Tapetal 3-Ketoacyl-Coenzyme A Synthases Are Involved in Pollen Coat Lipid Accumulation for Pollen-Stigma Interaction in Arabidopsis

Pollen coat lipids form an outer barrier to protect pollen itself and play essential roles in pollen-stigma interaction. However, the precise molecular mechanisms underlying the production, deposition, regulation, and function of pollen coat lipids during anther development remain largely elusive. I...

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Autores principales:	Zaibao Zhang, Huadong Zhan, Jieyang Lu, Shuangxi Xiong, Naiying Yang, Hongyu Yuan, Zhong-Nan Yang
Formato:	article
Lenguaje:	EN
Publicado:	Frontiers Media S.A. 2021
Materias:	pollen coat lipid 3-ketoacyl-coenzyme A synthase pollen hydration anther very long chain fatty acid Plant culture SB1-1110
Acceso en línea:	https://doaj.org/article/f4a0227fb2da42e78cfd3245ec0bc2b3
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spelling	oai:doaj.org-article:f4a0227fb2da42e78cfd3245ec0bc2b32021-11-30T13:48:29ZTapetal 3-Ketoacyl-Coenzyme A Synthases Are Involved in Pollen Coat Lipid Accumulation for Pollen-Stigma Interaction in Arabidopsis1664-462X10.3389/fpls.2021.770311https://doaj.org/article/f4a0227fb2da42e78cfd3245ec0bc2b32021-11-01T00:00:00Zhttps://www.frontiersin.org/articles/10.3389/fpls.2021.770311/fullhttps://doaj.org/toc/1664-462XPollen coat lipids form an outer barrier to protect pollen itself and play essential roles in pollen-stigma interaction. However, the precise molecular mechanisms underlying the production, deposition, regulation, and function of pollen coat lipids during anther development remain largely elusive. In lipid metabolism, 3-ketoacyl-coenzyme A synthases (KCS) are involved in fatty acid elongation or very-long-chain fatty acid (VLCFA) synthesis. In this study, we identified six members of the Arabidopsis KCS family expressed in anther. Among them, KCS7, KCS15, and KCS21 were expressed in tapetal cells at anther stages 8–10. Further analysis demonstrated that they act downstream of male sterility 1 (MS1), a regulator of late tapetum development. The kcs7/15/21 triple mutant is fertile. Both cellular observation and lipid staining showed pollen coat lipid was decreased in kcs7/15/21 triple mutant. After landing on stigma, the wild-type pollen grains were hydrated for about 5 min while the kcs7/15/21 triple mutant pollen took about 10 min to hydrate. Pollen tube growth of the triple mutant was also delayed. These results demonstrate that the tapetum-localized KCS proteins are involved in the accumulation of pollen coat lipid and reveal the roles of tapetal-derived pollen coat lipid for pollen-stigma interaction.Zaibao ZhangZaibao ZhangHuadong ZhanHuadong ZhanJieyang LuShuangxi XiongNaiying YangHongyu YuanZhong-Nan YangFrontiers Media S.A.articlepollen coatlipid3-ketoacyl-coenzyme A synthasepollen hydrationanthervery long chain fatty acidPlant cultureSB1-1110ENFrontiers in Plant Science, Vol 12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	pollen coat lipid 3-ketoacyl-coenzyme A synthase pollen hydration anther very long chain fatty acid Plant culture SB1-1110
spellingShingle	pollen coat lipid 3-ketoacyl-coenzyme A synthase pollen hydration anther very long chain fatty acid Plant culture SB1-1110 Zaibao Zhang Zaibao Zhang Huadong Zhan Huadong Zhan Jieyang Lu Shuangxi Xiong Naiying Yang Hongyu Yuan Zhong-Nan Yang Tapetal 3-Ketoacyl-Coenzyme A Synthases Are Involved in Pollen Coat Lipid Accumulation for Pollen-Stigma Interaction in Arabidopsis
description	Pollen coat lipids form an outer barrier to protect pollen itself and play essential roles in pollen-stigma interaction. However, the precise molecular mechanisms underlying the production, deposition, regulation, and function of pollen coat lipids during anther development remain largely elusive. In lipid metabolism, 3-ketoacyl-coenzyme A synthases (KCS) are involved in fatty acid elongation or very-long-chain fatty acid (VLCFA) synthesis. In this study, we identified six members of the Arabidopsis KCS family expressed in anther. Among them, KCS7, KCS15, and KCS21 were expressed in tapetal cells at anther stages 8–10. Further analysis demonstrated that they act downstream of male sterility 1 (MS1), a regulator of late tapetum development. The kcs7/15/21 triple mutant is fertile. Both cellular observation and lipid staining showed pollen coat lipid was decreased in kcs7/15/21 triple mutant. After landing on stigma, the wild-type pollen grains were hydrated for about 5 min while the kcs7/15/21 triple mutant pollen took about 10 min to hydrate. Pollen tube growth of the triple mutant was also delayed. These results demonstrate that the tapetum-localized KCS proteins are involved in the accumulation of pollen coat lipid and reveal the roles of tapetal-derived pollen coat lipid for pollen-stigma interaction.
format	article
author	Zaibao Zhang Zaibao Zhang Huadong Zhan Huadong Zhan Jieyang Lu Shuangxi Xiong Naiying Yang Hongyu Yuan Zhong-Nan Yang
author_facet	Zaibao Zhang Zaibao Zhang Huadong Zhan Huadong Zhan Jieyang Lu Shuangxi Xiong Naiying Yang Hongyu Yuan Zhong-Nan Yang
author_sort	Zaibao Zhang
title	Tapetal 3-Ketoacyl-Coenzyme A Synthases Are Involved in Pollen Coat Lipid Accumulation for Pollen-Stigma Interaction in Arabidopsis
title_short	Tapetal 3-Ketoacyl-Coenzyme A Synthases Are Involved in Pollen Coat Lipid Accumulation for Pollen-Stigma Interaction in Arabidopsis
title_full	Tapetal 3-Ketoacyl-Coenzyme A Synthases Are Involved in Pollen Coat Lipid Accumulation for Pollen-Stigma Interaction in Arabidopsis
title_fullStr	Tapetal 3-Ketoacyl-Coenzyme A Synthases Are Involved in Pollen Coat Lipid Accumulation for Pollen-Stigma Interaction in Arabidopsis
title_full_unstemmed	Tapetal 3-Ketoacyl-Coenzyme A Synthases Are Involved in Pollen Coat Lipid Accumulation for Pollen-Stigma Interaction in Arabidopsis
title_sort	tapetal 3-ketoacyl-coenzyme a synthases are involved in pollen coat lipid accumulation for pollen-stigma interaction in arabidopsis
publisher	Frontiers Media S.A.
publishDate	2021
url	https://doaj.org/article/f4a0227fb2da42e78cfd3245ec0bc2b3
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Tapetal 3-Ketoacyl-Coenzyme A Synthases Are Involved in Pollen Coat Lipid Accumulation for Pollen-Stigma Interaction in Arabidopsis

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