Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Zhang, Zaibao, Zhan, Huadong, Lu, Jieyang, Xiong, Shuangxi, Yang, Naiying, Yuan, Hongyu, Yang, Zhong-Nan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8650583/
https://www.ncbi.nlm.nih.gov/pubmed/34887893
http://dx.doi.org/10.3389/fpls.2021.770311
_version_ 1784611228549644288
author Zhang, Zaibao
Zhan, Huadong
Lu, Jieyang
Xiong, Shuangxi
Yang, Naiying
Yuan, Hongyu
Yang, Zhong-Nan
author_facet Zhang, Zaibao
Zhan, Huadong
Lu, Jieyang
Xiong, Shuangxi
Yang, Naiying
Yuan, Hongyu
Yang, Zhong-Nan
author_sort Zhang, Zaibao
collection PubMed
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 Online
Article
Text
id pubmed-8650583
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher Frontiers Media S.A.
record_format MEDLINE/PubMed
spelling pubmed-86505832021-12-08 Tapetal 3-Ketoacyl-Coenzyme A Synthases Are Involved in Pollen Coat Lipid Accumulation for Pollen-Stigma Interaction in Arabidopsis Zhang, Zaibao Zhan, Huadong Lu, Jieyang Xiong, Shuangxi Yang, Naiying Yuan, Hongyu Yang, Zhong-Nan Front Plant Sci Plant Science 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. Frontiers Media S.A. 2021-11-23 /pmc/articles/PMC8650583/ /pubmed/34887893 http://dx.doi.org/10.3389/fpls.2021.770311 Text en Copyright © 2021 Zhang, Zhan, Lu, Xiong, Yang, Yuan and Yang. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Zhang, Zaibao
Zhan, Huadong
Lu, Jieyang
Xiong, Shuangxi
Yang, Naiying
Yuan, Hongyu
Yang, Zhong-Nan
Tapetal 3-Ketoacyl-Coenzyme A Synthases Are Involved in Pollen Coat Lipid Accumulation for Pollen-Stigma Interaction in Arabidopsis
title 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_short 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
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8650583/
https://www.ncbi.nlm.nih.gov/pubmed/34887893
http://dx.doi.org/10.3389/fpls.2021.770311
work_keys_str_mv AT zhangzaibao tapetal3ketoacylcoenzymeasynthasesareinvolvedinpollencoatlipidaccumulationforpollenstigmainteractioninarabidopsis
AT zhanhuadong tapetal3ketoacylcoenzymeasynthasesareinvolvedinpollencoatlipidaccumulationforpollenstigmainteractioninarabidopsis
AT lujieyang tapetal3ketoacylcoenzymeasynthasesareinvolvedinpollencoatlipidaccumulationforpollenstigmainteractioninarabidopsis
AT xiongshuangxi tapetal3ketoacylcoenzymeasynthasesareinvolvedinpollencoatlipidaccumulationforpollenstigmainteractioninarabidopsis
AT yangnaiying tapetal3ketoacylcoenzymeasynthasesareinvolvedinpollencoatlipidaccumulationforpollenstigmainteractioninarabidopsis
AT yuanhongyu tapetal3ketoacylcoenzymeasynthasesareinvolvedinpollencoatlipidaccumulationforpollenstigmainteractioninarabidopsis
AT yangzhongnan tapetal3ketoacylcoenzymeasynthasesareinvolvedinpollencoatlipidaccumulationforpollenstigmainteractioninarabidopsis