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https://hdl.handle.net/2440/132646
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Type: | Journal article |
Title: | Grass-specific EPAD1 is essential for pollen exine patterning in rice |
Author: | Li, H.J. Kim, Y.J. Yang, L. Liu, Z. Zhang, J. Shi, H. Huang, G. Persson, S. Zhang, D. Liang, W. |
Citation: | The Plant Cell, 2020; 32(12):3961-3977 |
Publisher: | American Society of Plant Biologists |
Issue Date: | 2020 |
ISSN: | 1040-4651 1532-298X |
Statement of Responsibility: | HuanJun Li, Yu-Jin Kim, Liu Yang, Ze Liu, Jie Zhang, Haotian Shi ... et al. |
Abstract: | The highly variable and species-specific pollen surface patterns are formed by sporopollenin accumulation. The template for sporopollenin deposition and polymerization is the primexine that appears on the tetrad surface, but the mechanism(s) by which primexine guides exine patterning remain elusive. Here, we report that the Poaceae-specific EXINE PATTERN DESIGNER 1 (EPAD1), which encodes a nonspecific lipid transfer protein, is required for primexine integrity and pollen exine patterning in rice (Oryza sativa). Disruption of EPAD1 leads to abnormal exine pattern and complete male sterility, although sporopollenin biosynthesis is unaffected. EPAD1 is specifically expressed in male meiocytes, indicating that reproductive cells exert genetic control over exine patterning. EPAD1 possesses an N-terminal signal peptide and three redundant glycosylphosphatidylinositol (GPI)-anchor sites at its C terminus, segments required for its function and localization to the microspore plasma membrane. In vitro assays indicate that EPAD1 can bind phospholipids. We propose that plasma membrane lipids bound by EPAD1 may be involved in recruiting and arranging regulatory proteins in the primexine to drive correct exine deposition. Our results demonstrate that EPAD1 is a meiocyte-derived determinant that controls primexine patterning in rice, and its orthologs may play a conserved role in the formation of grass-specific exine pattern elements. |
Keywords: | Poaceae Flowers Pollen Carotenoids Biopolymers Carrier Proteins Plant Proteins Species Specificity Mutation Antigens, Plant Oryza |
Rights: | © 2020 ASPB. |
DOI: | 10.1105/tpc.20.00551 |
Grant ID: | http://purl.org/au-research/grants/arc/DP190101941 http://purl.org/au-research/grants/arc/FT160100218 |
Published version: | http://dx.doi.org/10.1105/tpc.20.00551 |
Appears in Collections: | Biochemistry publications |
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