Characterization of a predominantly pistil-expressed gene encoding a ?-thionin-like protein of Petunia inflata

Karunanandaa, Balasulojini; Singh, Anuradha; Kao, Teh Hui

doi:10.1007/bf00039555

Cited by 65 publications

(51 citation statements)

References 17 publications

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“…NaD1, PhD1, and PhD2 and the floral defensins, FST from cultivated tobacco (Gu et al, 1992) and TPP3 from tomato (Milligan and Gasser, 1995) all have a predicted C-terminal domain of 27 to 33 amino acids in addition to the defensin domain. In contrast, the floral defensins PPT from petunia (Karunanandaa et al, 1994) and TGAS118 from tomato (van den Heuvel et al, 2001) lack this C-terminal domain, as do the seed defensins from radish (Rs-AFP2; [Terras et al, 1995], alfalfa [alfAFP; Gao et al, 2000]), and wheat (␥1-P; Colilla et al, 1990;Fig. 1A).…”

Section: Resultsmentioning

confidence: 99%

“…Most plant defensins have been isolated from seeds (Broekaert et al, 1995), but they are also expressed in leaves (Terras et al, 1995;Segura et al, 1998), pods (Chiang and Hadwiger, 1991), tubers (Moreno et al, 1994;Stiekema et al, 1988), fruit (Meyer et al, 1996;Aluru et al, 1999), and floral tissues (Gu et al, 1992;Karunanandaa et al, 1994;Moreno et al, 1994;Milligan and Gasser, 1995;van den Heuvel et al, 2001;Park et al, 2002).…”

mentioning

confidence: 99%

“…Within the last decade, a number of defensin cDNA clones have been obtained using RNA from the floral tissues of solanaceous plants (Gu et al, 1992;Karunanandaa et al, 1994;Moreno et al, 1994;Milligan and Gasser, 1995;van den Heuvel et al, 2001). The proteins encoded by some of these clones are significantly different from the seed defensins because they have C-terminal domains of up to 33 amino acids in addition to the typical defensin domain of 47 to 48 amino acids.…”

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confidence: 99%

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Isolation and Properties of Floral Defensins from Ornamental Tobacco and Petunia

Brugliera²,

2003

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The flowers of the solanaceous plants ornamental tobacco (Nicotiana alata) and petunia (Petunia hybrida) produce high levels of defensins during the early stages of development. In contrast to the well-described seed defensins, these floral defensins are produced as precursors with C-terminal prodomains of 27 to 33 amino acids in addition to a typical secretion signal peptide and central defensin domain of 47 or 49 amino acids. Defensins isolated from N. alata and petunia flowers lack the C-terminal domain, suggesting that it is removed during or after transit through the secretory pathway. Immunogold electron microscopy has been used to demonstrate that the N. alata defensin is deposited in the vacuole. In addition to the eight canonical cysteine residues that define the plant defensin family, the two petunia defensins have an extra pair of cysteines that form a fifth disulfide bond and hence define a new subclass of this family of proteins. Expression of the N. alata defensinNaD1 is predominantly flower specific and is most active during the early stages of flower development. NaD1transcripts accumulate in the outermost cell layers of petals, sepals, anthers, and styles, consistent with a role in protection of the reproductive organs against potential pathogens. The floral defensins inhibit the growth of Botrytis cinerea andFusarium oxysporum in vitro, providing further support for a role in protection of floral tissues against pathogen invasion.

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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confidence: 99%

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Isolation and Properties of Floral Defensins from Ornamental Tobacco and Petunia

Brugliera²,

2003

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“…108, 1995Vol. 108, al., 1988Ishibashi et al, 1990;Chiang and Hadwiger, 1991;Gu et al, 1992;Karunanandaa et al, 1994).…”

Section: Plant Defensins Share Structural Properties Wlth Mammalian Amentioning

confidence: 99%

“…The following sequences were derived from protein sequencing: Rs-AFPI, Rs-AFP2 (Terras et al, 1992(Terras et al, , 1995; Hs-AFP1, Ah-AMP1, Dm-AMPI, Ct-AMP1 Sia2 (Bloch and Richardson, 1991;Nitti et al, 1995); y l -P (Collila et al, 1990); and y l -H (Mendez et al, 1990). The following sequences were deduced from cDNA clones with omission of the putative signal peptides: pSAS (Ishibashi et al, 1990);p1230 (Chiang andHadwiger, 1991); p322 (Stiekema et al, 1988); PPT (Karunanandaa et al, 1994); and FST (Gu et al, 1992 growth of a broad range of fungi at micromolar concentrations. At least two groups of antifungal plant defensins can be distinguished according to the morphogenic effects caused on treated fungal hyphae.…”

Section: Nicoliuna Iabacum (Fst) F Rec-ktesntfpgicitkppcrkacis-ek-ftdmentioning

confidence: 99%

Plant Defensins: Novel Antimicrobial Peptides as Components of the Host Defense System

Broekaert¹,

Terras²,

Cammue³

et al. 1995

Plant Physiol.

685

431

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Various mechanisms to fend off microbial invaders have been devised by a11 living organisms, including microorganisms themselves. The most sophisticated of these mechanisms relies on the synthesis of immunoglobulins directed against specific microbial targets. However, immunoglobulin-based immunity operates only in a relatively minor subset of living species, namely the higher vertebrates. A much more ancient and widespread defense strategy involves the production of small peptides that exert antimicrobial properties. As products of single genes, antimicrobial peptides can be synthesized in a swift and flexible way, and because of their small size they can be produced by the host with a minimal input of energy and biomass. Wellknown examples of antimicrobial peptides are the cecropins that accumulate in the hemolymph of many invertebrates in response to injury or infection (reviewed by Boman and Hultmark, 1987) and the magainins that are secreted by glands in the skin of amphibians (reviewed by Bevins and Zasloff, 1990). Cecropins and magainins are small (2040 residues) basic peptides displaying an amphipathic a-helical structure that can integrate in microbial membranes to form ion channels (Duclohier, 1994).Another class of antimicrobial peptides is formed by the Cys-rich peptides, which in contrast to cecropins and magainins, have a complex cystine-stabilized three-dimensional folding pattern often involving antiparallel P-sheets. Defensins are one class among the numerous types of Cys-rich antimicrobial peptides, which differ in length, number of cystine, bonds, or folding pattern (reviewed by Boman, 1995). Insect defensins (3443 residues, three disulfide bridges) are, like cecropins, produced in a pathogeninducible manner by the insect fat body and secreted in the hemolymph (reviewed by Hoffmann and Hétru, 1992).

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Plant defense peptides

Garcı́a-Olmedo¹,

Molina²,

Alamillo³

et al. 1998

Biopolymers

482

293

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Characterization of a predominantly pistil-expressed gene encoding a ?-thionin-like protein of Petunia inflata

Cited by 65 publications

References 17 publications

Isolation and Properties of Floral Defensins from Ornamental Tobacco and Petunia

Isolation and Properties of Floral Defensins from Ornamental Tobacco and Petunia

Plant Defensins: Novel Antimicrobial Peptides as Components of the Host Defense System

Plant defense peptides

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