MS32 -regulated timing of callose degradation during microsporogenesis in Arabidopsis is associated with the accumulation of stacked rough ER in tapetal cells

Fei, Houman; Sawhney, V. K.

doi:10.1007/s004970050191

Cited by 34 publications

(30 citation statements)

References 23 publications

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“…Bar 25 lm identified as callose, and an inner more electron dense aqueous layer. Although seen consistently in this and other studies (Peirson et al 1996), the aqueous layer adjacent to the callose wall may be an artifact of fixation (Fei and Sawhney 1999). No LeGRP92 protein was detected in the aqueous layer of the MMCs and tetrads.…”

Section: Legrp92 Localized To the Tapetum Tetrads And Microsporessupporting

confidence: 76%

A glycine-rich protein that facilitates exine formation during tomato pollen development

McNeil

Smith

2009

Planta

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Formation of the unique and highly diverse outer cell wall, or exine, of pollen is essential for normal pollen function and survival. However, little is known about the many contributing proteins and processes involved in the formation of this wall. The tomato gene LeGRP92 encodes for a glycine-rich protein produced specifically in the tapetum. LeGRP92 is found as four major forms that accumulate differentially in protein extracts from stamens at different developmental stages. The three largest molecular weight forms accumulated during early microspore development, while the smallest molecular weight form of LeGRP92 was present in protein extracts from stamens from early microsporogenesis through anther dehiscence, and was the only form present in dehisced pollen. Light microscopy immunolocalization experiments detected LeGRP92 at only two stages, late tetrad and early free microspore. However, we observed accumulation of the LeGRP92 at the early tetrad stage of development by removing the callose wall from tetrads, which allowed LeGRP92 detection. Transmission electron microscopy confirmed the LeGRP92 accumulation from microspore mother cells, tetrads through anther dehiscence. It was observed in the callose surrounding the microspore mother cells and tetrads, the exine of microspores and mature pollen, and orbicules. Plants expressing antisense RNA had reduced levels of LeGRP92 mRNA and protein, which correlated to pollen with altered exine formation and reduced pollen viability and germination. These data suggest that the LeGRP92 has a role in facilitating sporopollenin deposition and uniform exine formation and pollen viability.

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Section: Legrp92 Localized To the Tapetum Tetrads And Microsporessupporting

confidence: 76%

A glycine-rich protein that facilitates exine formation during tomato pollen development

McNeil

Smith

2009

Planta

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“…Tapetal cells secrete large amounts of proteins and lipids to the surface of pollen cells (Hsieh and Huang, 2007). Ultrastructural analyses have shown the presence of extensive layers of ER with dilation in tapetal cells of Arabidopsis and other plant species (Owen and Makaroff, 1995;Fei and Sawhney, 1999;Papini et al, 1999;Zheng et al, 2003). Thus, it appears likely that aspects of the ER stress response are important in the development and function of such secretory cells.…”

Section: Discussionmentioning

confidence: 99%

Arabidopsis bZIP60 Is a Proteolysis-Activated Transcription Factor Involved in the Endoplasmic Reticulum Stress Response

2008

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Proteins synthesized in the endoplasmic reticulum (ER) of eukaryotic cells must be folded correctly before translocation out of the ER. Disruption of protein folding results in the induction of genes for ER-resident chaperones, for example, BiP. This phenomenon is known as the ER stress response. We report here that bZIP60, an Arabidopsis thaliana basic leucine zipper (bZIP) transcription factor with a transmembrane domain, is involved in the ER stress response. When compared with wildtype Arabidopsis plants, homozygous bzip60 mutant plants show a markedly weaker induction of many ER stressresponsive genes. The bZIP60 protein resides in the ER membrane under unstressed condition and is cleaved in response to ER stress caused by either tunicamycin or DTT. The N-terminal fragment containing the bZIP domain is then translocated into the nucleus. Cleavage of bZIP60 is independent of the function of Arabidopsis homologs of mammalian S1P and S2P proteases, which mediate the proteolytic cleavage of the mammalian transcription factor ATF6. In Arabidopsis, expression of the bZIP60 gene and cleavage of the bZIP60 protein are observed in anthers in the absence of stress treatment, suggesting that the ER stress response functions in the normal development of active secretory cells.

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“…Some authors were able to relate rER abundance and unusual configurations in the cytoplasm of tapetal cells with tapetum and/or mmc abortion. For example, Fei and Sawhney (1999) related the presence of extensive stacks of rER in tapetal cells of Arabidopsis thaliana male sterile32 (ms32) with early callose dissolution and ultimately with mmc abortion. Similarly, Suzuki et al (2001) hypothesized that the abnormal arrangement of rER in tapetal cells under high temperatures negatively affects the function of those cells.…”

Section: Male-sterility: Tapetummentioning

confidence: 99%

Comparative microsporangium development in male‐fertile and male‐sterile flowers ofConsolea(Cactaceae): When and how does pollen abortion occur

Strittmatter

Negrón-Ortiz

Hickey

2006

Grana

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MS32 -regulated timing of callose degradation during microsporogenesis in Arabidopsis is associated with the accumulation of stacked rough ER in tapetal cells

Cited by 34 publications

References 23 publications

A glycine-rich protein that facilitates exine formation during tomato pollen development

A glycine-rich protein that facilitates exine formation during tomato pollen development

Arabidopsis bZIP60 Is a Proteolysis-Activated Transcription Factor Involved in the Endoplasmic Reticulum Stress Response

Comparative microsporangium development in male‐fertile and male‐sterile flowers ofConsolea(Cactaceae): When and how does pollen abortion occur

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