The N-terminal acetyltransferase Naa50 regulates tapetum degradation and pollen development in Arabidopsis.


Journal

Plant science : an international journal of experimental plant biology
ISSN: 1873-2259
Titre abrégé: Plant Sci
Pays: Ireland
ID NLM: 9882015

Informations de publication

Date de publication:
Mar 2022
Historique:
received: 03 09 2021
revised: 05 01 2022
accepted: 10 01 2022
entrez: 13 2 2022
pubmed: 14 2 2022
medline: 16 2 2022
Statut: ppublish

Résumé

The N-terminal acetylation of proteins is a key modification in eukaryotes. However, knowledge of the biological function of N-terminal acetylation modification of proteins in plants is limited. Naa50 is the catalytic subunit of the N-terminal acetyltransferase NatE complex. We previously demonstrated that the absence of Naa50 leads to sterility in Arabidopsis thaliana. In the present study, the lack of Naa50 resulted in collapsed and sterile pollen in Arabidopsis. Further experiments showed that the mutation in Naa50 accelerated programmed cell death in the tapetum. Expression pattern analysis revealed the specific expression of Naa50 in the tapetum cells of anthers at 9-11 stages during pollen development, when tapetal programmed cell death occurred. Reciprocal cross analyses indicated that male sterility in naa50 is caused by sporophytic effects. mRNA sequencing and quantitative PCR of the closed buds showed that the deletion of Naa50 resulted in the upregulation of the cysteine protease coding gene CEP1 and impaired the expression of several genes involved in pollen wall deposition and pollen mitotic division. The collective data suggest that Naa50 balances the degradation of tapetum cells during anther development and plays an important role in pollen development by affecting several pathways.

Identifiants

pubmed: 35151444
pii: S0168-9452(22)00004-8
doi: 10.1016/j.plantsci.2022.111180
pii:
doi:

Substances chimiques

Arabidopsis Proteins 0
AT5G11340 protein, Arabidopsis EC 2.3.1.258
N-Terminal Acetyltransferase E EC 2.3.1.258
N-Terminal Acetyltransferases EC 2.3.1.88

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

111180

Informations de copyright

Copyright © 2022 Elsevier B.V. All rights reserved.

Auteurs

Jinlin Feng (J)

College of Life Sciences, Shanxi Normal University, Taiyuan, 030000 Shanxi, China; Higher Education Key Laboratory of Plant Molecular and Environment Stress Response (Shanxi Normal University) in Shanxi Province, Taiyuan, 030000 Shanxi, China. Electronic address: jinlin_feng@163.com.

Minghui Qin (M)

College of Life Sciences, Shanxi Normal University, Taiyuan, 030000 Shanxi, China; Higher Education Key Laboratory of Plant Molecular and Environment Stress Response (Shanxi Normal University) in Shanxi Province, Taiyuan, 030000 Shanxi, China.

Lixia Yao (L)

College of Life Sciences, Shanxi Normal University, Taiyuan, 030000 Shanxi, China; Higher Education Key Laboratory of Plant Molecular and Environment Stress Response (Shanxi Normal University) in Shanxi Province, Taiyuan, 030000 Shanxi, China.

Yan Li (Y)

College of Life Sciences, Capital Normal University, Beijing, 100048, China.

Rong Han (R)

College of Life Sciences, Shanxi Normal University, Taiyuan, 030000 Shanxi, China; Higher Education Key Laboratory of Plant Molecular and Environment Stress Response (Shanxi Normal University) in Shanxi Province, Taiyuan, 030000 Shanxi, China.

Ligeng Ma (L)

College of Life Sciences, Capital Normal University, Beijing, 100048, China. Electronic address: ligeng.ma@cnu.edu.cn.

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Classifications MeSH