Expression of Arabidopsis callose synthase 5 results in callose accumulation and cell wall permeability alteration

Xie, Bo; Deng, Yunfei; Kanaoka, Masahiro M.; Okada, Kiyotaka; Hong, Zonglie

doi:10.1016/j.plantsci.2011.10.015

Cited by 43 publications

(32 citation statements)

References 39 publications

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“…Callose synthase 5 (CalS5) is responsible for the synthesis of callose deposited in the primary cell wall of meiocytes, tetrads, and microspores, and expression of this gene is essential for exine formation in the pollen wall (Dong et al, 2005). Absence or overexpression of CalS5 causes aberrations in callose accumulation, exine patterning, and pollen wall permeability alterations (Chang et al, 2012;Xie et al, 2012). The expression of CalS5 increased 2.24-and 2.62-fold at stages 7-9 and stages 10-11 in the cep1 mutant, respectively, suggesting aberrant callose deposition and abnormal exine development.…”

Section: Changes In the Expression Of Genes Involved In Tapetal Cell mentioning

confidence: 99%

The Cysteine Protease CEP1, a Key Executor Involved in Tapetal Programmed Cell Death, Regulates Pollen Development in Arabidopsis

et al. 2014

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Tapetal programmed cell death (PCD) is a prerequisite for pollen grain development in angiosperms, and cysteine proteases are the most ubiquitous hydrolases involved in plant PCD. We identified a papain-like cysteine protease, CEP1, which is involved in tapetal PCD and pollen development in Arabidopsis thaliana. CEP1 is expressed specifically in the tapetum from stages 5 to 11 of anther development. The CEP1 protein first appears as a proenzyme in precursor protease vesicles and is then transported to the vacuole and transformed into the mature enzyme before rupture of the vacuole. cep1 mutants exhibited aborted tapetal PCD and decreased pollen fertility with abnormal pollen exine. A transcriptomic analysis revealed that 872 genes showed significantly altered expression in the cep1 mutants, and most of them are important for tapetal cell wall organization, tapetal secretory structure formation, and pollen development. CEP1 overexpression caused premature tapetal PCD and pollen infertility. ELISA and quantitative RT-PCR analyses confirmed that the CEP1 expression level showed a strong relationship to the degree of tapetal PCD and pollen fertility. Our results reveal that CEP1 is a crucial executor during tapetal PCD and that proper CEP1 expression is necessary for timely degeneration of tapetal cells and functional pollen formation.

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Section: Changes In the Expression Of Genes Involved In Tapetal Cell mentioning

confidence: 99%

The Cysteine Protease CEP1, a Key Executor Involved in Tapetal Programmed Cell Death, Regulates Pollen Development in Arabidopsis

et al. 2014

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“…In support of this, studies on N. tabacum pollen tube growth revealed that PM targeting of CalS occurs via endomembrane dynamics, e.g., through Golgi body and/or vesicle movement along actin filaments. In addition, (Xie et al, 2012) found that CalS5 not only localizes to the PM but also to Golgi-related endosomes, indicating that subcellular localization of CalS depends on Golgi-derived vesicle trafficking. Hence, the functional role of sterols in PD callose deposition may be related to their structural implication in PD-directed trafficking of CalS-containing endosomes.…”

Section: A Putative Role For Sterols In Modulating Callose Depositionmentioning

confidence: 99%

Callose homeostasis at plasmodesmata: molecular regulators and developmental relevance

