Cloning and characterization of a gene encoding the endopolygalacturonase of Fusarium moniliforme

Caprari, Claudio; Richter, Arndt; Bergmann, Carl; Cicero, Stefania Lo; Salvi, Giovanni E.; Cervone, Felice; Lorenzo, Giulia De

doi:10.1016/s0953-7562(09)80138-x

Cited by 69 publications

(38 citation statements)

References 39 publications

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“…F. moniliforme Sheldon) is the most intensively studied CWDE thus far (Caprari et al, 1993;Posada et al, 2000Posada et al, , 2001Daroda et al, 2001). PG degrades the a-1,4 galacturonosyl bonds of the homogalacturonan regions of pectins within the middle lamella and primary cell wall, and may facilitate the growth of hyphae within the plant tissue.…”

Section: Introductionmentioning

confidence: 99%

A single amino acid substitution in highly similar endo-PGs from Fusarium verticillioides and related Fusarium species affects PGIP inhibition

Raiola

Sella

Castiglioni

et al. 2008

Fungal Genetics and Biology

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Section: Introductionmentioning

confidence: 99%

A single amino acid substitution in highly similar endo-PGs from Fusarium verticillioides and related Fusarium species affects PGIP inhibition

Raiola

Sella

Castiglioni

et al. 2008

Fungal Genetics and Biology

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“…dition, comparison of two fungal PGs, C. carbonum [14] and F. moniliforme [6], also showed 51~o and 44.5~o similarity, respectively, at the protein level (not shown). These sequence comparisons suggest that cotton G9 belongs to the P G family of proteins.…”

mentioning

confidence: 99%

Cotton (Gossypium hirsutum L.) pollen-specific polygalacturonase mRNA: tissue and temporal specificity of its promoter in transgenic tobacco

John¹,

Petersen²

1994

Plant Mol Biol

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A gene (G9) expressed during late microsporogenesis in cotton (Gossypium hirsutum L.) was isolated. Sequence analysis of the cDNA (1.3 kb) as well as the gene (2.6 kb) revealed an open reading frame of 1233 bases encoding a protein of 43.9 kDa. The coding region of the gene is interrupted by three introns. Northern analysis of the RNA from developing anthers showed that the transcripts appear 12 days before anthesis and that the maximal concentration of RNA occurs in pollen on the day of anthesis. This pattern of gene expression suggests functions in post-anthesis events. Sequence comparisons with other known plant genes indicated that G9 is homologous to polygalacturonases. The G9 promoter conferred tissue and temporal specificity of beta-glucuronidase (GUS) expression in transgenic tobacco plants. Thus, the G9 promoter can be used to drive gene expression in homologous as well as heterologous plants in a tissue-specific manner.

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“…A signal peptide cleavage site was predicted in PGD after the ¢rst 16 N-terminal amino acid residues [15] and con¢rmed by the N-terminal sequencing of the puri¢ed enzyme. PGD shares the highest sequence similarity with the Fusarium moniliforme PG [16] and BcPG3 from Botrytis cinerea [17]. This is demonstrated also at the molecular level by the similar exon and intron organization and the presence of the additional exon in the 5P part of pgaD, when compared to the F. moniliforme PG-encoding gene and to Bcpg3 from B. cinerea, respectively (Fig.…”

Section: The Primary Amino Acid Sequence Of Pgdmentioning

confidence: 89%

Characterization of a novel endopolygalacturonase fromAspergillus nigerwith unique kinetic properties

Pařenicová¹,

Kester²,

Benen³

et al. 2000

FEBS Letters

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We isolated and characterized a new type of endopolygalacturonase (PG)-encoding gene, pgaD, from Aspergillus niger. The primary structure of PGD differs from that of other A. niger PGs by a 136 amino acid residues long N-terminal extension. Biochemical analysis demonstrated extreme processive behavior of the enzyme on oligomers longer than five galacturonate units. Furthermore, PGD is the only A. niger PG capable of hydrolyzing di-galacturonate. It is tentatively concluded that the enzyme is composed of four subsites. The physiological role of PGD is discussed.z 2000 Federation of European Biochemical Societies.

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Cloning and characterization of a gene encoding the endopolygalacturonase of Fusarium moniliforme

Cited by 69 publications

References 39 publications

A single amino acid substitution in highly similar endo-PGs from Fusarium verticillioides and related Fusarium species affects PGIP inhibition

A single amino acid substitution in highly similar endo-PGs from Fusarium verticillioides and related Fusarium species affects PGIP inhibition

Cotton (Gossypium hirsutum L.) pollen-specific polygalacturonase mRNA: tissue and temporal specificity of its promoter in transgenic tobacco

Characterization of a novel endopolygalacturonase fromAspergillus nigerwith unique kinetic properties

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