The amino acid sequence and reactive site of a single-headed trypsin inhibitor from wheat endosperm

Poerio, Elia; Caporale, Carlo; Carrano, Lùcia; Caruso, Carla; Vacca, Francesco; Buonocore, Vincenzo

doi:10.1007/bf01891977

Cited by 13 publications

(6 citation statements)

References 37 publications

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“…Hasan and Leatherbarrow, 1998) and wheat (e.g. Poerio et al, 1994). However, only Cordero et al (1994) have employed PIs to investigate wound-associated signalling in cereals.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a proteinase inhibitor from Brachypodium distachyon suggests the conservation of defence signalling pathways between dicotyledonous plants and grasses

Mur

Casson

et al. 2004

Molecular Plant Pathology

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SUMMARY Proteinase inhibitors (PIs) are established markers for wound- and especially jasmonate-mediated signalling in dicot species such as tomato and potato. Differential screening of a cDNA library constructed from RNA isolated from wounded leaves of the grass Brachypodium distachyon led to the identification of a proteinase inhibitor gene (Bdpin1). Bdpin1 exhibited the highest homology to the subtilisin/chymotrypsin-inhibiting subgroup of the pin1 class of plant PIs. Northern analyses indicated that Bdpin1 was induced within 6 h at the site of wounding and systemically, by 24 h, thereby providing evidence for long-distance signalling in grasses. Bdpin1 also proved to be more rapidly induced in susceptible than in resistant ecotypes of B. distachyon following challenge with the Rice blast pathogen, Magnaporthe grisea. Screening with chemical signals indicated that Bdpin1 could be induced with MeJA but not with the putative mimic of salicylic acid, benzothiadiazole. Genomic Southern hybridization was consistent with Bdpin1 existing at a single locus, which was isolated following screening of a genomic cosmid library. DNA upstream of the Bdpin1 coding sequence was characterized via fusion to a GUS reporter and was found to confer wound-responsive transcription in B. distachyon and other cereals following biolistic bombardment. Both wound- and TMV-activated Bdpin1-GUS activity was detected in transgenic tobacco. Given that B. distachyon represents an ancestral grass species, our data suggest that there is considerable conservation in defence-associated signalling between dicots and grasses.

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“…Hasan and Leatherbarrow, 1998) and wheat (e.g. Poerio et al, 1994). However, only Cordero et al (1994) have employed PIs to investigate wound-associated signalling in cereals.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a proteinase inhibitor from Brachypodium distachyon suggests the conservation of defence signalling pathways between dicotyledonous plants and grasses

Mur

Casson

et al. 2004

Molecular Plant Pathology

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“…In recent years, a Bowman–Birk‐type protease inhibitor, coded WTI (wheat trypsin inhibitor), has been purified and characterized from wheat kernels (Poerio et al . 1989, 1994). The physiological role of WTI has been associated with the control of protein metabolism during kernel development and germination by forming inactive trypsin‐inhibitor complexes.…”

Section: Introductionmentioning

confidence: 99%

Antifungal Activity of a Bowman–Birk‐type Trypsin Inhibitor from Wheat Kernel

Chilosi¹,

Caruso²,

Caporale³

et al. 2000

Journal of Phytopathology

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A trypsin inhibitor from wheat kernel (WTI) was found to have a strong antifungal activity against a number of pathogenic fungi and to inhibit fungal trypsin‐like activity. WTI inhibited in vitro spore germination and hyphal growth of pathogens, with protein concentration required for 50% growth inhibition (IC50) values ranging from 111.7 to above 500 μg/ml. As observed by electron microscopy, WTI determined morphological alterations represented by hyphal growth inhibition and branching. One of the fungal species tested, Botrytis cinerea produced a trypsin‐like protease, which was inhibited by the trypsin inhibitor. WTI, as well as other seed defence proteins, appear to be an important resistance factor in wheat kernels during rest and early germination when plants are particularly exposed to attack by potential soil‐borne pathogens.

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“…Many biological aspects of these inhibitors such as tissue localization, speci city, molecular and structural properties, regulatory function, and nutritional role have been investigated (2).…”

Section: Introductionmentioning

confidence: 99%

Isolation and Characterization of a New Trypsin Inhibitor from Crotalaria paulina Seeds

Pando

Ciero²,

Novello

et al. 1999

IUBMB Life

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SummaryA new trypsin inhibitor (CPTI) has been isolated from Crotalaria paulina seeds. Puri cation of the inhibitor was carried out by gel ltration, ion-exchange chromatography, and subsequent reversed-phase HPLC. The presence of a single polypeptide chain, with a molecular mass of 20 kDa and isoelectric point 4.0, was detected. The trypsin inhibitor had a K i value of 4.5 £ 10 ¡ 8 M and was capable of acting on human, bovine, and porcine trypsin and weakly on bovine chymotrypsin. Amino acid analysis showed that CPTI has a high content of aspartate, glutamate, leucine, serine, and glycine, having 177 amino acid residues in its composition. These data suggest that the protein belongs to the Kunitz-type trypsin inhibitors. IUBMB Life, 48: 519-523, 1999

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The amino acid sequence and reactive site of a single-headed trypsin inhibitor from wheat endosperm

Cited by 13 publications

References 37 publications

Characterization of a proteinase inhibitor from Brachypodium distachyon suggests the conservation of defence signalling pathways between dicotyledonous plants and grasses

Characterization of a proteinase inhibitor from Brachypodium distachyon suggests the conservation of defence signalling pathways between dicotyledonous plants and grasses

Antifungal Activity of a Bowman–Birk‐type Trypsin Inhibitor from Wheat Kernel

Isolation and Characterization of a New Trypsin Inhibitor from Crotalaria paulina Seeds

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