Analysis of Pectin Methyl Esterases

Bordenave, Marianne

doi:10.1007/978-3-642-60989-3_10

Cited by 53 publications

(60 citation statements)

References 65 publications

(87 reference statements)

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“…The isoelectric pH (pI) of PMEs varies from as low as 3.1 for fungal PME to 11 for tomato PME. Most of the purified plant PMEs have a neutral to alkaline pI, with an exception of a few acidic ones (Bordenave 1996).…”

Section: Pectin Methyl Esterase (Pme)mentioning

confidence: 99%

Pectins in Processed Fruit and Vegetables: Part I—Stability and Catalytic Activity of Pectinases

Duvetter¹,

Sila²,

Buggenhout³

et al. 2009

Comp Rev Food Sci Food Safe

115

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Pectinases catalyze numerous pectin conversion reactions strongly impacting on the quality of fruits, vegetables, and the related intermediate and end products. The effect of processing on the stability and catalytic activity of pectinases is of prime importance to food processors since desirable and/or deleterious reactions can be tailored (accelerated or inhibited) meeting specific quality targets. Of the multiple endogenous enzymes involved in the modification and degradation of pectin, pectinmethylesterase (PME), and polygalacturonase (PG) have been widely investigated in the context of fruit and vegetable processing. This review covers the stability and catalytic activity of endogenous plant PME and PG including the quantitative approaches applied in inactivating and/or boosting the catalytic activity of the enzymes in purified and real food systems. This will be discussed in the context of both traditional and novel food processing technologies.

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Section: Pectin Methyl Esterase (Pme)mentioning

confidence: 99%

Pectins in Processed Fruit and Vegetables: Part I—Stability and Catalytic Activity of Pectinases

Duvetter¹,

Sila²,

Buggenhout³

et al. 2009

Comp Rev Food Sci Food Safe

115

View full text Add to dashboard Cite

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“…*, Coomassie Brilliant Blue staining; 0.1 M NaCl, proteins extracted with low-salt extraction buffer; 1 M NaCl, remaining pellet after low-salt extraction reextracted with high-salt buffer; 25 mL protein extract was loaded in each lane. PMEs have been implicated in a number of processes, including cell wall extension, fruit maturation and senescence, pathogenesis, systemic movement of tobacco mosaic virus, cambial cell differentiation, and border cell separation from root caps (Moustacas et al, 1991;Tieman and Handa, 1994;Bordenave, 1996;Wen et al, 1999;Micheli et al, 2000;Chen and Citovsky, 2003). Although it has been suggested that PMEs also participate in pollen tube growth (Mu et al, 1994;Wakeley et al, 1998), evidence for this has only recently been presented in a study in which the functional interruption of an Arabidopsis pollen PME, called VANGUARD1 (VGD1), reduced the total PME activity in pollen to 82% of the wild-type pollen.…”

Section: Expression Of the Pme Domain Alters The Methylesterificationmentioning

confidence: 99%

“…On one hand, PMEs produce acidic pectins, which can bind Ca 21 and reinforce the wall structure. On the other hand, the protons produced by the hydrolysis decrease the local cell wall pH and, consequently, can promote the activity of cell wall hydrolases and result in cell extension and growth (Gaffe et al, 1994;Bordenave, 1996). Which of these two effects prevails might depend on the PME isoform itself, the local pH, the availability of cations, the presence of cell wall-loosening hydrolases, or even the degree and distribution of esterification on the secreted pectins (Moustacas et al, 1991;Charnay et al, 1992;Bordenave, 1996;Catoire et al, 1998).…”

Section: Expression Of the Pme Domain Alters The Methylesterificationmentioning

confidence: 99%

“…Alternatively, it has been proposed that the localized reduction in pH, due to the deesterification process, could promote cell wall extension or growth by stimulating the activity of several cell wall-loosening hydrolases, such as polygalacturonases and pectate lyases (Wen et al, 1999; Ren and Kermode, 2000). It is suggested that these opposing effects, cell wall stiffening versus cell wall loosening, are associated with specific PME isoforms or are regulated depending on the microenvironment, in particular apoplastic pH and the availability of divalent cations (Moustacas et al, 1991;Charnay et al, 1992;Bordenave, 1996;Catoire et al, 1998).…”

mentioning

confidence: 99%

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Pectin Methylesterase, a Regulator of Pollen Tube Growth

