Characterization and Localization of New Antifungal Cysteine-Rich Proteins from<i>Beta vulgaris</i>

Km, Kragh; Nielsen, Jeppe Agger; Kk, Nielsen; Dreboldt, S; Jd, Mikkelsen

doi:10.1094/mpmi-8-0424

Cited by 95 publications

(68 citation statements)

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“…Plant and fungal defensins are cysteine-rich proteins ranging from 45 to 54 amino acids, are positively charged, and in most cases contain four disulfide bonds that stabilize each protein in solution (4,5,38,49,87,88,106,110,135,155,168,169,170,181). In addition, most defensins are highly oligomeric (many subunits of 4 to 5 kDa) in situ (168,169).…”

Section: Fungal Cell Wall Structurementioning

confidence: 99%

Antifungal Proteins

Selitrennikoff

2001

Appl Environ Microbiol

529

362

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Section: Fungal Cell Wall Structurementioning

confidence: 99%

Antifungal Proteins

Selitrennikoff

2001

Appl Environ Microbiol

529

362

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“…jl-1 corresponded exactly to the characterized cDNA, but j1-2, which also has a putative coding sequence Figure 2. A, Amino acid sequence alignment of the deduced J1-1 protein with similar polypeptides from barley (y-H) , wheat (yi-P and y2-P) , petunia pistil (PPT) (Karunanandaa et al, 1994), tobacco flowers (FST) (Gu et al, 1992), sugar beet leaves (AX1) (Kragh et al, 1995), radish seeds (Rs-AFPI) (Terras et al, 1992), insect (phormicin or insect defensin A) (Lambert et al, 1989), and scorpion (Lqh ChTX, charybdotoxin from Leiurus quinquestriatus hebraeus) (Martins et al, 1990). Boldface letters indicate the conserved residues.…”

Section: Cene Familymentioning

confidence: 99%

“…For this reason, and based on structural and functional homologies with pathogen-inducible insect defensins, the term "plant defensin" was proposed to describe this class of plant peptides (Terras et al, 1995). Plant defensins have been found in radish seeds (Terras et al, 1992), tobacco flowers (Gu et al, 1992), potato flowers (Moreno et al, 1994), petunia pistils (Karunanandaa et al, 1994), and sugar beet leaves infected with Cercospora beticola (Kragh et al, 1995). These plant defensins present a specific Cys arrangement involving a particular globular structure stabilized by four disulfide bridges.…”

mentioning

confidence: 99%

Fruit-Specific Expression of a Defensin-Type Gene Family in Bell Pepper (Upregulation during Ripening and upon Wounding)

et al. 1996

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We have isolated a 454-bp cDNA that encodes a nove1 fruit-specific defensin from bell pepper (Capsicum annuum). The encoded 75-amino-acid polypeptide contains an N-terminal domain characteristic of a signal peptide and a 48-amino-acid mature domain named 11. The mature protein, from which the N-terminal amino acid sequence was determined, contains eight cysteines that form four intramolecular disulfide bridges, suggesting a monomeric form for 11. In healthy fruits J1 is undetectable at the green stage but high levels accumulate during ripening. In wound areas of the green fruit the accumulation of 11 dramatically increased, suggesting a role for Jl in the plant's defense response. Moreover, we have demonstrated that 11 possesses an antifungal activity. We have isolated and characterized the corresponding two homologous genes (jl-1 and jl-2) that exist in the hell pepper genome. Both genes are interrupted hy the insertion, at the same position, of one intron of 853 bp for j7-7 and 4900 bp for j7-2. Northern blot and reverse transcriptase-polymerase chain reaction and restriction fragment length polymorphism analyses revealed that jl-7 transcripts are present only in fruits, only in trace amounts in mature green fruits, and that they accumulate to high levels in fully ripe fruits, whereas no jl-2 transcripts were detected in the samples monitored.

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“…In the sugar beet, defensins (former name, AX proteins) were found in the stomatal cells of infected and noninfected leaves. 24) These defensins might protect leaf tissue against pathogens, because the stomata are the entry route for fungal pathogens into the internal tissues of the leaf. ATSP7 and 21 might have the same protective function in the GCs of A. thaliana.…”

Section: Discussionmentioning

confidence: 99%

Expression Analysis ofArabidopsis thalianaSmall Secreted Protein Genes

Nakamura¹,

Suzuki²,

Kawamukai³

et al. 2012

Bioscience, Biotechnology, and Biochemistry

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Small proteins secreted to the extracellular matrix in plants regulate many physiological activities, including pathogen response, material transport, and morphogenesis, but the functions of most small secreted proteins have not been elucidated except for some well-known small secreted proteins. To predict the functions and physiological roles of unidentified small secreted proteins, information on their expression patterns is valuable. Here, we report expression analysis of Arabidopsis thaliana small secreted protein (ATSP) genes that encode proteins possessing a signal peptide at Nterminal, and protein sizes were less than 100 amino acid residues. By promoter:reporter experiments, we examined the expression of 122 ATSPs, including 47 unannotated ATSPs that do not have any discernable motifs, in tissues and at the cellular level in Arabidopsis seedlings, and floral organs. As a result, 79 ATSP genes were expressed in various regions of the seedlings, and 37 ATSP genes were specifically expressed.

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Characterization and Localization of New Antifungal Cysteine-Rich Proteins fromBeta vulgaris

Cited by 95 publications

References 0 publications

Antifungal Proteins

Antifungal Proteins

Fruit-Specific Expression of a Defensin-Type Gene Family in Bell Pepper (Upregulation during Ripening and upon Wounding)

Expression Analysis ofArabidopsis thalianaSmall Secreted Protein Genes

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