Characterization of changes in pectin methylesterase expression and pectin esterification during tomato fruit ripening

2000 ◽  
Vol 78 (5) ◽  
pp. 607-618 ◽  
Author(s):  
J M Blumer ◽  
R P Clay ◽  
C W Bergmann ◽  
P Albersheim ◽  
A Darvill
Keyword(s):  
Cell Walls ◽  
Tomato Fruit ◽  
Middle Lamella ◽  
Pectin Methylesterase ◽  
Fresh Market ◽  
Tomato Fruit Ripening ◽  
Tissue Print ◽  
Pectin Esterification

The production, accumulation, and in situ location of pectin methylesterase (EC 3.1.11) was examined in ripening fruit of the processing tomato cv. UC82B. Pectin methylesterase detected with a monoclonal antibody (PME-1) first appeared adjacent to seeds in immature green fruit and was later detected only in tissue adjacent to the cuticle (i.e., exopericarp) during ripening. Enzyme-linked immunosorbant assay and Western blot analysis using PME-1 demonstrated that the fresh-market cultivars Celebrity and Better Boy accumulated lower levels of this immunologically detectable pectin methylesterase during maturation than did processing cv. UC82B, and that the immunologically detected pectin methylesterase and the total detectable pectin methylesterase activities of 'Celebrity' and 'Better Boy' increased throughout ripening. In contrast, processing cv. UC82B displayed a total detectable pectin methylesterase activity profile that peaked during the breaker stage, a finding supported immunologically by tissue-printing. To correlate pectin methylesterase expression during ripening to the degree of methylesterification of pectins in exopericarp cell walls, we subjected exopericarp tissue from 'UC82B' fruit to an immunocytochemical and ultrastructure study. Esterified pectin decreased in some regions of the exopericarp cell walls during fruit development but persisted in some regions as well. Less-esterified pectin was localized in the middle lamella of exopericarp cell walls during preripe stages, while in ripe fruit, this labeling was largely absent.Key words: pectin methylesterase (PME), immunocytochemistry, tissue-print, pectin esterification, Lycopersicon esculentum.

Characterization of changes in pectin methylesterase expression and pectin esterification during tomato fruit ripening

2000 ◽  
Vol 78 (5) ◽  
pp. 607-618 ◽  
Author(s):  
J.M. Blumer ◽  
R.P. Clay ◽  
C.W. Bergmann ◽  
P. Albersheim ◽  
A. Darvill
Keyword(s):  
Fruit Ripening ◽  
Tomato Fruit ◽  
Pectin Methylesterase ◽  
Tomato Fruit Ripening ◽  
Pectin Esterification

Multifaceted roles of nitric oxide in tomato fruit ripening: NO-induced metabolic rewiring and consequences for fruit quality traits

2020 ◽  
Author(s):  
Rafael Zuccarelli ◽  
Marta Rodríguez-Ruiz ◽  
Patrícia J Lopes-Oliveira ◽  
Grazieli B Pascoal ◽  
Sónia C S Andrade ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Tomato Fruit ◽  
Simultaneous Action ◽  
Minimal Impact ◽  
Tomato Fruit Ripening ◽  
Early Ripening ◽  
Tissue Sensitivity ◽  
Climacteric Stage ◽  
Scavenging Enzymes

Abstract Nitric oxide (NO) has been implicated as part of the ripening regulatory network in fleshy fruits. However, very little is known about the simultaneous action of NO on the network of regulatory events and metabolic reactions behind ripening-related changes in fruit color, taste, aroma and nutritional value. Here, we performed an in-depth characterization of the concomitant changes in tomato (Solanum lycopersicum) fruit transcriptome and metabolome associated with the delayed-ripening phenotype caused by NO supplementation at the pre-climacteric stage. Approximately one-third of the fruit transcriptome was altered in response to NO, including a multilevel down-regulation of ripening regulatory genes, which in turn restricted the production and tissue sensitivity to ethylene. NO also repressed hydrogen peroxide-scavenging enzymes, intensifying nitro-oxidative stress and S-nitrosation and nitration events throughout ripening. Carotenoid, tocopherol, flavonoid and ascorbate biosynthesis were differentially affected by NO, resulting in overaccumulation of ascorbate (25%) and flavonoids (60%), and impaired lycopene production. In contrast, the biosynthesis of compounds related to tomato taste (sugars, organic acids, amino acids) and aroma (volatiles) was slightly affected by NO. Our findings indicate that NO triggers extensive transcriptional and metabolic rewiring at the early ripening stage, modifying tomato antioxidant composition with minimal impact on fruit taste and aroma.