2014

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Plasmodesmata are membrane-lined channels that are located in the plant cell wall and that physically interconnect the cytoplasm and the endoplasmic reticulum (ER) of adjacent cells. Operating as controllable gates, plasmodesmata regulate the symplastic trafficking of micro- and macromolecules, such as endogenous proteins [transcription factors (TFs)] and RNA-based signals (mRNA, siRNA, etc.), hence mediating direct cell-to-cell communication and long distance signaling. Besides this physiological role, plasmodesmata also form gateways through which viral genomes can pass, largely facilitating the pernicious spread of viral infections. Plasmodesmatal trafficking is either passive (e.g., diffusion) or active and responses both to developmental and environmental stimuli. In general, plasmodesmatal conductivity is regulated by the controlled build-up of callose at the plasmodesmatal neck, largely mediated by the antagonistic action of callose synthases (CalSs) and β-1,3-glucanases. Here, in this theory and hypothesis paper, we outline the importance of callose metabolism in PD SEL control, and highlight the main molecular factors involved. In addition, we also review other proteins that regulate symplastic PD transport, both in a developmental and stress-responsive framework, and discuss on their putative role in the modulation of PD callose turn-over. Finally, we hypothesize on the role of structural sterols in the regulation of (PD) callose deposition and outline putative mechanisms by which this regulation may occur.

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“…A 530-592-nm emission filter (red) was used to detect the Golgi apparatus stained with BODIPY TR ceramide at an excitation wavelength of 532 nm (20).…”

Section: Methodsmentioning

confidence: 99%

Cloning of a cDNA Encoding the Gly m Bd 28K Precursor and Its Vacuole Transport in Tobacco BY2 Suspension-Cultured Cells

Yumioka-Ito

Misaki

Yokoro

et al. 2014

J Nutr Sci Vitaminol

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Summary Gly m Bd 28K (Gm28K), a soybean allergen, is formed as a preproprotein consisting of a predicted signal peptide, Gm28K, and the 23-kDa peptide (Gm23K). Gm28K and Gm23K are found in the protein-storage vacuoles (PSVs) of developing soybean seeds. However, the complete structure of Gm28K has not yet been identified and its processing and transport to the vacuoles has never been clarified. In the present study, we elucidated the 5′-nucleotide sequence of cDNA encoding the Gm28K precursor and identified a putative signal peptide (SP) with 24 N-terminal amino acid residues. We expressed peptides from the Gm28K precursor as fusion proteins with enhanced green fluorescent protein (EGFP) in tobacco BY2 suspension-cultured cells. BY2 cells transformed by an expression vector for SP-EGFP-Gm28-Gm23K (SP-EGFP-Gm28-Gm23K/BY2 cells) and SP-Gm28-Gm23K-EGFP/ BY2 cells produced the EGFP fused-Gm28K precursor, and the EGFP-fluorescence in their vacuoles were recorded. In the experiments with SP-EGFP/BY2 and SP-EGFP-Gm28K/BY2 cells, large amounts of the EGFP segments were secreted into the medium. On the other hand, the fluorescence of EGFP in SP-EGFP-Gm23K/BY2 cells was shown to accumulate only in the endoplasmic reticulum without secretion into the medium. These findings show that the SP signals the precursor to enter the lumen of the endoplasmic reticulum and that both the Gm28K and Gm23K components may be involved in the transport from the endoplasmic reticulum (ER) lumen via the Golgi to the vacuoles in a proprotein form. Key Words soybean allergen, Gly m Bd28K, 23-kDa peptide, signal peptide, vacuole E-mail: yumioka@icb.osaka-u.ac.jp The new nucleotide sequence of the 5′-nucleotide sequence region of cDNA encoding the Gly m Bd 28K precursor elucidated in the present study was registered under accession number AB046874.2 on DDBJ.

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Expression of Arabidopsis callose synthase 5 results in callose accumulation and cell wall permeability alteration

Cited by 43 publications

References 39 publications

The Cysteine Protease CEP1, a Key Executor Involved in Tapetal Programmed Cell Death, Regulates Pollen Development in Arabidopsis

The Cysteine Protease CEP1, a Key Executor Involved in Tapetal Programmed Cell Death, Regulates Pollen Development in Arabidopsis

Callose homeostasis at plasmodesmata: molecular regulators and developmental relevance

Cloning of a cDNA Encoding the Gly m Bd 28K Precursor and Its Vacuole Transport in Tobacco BY2 Suspension-Cultured Cells

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