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

Meyer, Béatrice; Houlné, Guy; Pozueta‐Romero, Javier; Schantz, Marie-Luce; Schantz, Rodolphe

doi:10.1104/pp.112.2.615

Cited by 81 publications

(70 citation statements)

References 22 publications

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“…Plant defensins have initially been identified in seeds , and recently been reported in other plant organs and tissues, e.g., leaves, flower, fruit, pods and tubers (Stiekema et al 1988;Chiang and Hadwiger 1991;Meyer et al 1996;Urdangarin et al 2000). They play a significant role in host defense.…”

Section: Introductionmentioning

confidence: 99%

Antifungal activity of a recombinant defensin CADEF1 produced by Escherichia coli

2009

World J Microbiol Biotechnol

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The defensin CADEF1 has been known to be uptranscripted in the pepper Capsicum annuum L., upon bacterial attack, abiotic elicitors and environmental stresses. However, the native form of CADEF1 has not been purified from the pepper, and its activity against fungi has been uncertain. In this study, the full-length cDNA of CADEF1 was obtained by fragment piecing-together method. Thereafter, its mature peptide coding sequence was inserted into bacterial expression vector pET28a(?), and the recombinant vector was transformed into Escherichia coli BL21 (DE3). Based on SDS-PAGE and Western blotting analysis, the recombinant CADEF1 was produced as a 5.6 kDa protein in the form of inclusion body in E. coli BL21 (DE3) and the expression level accounted for 15% of the bacterial total protein. Further processing through protein refolding and purification, converted the inclusion body type of CADEF1 into active form with the yield about 13 lg/ml of culture. The refolded CADEF1 significantly showed the activity against growth of the fungal pathogen Verticillium dahliae on average by 67.9% in vitro assay. These results verified the novel activity of CADEF1, which might benefit in prevention of the fungus-related disease in agricultural production.

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Section: Introductionmentioning

confidence: 99%

Antifungal activity of a recombinant defensin CADEF1 produced by Escherichia coli

2009

World J Microbiol Biotechnol

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“…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).…”

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confidence: 99%

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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“…It is possible that, although being expressed, the frameshifted MUC1/ZD protein (and perhaps similar MUC1-frameshifted proteins) may have no biological function. However, a tblastn search did reveal limited similarity with a group of proteins that function in the innate immune system (42)(43)(44)(45). The best fit is seen between MUC1/ZD and CD14, a protein that binds bacterial surface components (46).…”

Section: E1 and E2 Compare Spots Designated By Arrowheads)mentioning

confidence: 99%

A Novel Protein Derived from the MUC1 Gene by Alternative Splicing and Frameshifting

Levitin

Baruch

Weiss

et al. 2005

Journal of Biological Chemistry

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Genes that have been designated the name "MUC" code for proteins comprising mucin domains. These proteins may be involved in barrier and protective functions. The first such gene to be characterized and sequenced is the MUC1 gene. Here we report a novel small protein derived from the MUC1 gene by alternative splicing that does not contain the hallmark of mucin proteins, the mucin domain. This protein termed MUC1/ZD retains the same N-terminal MUC1 sequences as all of the other known MUC1 protein isoforms. The common N-terminal sequences comprise the signal peptide and a subsequent stretch of 30 amino acids. In contrast, the MUC1/ZD C-terminal 43 amino acids are novel and result from a reading frameshift engendered by a splicing event that forms MUC1/ZD. The expression of MUC1/ZD at the protein level in human tissues is demonstrated by Western blotting, immunohistochemistry, immunoprecipitation, and an ELISA. Utilization was made of affinity-purified MUC1/ZD-specific polyclonal antibodies as well as two different monoclonal antibodies that are monospecific for the MUC1/ZD protein. The MUC1/ZD protein is expressed in tissues as an oligomeric complex composed of monomers linked by disulfide bonds contributed by MUC1/ZD cysteine residues. MUC1/ZD protein expression did not parallel that of the tandem-repeat array-containing MUC1 protein. Results presented here demonstrate for the first time the expression of a novel MUC1 protein isoform MUC1/ZD, which is generated by an alternative splicing event that both deletes the tandem-repeat array and leads to a C-terminal reading frameshift.Genes classified, for the most part, as MUC genes code for proteins that comprise mucin domains rich in proline, threonine, and serine residues (1). The heavily glycosylated mucin proteins derived from the MUC genes can be divided into those that are secreted from the cell (secreted mucins) and mucins that comprise a transmembrane domain that anchors them to the cell membrane (transmembrane mucins). The archetype membrane-tethered mucin, which was the one to be first characterized and sequenced, is derived from the MUC1 gene (2-5). It is a transmembrane protein that contains the serine-threonine-rich tandem-repeat region in its extracellular domain (Fig. 1A, MUC1/REP) and also comprises a 72 amino acid tail that can be tyrosine-phosphorylated (6, 7). The phosphorylated cytoplasmic domain subsequently interacts with second messenger proteins (6 -23), thereby relaying a signal to the nucleus that modifies gene expression.Challenging the classical definition of a mucin gene is the discovery of MUC1 mRNAs, which although transcribed from a mucin gene are devoid of a tandem-repeat array (24 -32). Alternative splicing generates these MUC1-derived mRNAs that no longer code for tandem-repeat array-containing mucin proteins. The prime example is the tandem-repeat array-deleted MUC1/Y isoform, which is expressed both as mRNA and protein (24 -26, 30, 31). The MUC1/Y protein is similar to MUC1/ REP in that it also contains the transmembrane and cytop...

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

Cited by 81 publications

References 22 publications

Antifungal activity of a recombinant defensin CADEF1 produced by Escherichia coli

Antifungal activity of a recombinant defensin CADEF1 produced by Escherichia coli

Isolation and Properties of Floral Defensins from Ornamental Tobacco and Petunia

A Novel Protein Derived from the MUC1 Gene by Alternative Splicing and Frameshifting

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