Electrophoretic characterization of endo-(1,4)-β-glucanases secreted during assimilative growth and antheridiol-induced branching inAchlya ambisexualis

1996 ◽  
Vol 42 (6) ◽  
pp. 557-561 ◽  
Author(s):  
Terry W. Hill
Keyword(s):  
Enzyme Activity ◽  
Sodium Dodecyl Sulfate ◽  
Cell Walls ◽  
Sodium Dodecyl ◽  
Achlya Ambisexualis ◽  
Dodecyl Sulfate ◽  
Exclusion Chromatography ◽  
Molecular Masses

Secreted endo-(1,4)-β-glucanases ("cellulases") of Achlya ambisexualis were analyzed by a technique that permits visualization of enzyme activity in situ after electrophoresis in gels containing sodium dodecyl sulfate. Catalytic polypeptides with molecular masses of about 97, 74, 36, 29, and 25 kDa were observed in media from young cultures, though progressively fewer bands were observed as cultures aged. Based on size estimations of native enzymes with gel exclusion chromatography, the 97- and 36-kDa polypeptides were concluded to be subunits of a 245-kDa holoenzyme and the 25-kDa polypeptides were concluded to be subunits of a second holoenzyme of about 92 kDa. The data were insufficient to allow similar assignments for the more ephemeral 74- and 29-kDa polypeptides. The endoglucanases secreted during branch induction by antheridiol or 0.2% peptone comigrated in electrophoretic gels with enzymes secreted during normal assimilative growth. No endoglucanases specific to induced branching were observed.Key words: oomycetes, cell walls, endoglucanases, cellulases, antheridiol.

Characterization of tomato fruit ripening and analysis of gene expression in F1 hybrids of the ripening inhibitor (rin) mutant

2005 ◽  
Vol 123 (3) ◽  
pp. 331-338 ◽  
Author(s):  
Mamiko Kitagawa ◽  
Hirotaka Ito ◽  
Takeo Shiina ◽  
Nobutaka Nakamura ◽  
Takahiro Inakuma ◽  
...  
Keyword(s):  
Gene Expression ◽  
Fruit Ripening ◽  
Tomato Fruit ◽  
F1 Hybrids ◽  
Tomato Fruit Ripening ◽  
Ripening Inhibitor ◽  
Rin Mutant

scholarly journals Functional Characterization of SlSAHH2 in Tomato Fruit Ripening

2017 ◽  
Vol 8 ◽  
Author(s):  
Lu Yang ◽  
Guojian Hu ◽  
Ning Li ◽  
Sidra Habib ◽  
Wei Huang ◽  
...  
Keyword(s):  
Fruit Ripening ◽  
Tomato Fruit ◽  
Functional Characterization ◽  
Tomato Fruit Ripening

A functional pectin methylesterase inhibitor protein (SolyPMEI) is expressed during tomato fruit ripening and interacts with PME-1

2012 ◽  
Vol 79 (4-5) ◽  
pp. 429-442 ◽  
Author(s):  
Ida Barbara Reca ◽  
Vincenzo Lionetti ◽  
Laura Camardella ◽  
Rossana D’Avino ◽  
Thierry Giardina ◽  
...  
Keyword(s):  
Fruit Ripening ◽  
Tomato Fruit ◽  
Pectin Methylesterase ◽  
Inhibitor Protein ◽  
Pectin Methylesterase Inhibitor ◽  
Tomato Fruit Ripening

scholarly journals Host-Elicited Germination and Mechanism of Penetration in Broomrape (Orobanche Spp.)

1993 ◽  
Author(s):  
Daniel M. Joel ◽  
John C. Steffens ◽  
Alfred M. Mayer
Keyword(s):  
Host Cell ◽  
Sesquiterpene Lactone ◽  
Cell Walls ◽  
High Field ◽  
Infection Process ◽  
Pectin Methyl Esterase ◽  
Parasitic Weed ◽  
Enzymatic Nature

Orobanche is an important parasitic weed. For developing novel methods for its control, a thorough understanding of crucial stages of its development is needed. Therefore, the objectives of this project were characterization of Orobanche germination stimulants, analysis of mechanisms of haustorial penetration, and characterization and isolation of penetration enzymes. The first highly potent natural germination stimulant for Orobanche was isolated from sunflower and identified by high-field 1D (1H and 13C), 2D (1H-1H COSY, HMQC, HMBC)-NMR, GC.FT-IR, and GC.MS as costuslactone, a guaiane type sesquiterpene lactone that resembles strigol only in possessing a lactone moiety that is required for activity. The first direct in situ evidence for the enzymatic nature of the infection process of a parasitic angiosperm was established. Pectin deesterification and depletion of pectins in host cell walls were shown adjacent to haustorial cells. Pectin methyl esterase and polygalacturonase were immunocytochemically detected in intrusive cells and in adjacent host apoplast. Orobanche tissues contain inhibitors of PGase activity. PME and three PGases were isolated from Orobanche calli. PME was characterized and purified, and antibodies were prepared against it. This study presents novel findings regarding parasitism in Orobanche, which may help to open up new approaches for controlling broomrapes.

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