Localization of pectins and arabinogalactan-proteins in lily (Lilium longiflorum L.) pollen tube and style, and their possible roles in pollination

Jauh, Guang‐Yuh; Lord, Elizabeth M.

doi:10.1007/bf00196566

Cited by 169 publications

(186 citation statements)

References 39 publications

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“…We know that phospholipase C releases membrane-bound AGPs as soluble periplasmic AGPs that are then incorporated into the growing wall as putative pectic plasticizers (Lamport, 2001;Lamport et al, 2006). We also know that the b-D-glucosyl Yariv reagent inhibits expansion growth (Jauh and Lord, 1996) and that this reagent strongly associates with AGPs, potentially negating the role of AGPs as a plasticizer in muro and thus inhibiting expansion growth. Taking what we know Figure 2.…”

Section: The Noughties: Form and Functionmentioning

confidence: 99%

Role of the Extensin Superfamily in Primary Cell Wall Architecture

et al. 2011

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Section: The Noughties: Form and Functionmentioning

confidence: 99%

Role of the Extensin Superfamily in Primary Cell Wall Architecture

et al. 2011

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“…Moreover, transgenic tobacco plants successfully engineered for downregulated TTS expression demonstrated reduced pollen tube growth in the style and reduced seed production compared with wild-type plants [26]. In another set of experiments, Yariv reagent was applied to lily pollen tubes and shown to inhibit their growth and to produce a bulbous morphology at the pollen tube tip [70,71]. Furthermore, the normal influx of calcium at the tip was inhibited by the addition of Yariv reagent.…”

Section: Reproductive Growth and Developmentmentioning

confidence: 99%

Arabinogalactan-proteins: structure, expression and function

Showalter

2001

CMLS, Cell. Mol. Life Sci.

523

480

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Abstract. Arabinogalactan-proteins (AGPs) are a family of extensively glycosylated hydroxyproline-rich glycoproteins that are thought to have important roles in various aspects of plant growth and development. After a brief introduction to AGPs highlighting the problems associated with defining and classifying this diverse family of glycoproteins, AGP structure is described in terms of the protein component (including data from molecular cloning), carbohydrate component, processing of AGPs (including recent data on glycosylphosphatidylinositol membrane anchors) and overall molecular shape. Next, the expression of AGPs is examined at several different levels, from the whole plant to the cellular levels, using a variety of experimental techniques and tools. Finally, AGP function is considered. Although the existing functional evidence is not incontrovertible, it does clearly droxyproline poor, lightly glycosylated and largely unreactive with Yariv reagent. It is worth remembering that it is human nature to group and classify things to facilitate their comprehension and discourse, whereas Mother Nature simply constructs biological entities, including AGPs, using material at hand with blatant, pedagogical disregard. Structure Protein moietyKnowledge of the protein moieties of AGPs has mostly come from purifying AGPs, deglycosylating them and analyzing their respective core proteins by amino acid analysis and, to a more limited extent, by sequence analysis ( fig. 2) [3 -10]. More recently, molecular cloning of several confirmed and putative AGP core proteins has CMLS, Cell. Mol. Life Sci. 58 (2001) 1399 -1417 1420-682X/01/101399-19 $ 1.50 + 0.20/0 © Birkhäuser Verlag, Basel, 2001 CMLS Cellular and Molecular Life Sciences point to roles for AGPs in vegetative, reproductive, and cellular growth and development as well as programmed cell death and social control. In addition and most likely inextricably linked to their functions, AGPs are presumably involved in molecular interactions and cellular signaling at the cell surface. Some likely scenarios are discussed in this context. AGPs also have functions of real or potential commercial value, most notably as emulsifiers in the food industry and as potential immunological regulators for human health. Several important questions remain to be answered with respect to AGPs. Clearly, elucidating the unequivocal functions of particular AGPs and relating these functions to their respective structures and modes of action remain as major challenges in the years ahead.

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“…This labeling pattern is also observed in pollen tubes from plants possessing a solid style, such as species in the Solanaceae (potato [Solanum tuberosum], tobacco, and petunia [Petunia hybrida]), the Oleaceae (jasmine [Jasmium spp. ]), and the Poaceae (maize [Zea mays]; Li et al, 1994;Qin et al, 2007; for review, see Mollet et al, 2013), and those with a hollow style, such as lily (Jauh and Lord, 1996). The methylesterified HG in the apical dome of the pollen tube is thought to provide sufficient plasticity of the cell wall to sustain pollen tube growth (Chebli and Geitmann, 2007).…”

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PECTIN METHYLESTERASE48 Is Involved in Arabidopsis Pollen Grain Germination

et al. 2014

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Germination of pollen grains is a crucial step in plant reproduction. However, the molecular mechanisms involved remain unclear. We investigated the role of PECTIN METHYLESTERASE48 (PME48), an enzyme implicated in the remodeling of pectins in Arabidopsis (Arabidopsis thaliana) pollen. A combination of functional genomics, gene expression, in vivo and in vitro pollen germination, immunolabeling, and biochemical analyses was used on wild-type and Atpme48 mutant plants. We showed that AtPME48 is specifically expressed in the male gametophyte and is the second most expressed PME in dry and imbibed pollen grains. Pollen grains from homozygous mutant lines displayed a significant delay in imbibition and germination in vitro and in vivo. Moreover, numerous pollen grains showed two tips emerging instead of one in the wild type. Immunolabeling and Fourier transform infrared analyses showed that the degree of methylesterification of the homogalacturonan was higher in pme482/2 pollen grains. In contrast, the PME activity was lower in pme482/2, partly due to a reduction of PME48 activity revealed by zymogram. Interestingly, the wild-type phenotype was restored in pme482/2 with the optimum germination medium supplemented with 2.5 mM calcium chloride, suggesting that in the wild-type pollen, the weakly methylesterified homogalacturonan is a source of Ca 2+ necessary for pollen germination. Although pollen-specific PMEs are traditionally associated with pollen tube elongation, this study provides strong evidence that PME48 impacts the mechanical properties of the intine wall during maturation of the pollen grain, which, in turn, influences pollen grain germination.

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Localization of pectins and arabinogalactan-proteins in lily (Lilium longiflorum L.) pollen tube and style, and their possible roles in pollination

Abstract: In lily, adhesion of the pollen tube to the trans-

Cited by 169 publications

References 39 publications

Role of the Extensin Superfamily in Primary Cell Wall Architecture

Role of the Extensin Superfamily in Primary Cell Wall Architecture

Arabinogalactan-proteins: structure, expression and function

PECTIN METHYLESTERASE48 Is Involved in Arabidopsis Pollen Grain Germination

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