisi (Nectria haematococca) isolate with one cutinase gene produced 10 to 20% of the cutinase produced by isolate T-8 that has multiple cutinase genes, whereas cutinase gene-disrupted mutant of isolate did not produce cutinase.

On the surface of pea stem segments, lesion formation was most frequent and most severe with T-8, less frequent and less. made up of other lipases [7].

Cutinase has been purified and characterized from several different sources, mainly fungi and pollen, but also bacteria [8]. The majority of the work has been done with a fungal pathogen of peas, Fusarium solani.

pisi [9]. The production of cutinase seems to be highly regulated by growth conditions. [10]. Amino Acid Sequence of Cutinase 1 and Cutinase 2. Cutinase 1 and cutinase 2 were purified from the culture filtrates of cutin-grownF. solani pisi ().Samples of each cutinase were reduced, and SH groups were derivatized with 14 C-labeled iodoacetamide ( Ci/mol, PerkinElmer Life Sciences) and digested with trypsin as described before ().The digests were fractionated by high pressure liquid.

Spores of the phytopathogenic fungus Fusarium solani f. pisi were shown to produce the extracellular enzyme, cutinase, only when cutin or cutin hydrolysate was added to the spore suspension. Dihydroxy-C16 acid and trihydroxy-C18 acid, which are unique cutin monomers, showed the greatest cutinase-inducing activity.

Experiments with several compounds structurally related to these fatty. The cutinolytic esterase from F. solani f. pisi is active on a wide range of substrates [23,24] and this leads to the speculation that this enzyme and those characterised recently from several other pathogenic fungi (and now including the one in F.

solani f. cucurbitae race 2 strain, PGB) are multi-purpose esterases capable of. Abstract. Spores of the phytopathogenic fungus Fusarium solani f. pisi were shown to produce the extracellular enzyme, cutinase, only when cutin or cutin hydrolysate was added to the spore suspension.

Dihydroxy-C 16 acid and trihydroxy-C 18 acid, which are unique cutin monomers, showed the greatest cutinase-inducing activity. Experiments with several compounds structurally related to these. FIG. Effect ofcutin addition on cutinase production by the spores of F. solani f. pisi. Cutinase activity was measured spectrophotometrically withp-nitrophenylbutyrateasthe substrate (PNBactivity).

Botany: WoloshukandKolattukudy Downloaded at Microsoft Corporation on April 3, Fusarium solani f sp pisi (Nectria haematococca) isolate with one cutinase gene produced 10 to 20% of the cutinase produced by isolate T-8 that has multiple cutinase genes, whereas cutinase. abstract = "Fusarium venenatum A3/5 was transformed using the Aspergillus niger expression plasmid, pIGF, in which the coding sequence for the F.

solani f. sp. pisi cutinase gene had been inserted in frame, with a KEX2 cleavage site, with the truncated A. niger glucoamylase gene under control of the A.

niger glucoamylase promoter.The Plant Cell, Vol. 6,July O American Society of Plant Physiologists Cutinase Gene Disruption in Fusarium solani f sp pisi Decreases Its Virulence on Pea Linda M. Rogers, Moshe A. Flaishman, and Pappachan E. Kolattukudy’ Ohio State Biotechnology Center, Rightmire Hall, Carmack Road, The Ohio State University, Columbus, Ohio.Chitosan, a polymer of β-1,4-linked glucosamine residues with a strong affinity for DNA, was implicated in the pea pod- Fusarium solani interaction as an elicitor of phytoalexin production, an inhibitor of fungal growth and a chemical which can protect pea tissue from infection by F.

solani f. sp. pisi. Purified Fusarium fungal cell walls can elicit phytoalexin production in pea pod tissue.