The Role of Arabidopsis ABCG9 and ABCG31 ATP Binding Cassette Transporters in Pollen Fitness and the Deposition of Steryl Glycosides on the Pollen Coat

Author:

Choi Hyunju1,Ohyama Kiyoshi23,Kim Yu-Young1,Jin Jun-Young1,Lee Saet Buyl4,Yamaoka Yasuyo1,Muranaka Toshiya25,Suh Mi Chung4,Fujioka Shozo6,Lee Youngsook1

Affiliation:

1. Pohang University of Science and Technology–University of Zurich Cooperative Laboratory, Department of Integrative Bioscience and Biotechnology, Pohang University of Science and Technology, Pohang 790-784, Korea

2. RIKEN Center for Sustainable Resource Science, Tsurumi-ku, Yokohama, Kanagawa 244-0045, Japan

3. Department of Chemistry and Materials Science, Graduate School of Science and Engineering, Tokyo Institute of Technology, Meguro-ku, Tokyo 152-8551, Japan

4. Department of Bioenergy Science and Technology, College of Agriculture and Life Sciences, Chonnam National University, Gwangju 500-757, Korea

5. Department of Biotechnology, Graduate School of Engineering, Osaka University, Suita-shi, Osaka 565-0871, Japan

6. RIKEN Advanced Science Institute, Wako-shi, Saitama 351-0198, Japan

Abstract

Abstract The pollen coat protects pollen grains from harmful environmental stresses such as drought and cold. Many compounds in the pollen coat are synthesized in the tapetum. However, the pathway by which they are transferred to the pollen surface remains obscure. We found that two Arabidopsis thaliana ATP binding cassette transporters, ABCG9 and ABCG31, were highly expressed in the tapetum and are involved in pollen coat deposition. Upon exposure to dry air, many abcg9 abcg31 pollen grains shriveled up and collapsed, and this phenotype was restored by complementation with ABCG9pro:GFP:ABCG9. GFP-tagged ABCG9 or ABCG31 localized to the plasma membrane. Electron microscopy revealed that the mutant pollen coat resembled the immature coat of the wild type, which contained many electron-lucent structures. Steryl glycosides were reduced to about half of wild-type levels in the abcg9 abcg31 pollen, but no differences in free sterols or steryl esters were observed. A mutant deficient in steryl glycoside biosynthesis, ugt80A2 ugt80B1, exhibited a similar phenotype. Together, these results indicate that steryl glycosides are critical for pollen fitness, by supporting pollen coat maturation, and that ABCG9 and ABCG31 contribute to the accumulation of this sterol on the surface of pollen.

Publisher

Oxford University Press (OUP)

Subject

Cell Biology,Plant Science

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