2005

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The apical wall of growing pollen tubes must be strong enough to withstand the internal turgor pressure, but plastic enough to allow the incorporation of new membrane and cell wall material to support polarized tip growth. These essential rheological properties appear to be controlled by pectins, which constitute the principal component of the apical cell wall. Pectins are secreted as methylesters and subsequently deesterified by the enzyme pectin methylesterase (PME) in a process that exposes acidic residues. These carboxyls can be cross-linked by calcium, which structurally rigidifies the cell wall. Here, we examine the role of PME in cell elongation and the regulation of its secretion and enzymatic activity. Application of an exogenous PME induces thickening of the apical cell wall and inhibits pollen tube growth. Screening a Nicotiana tabacum pollen cDNA library yielded a pollen-specific PME, NtPPME1, containing a pre-region and a pro-region. Expression studies with green fluorescent protein fusion proteins show that the pro-region participates in the correct targeting of the mature PME. Results from in vitro growth analysis and immunolocalization studies using antipectin antibodies (JIM5 and JIM7) provide support for the idea that the pro-region acts as an intracellular inhibitor of PME activity, thereby preventing premature deesterification of pectins. In addition to providing experimental data that help resolve the significance and function of the pro-region, our results give insight into the mechanism by which PME and its pro-region regulate the cell wall dynamics of growing pollen tubes.Pollen tube growth, which delivers the sperm cells to the female gametophyte in the ovule, is essential for plant reproduction. The elongation process is driven by the secretion of Golgi-derived vesicles that dock and fuse with the plasma membrane at the extreme apex of the tube, providing new plasma membrane and cell wall components necessary for polarized pollen tube growth. Their fast growth and relative ease of culture in vitro make pollen tubes a wellestablished model system for studying cell elongation in plants. In the search for cellular components that regulate pollen tube growth, most of the attention has been drawn to secretory membrane traffic, intracellular motility, ion activities, and turgor pressure, while the contribution of the cell wall has been somewhat neglected ). Yet, the apical cell wall certainly is a key component since it has to be strong enough to withstand the internal turgor pressure, but, at the same time, provide enough plasticity to allow the incorporation of new membrane and cell wall material to support tip growth (Steer and Steer, 1989).The wall in the tip region of the pollen tube is composed of a single pectin layer, where neither cellulose nor callose has been detected (Ferguson et al., 1998). Homogalacturonan, a major component of pectins, is a linear polymer composed of (1,4)-a-D-galacturonic acid (GalUA) residues. Current evidence indicates that these pectins are synthesized and ...

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“…In higher plants, though some PMEs are ubiquitously present (Gaffe et al, 1997), others are specifically expressed during root development (Wen et al, 1999), fruit ripening (Frenkel et al, 1998), or stem elongation (Bordenave, 1996;Pilling et al, 2000). Furthermore, recent analysis of pollen-specific transcriptome of Arabidopsis indicated that several PMEs are specifically expressed in floral buds, including pollen (Pina et al, 2005).…”

Section: Tissue Specific Expression Of Ospme1mentioning

confidence: 99%

Isolation and Expression analysis of OsPME1, encoding for a putative Pectin Methyl Esterase from Oryza sativa (subsp. indica)

Kanneganti

Gupta

2009

Physiol Mol Biol Plants

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Pectin Methyl Esterases (PMEs) play an essential role during plant development by affecting the mechanical properties of the plant cell walls. Recent studies indicated that PMEs play important role in pollen tube development. In this study, we isolated a 1.3 kb cDNA clone from rice panicle cDNA library. It contained a 1038 bp of open reading frame (ORF) encoding for a putative pectin methyl esterase of 345 aminoacids with a 20 aminoacid signal peptide and was hence designated as OsPME1 (Oryza sativa Pectin Methyl Esterase 1). It contained the structural arrangement GXYXE and GXXDFIF, found in the active groups of all PMEs. OsPME1 gene product shared varying identities, ranging from 52 % to 33 % with PMEs from other plant species belonging to Brassicaceae, Fabaceae, Amaranthaceae and Funariaceae. Southern blot analysis indicated that PME1 exists as a single copy in the rice genome. Expression pattern analysis revealed that OsPME1 is expressed only in pollen grains, during the later stages of their development and was also regulated by various abiotic stress treatments and phytohormones. Functional characterization of this pollen specific PME from rice would enable us to understand its role in pollen development.

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Analysis of Pectin Methyl Esterases

Cited by 53 publications

References 65 publications

Pectins in Processed Fruit and Vegetables: Part I—Stability and Catalytic Activity of Pectinases

Pectins in Processed Fruit and Vegetables: Part I—Stability and Catalytic Activity of Pectinases

Pectin Methylesterase, a Regulator of Pollen Tube Growth

Isolation and Expression analysis of OsPME1, encoding for a putative Pectin Methyl Esterase from Oryza sativa (subsp. indica)

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