The use of microarray μPEACH1.0 to investigate transcriptome changes during transition from pre-climacteric to climacteric phase in peach fruit

Trainotti, Livio; Bonghi, Claudio; Ziliotto, F.; Zanin, Dario; Rasori, Angela; Casadoro, Giorgio; Ramina, Angelo; Tonutti, Pietro

doi:10.1016/j.plantsci.2005.10.015

Cited by 125 publications

(106 citation statements)

References 56 publications

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“…Recent data indicated that a Pru p 1.01 isoform, named Pru p 1.06D according to its sequence identity (Gao et al, 2005;Chen et al, 2008), is one of the most abundantly expressed genes among the ripe peach mesocarp transcriptome (Trainotti et al, 2006). Pru p 1.06D shows high sequence identity (73%) to Pru p Figure 5.…”

Section: Discussionmentioning

confidence: 99%

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The RNA Hydrolysis and the Cytokinin Binding Activities of PR-10 Proteins Are Differently Performed by Two Isoforms of the Pru p 1 Peach Major Allergen and Are Possibly Functionally Related

et al. 2009

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PR-10 proteins are a family of pathogenesis-related (PR) allergenic proteins playing multifunctional roles. The peach (Prunus persica) major allergen, Pru p 1.01, and its isoform, Pru p 1.06D, were found highly expressed in the fruit skin at the pit hardening stage, when fruits transiently lose their susceptibility to the fungal pathogen Monilinia spp. To investigate the possible role of the two Pru p 1 isoforms in plant defense, the recombinant proteins were expressed in Escherichia coli and purified. Light scattering experiments and circular dichroism spectroscopy showed that both proteins are monomers in solution with secondary structures typical of PR-10 proteins. Even though the proteins do not display direct antimicrobial activity, they both act as RNases, a function possibly related to defense. The RNase activity is different for the two proteins, and only that of Pru p 1.01 is affected in the presence of the cytokinin zeatin, suggesting a physiological correlation between Pru p 1.01 ligand binding and enzymatic activity. The binding of zeatin to Pru p 1.01 was evaluated using isothermal titration calorimetry, which provided information on the stoichiometry and on the thermodynamic parameters of the interaction. The structural architecture of Pru p 1.01 and Pru p 1.06D was obtained by homology modeling, and the differences in the binding pockets, possibly accounting for the observed difference in binding activity, were evaluated.

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Section: Discussionmentioning

confidence: 99%

“…The fruit growth curve showed the typical double sigmoid pattern with the four standard growth stages (S1-S4; Bregoli et al, 2002;Trainotti et al, 2006). Four samples, consisting of three replicates of five fruits each, representative of the four stages, were chosen for expression analysis.…”

Section: Fruit Materialsmentioning

confidence: 99%

The RNA Hydrolysis and the Cytokinin Binding Activities of PR-10 Proteins Are Differently Performed by Two Isoforms of the Pru p 1 Peach Major Allergen and Are Possibly Functionally Related

et al. 2009

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“…Substantial research has been conducted to investigate the events that occur in a fruit following the appearance of the climacteric rise (Brummell and Harpster, 2001;Dumville and Fry, 2003;Trainotti et al, 2006;Chourasia et al, 2006). Fruit softening is probably caused by the cumulative effect of a range of modifications occurring in the networks of polymers making up the primary cell wall, all of which contribute in different ways to a loss of firmness and changes in textural qualities.…”

Section: Introductionmentioning

confidence: 99%

Biochemistry of fruit softening: an overview

Payasi¹,

Mishra

Chaves

et al. 2009

Physiol Mol Biol Plants

205

125

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Softening is a developmentally programmed ripening process, associated with biochemical changes in cell wall fractions involving hydrolytic processes resulting in breakdown of cell-wall polymers such as cellulose, hemicelluloses and pectin etc. Various hydrolytic reactions are brought about by polygalacturonase, pectin methyl esterase, pectate lyase, rhamnogalacturonase, cellulase and β-galactosidase etc. Besides these enzymes, expansin protein also plays an important role in softening. Textural changes during ripening help in determining the shelf life of a fruit. An understanding of these changes would help in formulating procedures for controlling fruit softening vis-à-vis enhancing shelf life of fruits. In the present review an attempt has been made to coalesce recent findings on biochemistry of fruit softening.

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“…Since our main interest was fruit quality, we focused our study on the identification of genes differentially expressed during fruit development. A similar approach has been successfully applied in peach (Trainotti et al 2006) and in pear (Fonseca et al 2004), two climacteric fruits, and in citrus, a non-climacteric fruit (Cercós et al 2006). The ultimate goal of our work was the identification of genes responsible for QTLs controlling fruit quality traits and to provide a general overview of the major metabolic processes occurring during fruit development.…”

Section: Introductionmentioning

confidence: 99%

Transcription analysis of apple fruit development using cDNA microarrays

Soglio

Costa

Molthoff³

et al. 2009

Tree Genetics & Genomes

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The knowledge of the molecular mechanisms underlying fruit quality traits is fundamental to devise efficient marker-assisted selection strategies and to improve apple breeding. In this study, cDNA microarray technology was used to identify genes whose expression changes during fruit development and maturation thus potentially involved in fruit quality traits. The expression profile of 1,536 transcripts was analysed by microarray hybridisation.

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The use of microarray μPEACH1.0 to investigate transcriptome changes during transition from pre-climacteric to climacteric phase in peach fruit

Cited by 125 publications

References 56 publications

The RNA Hydrolysis and the Cytokinin Binding Activities of PR-10 Proteins Are Differently Performed by Two Isoforms of the Pru p 1 Peach Major Allergen and Are Possibly Functionally Related

The RNA Hydrolysis and the Cytokinin Binding Activities of PR-10 Proteins Are Differently Performed by Two Isoforms of the Pru p 1 Peach Major Allergen and Are Possibly Functionally Related

Biochemistry of fruit softening: an overview

Transcription analysis of apple fruit development using cDNA microarrays

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