Microspore-expressed SCULP1 is required for p-coumaroylation of sporopollenin, exine integrity, and pollen development in wheat
文献类型： 外文期刊
作者： Xu, Lei 1 ; Tang, Yimiao 3 ; Yang, Yanzhi 1 ; Wang, Dezhou 3 ; Wang, Haijun 1 ; Du, Jianmei 1 ; Bai, Yajun 1 ; Su, Shichao 3 ; Zhao, Changping 3 ; Li, Lei 1 ;
作者机构： 1.Peking Univ, Sch Adv Agr Sci, State Key Lab Prot & Plant Gene Res, Beijing 100871, Peoples R China
2.Peking Univ, Acad Adv Interdisciplinary Studies, Peking Tsinghua Ctr Life Sci, Beijing 100871, Peoples R China
3.Beijing Acad Agr & Forestry Sci, Inst Hybrid Wheat, Beijing 100097, Peoples R China
关键词： exine; multicopper oxidase; pollen; sporopollenin; wheat
期刊名称：NEW PHYTOLOGIST （ 影响因子：9.4； 五年影响因子：10.5 ）
ISSN： 0028-646X
年卷期： 2023 年 239 卷 1 期
页码：
收录情况： SCI
摘要： Sporopollenin is one of the most structurally sophisticated and chemically recalcitrant biopolymers. In higher plants, sporopollenin is the dominant component of exine, the outer wall of pollen grains, and contains covalently linked phenolics that protect the male gametes from harsh environments. Although much has been learned about the biosynthesis of sporopollenin precursors in the tapetum, the nutritive cell layer surrounding developing microspores, little is known about how the biopolymer is assembled on the microspore surface.We identified SCULP1 (SKS clade universal in pollen) as a seed plant conserved clade of the multicopper oxidase family. We showed that SCULP1 in common wheat (Triticum aestivum) is specifically expressed in the microspore when sporopollenin assembly takes place, localized to the developing exine, and binds p-coumaric acid in vitro.Through genetic, biochemical, and 3D reconstruction analyses, we demonstrated that SCULP1 is required for p-coumaroylation of sporopollenin, exine integrity, and pollen viability. Moreover, we found that SCULP1 accumulation is compromised in thermosensitive genic male sterile wheat lines and its expression partially restored exine integrity and male fertility.These findings identified a key microspore protein in autonomous sporopollenin polymer assembly, thereby laying the foundation for elucidating and engineering sporopollenin biosynthesis.
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