Dynamic proteome and acetylome profiling reveals key regulators of sucrose accumulation in sugarcane.

IF 5.3 2区 生物学 Q1 PLANT SCIENCES
Miao Wang, Ao-Mei Li, Zhong-Liang Chen, Cui-Xian Qin, Fen Liao, You-Qiang Pan, Prakash Lakshmanan, Xiao-Feng Li, Dong-Liang Huang
{"title":"Dynamic proteome and acetylome profiling reveals key regulators of sucrose accumulation in sugarcane.","authors":"Miao Wang, Ao-Mei Li, Zhong-Liang Chen, Cui-Xian Qin, Fen Liao, You-Qiang Pan, Prakash Lakshmanan, Xiao-Feng Li, Dong-Liang Huang","doi":"10.1007/s00299-025-03449-2","DOIUrl":null,"url":null,"abstract":"<p><strong>Key message: </strong>Lysine acetylation and protein abundance both play crucial roles in regulating sucrose accumulation in sugarcane, with 73 dual-function proteins identified as potential targets for molecular breeding to enhance sucrose levels. Lysine acetylation plays a crucial role in regulating various biological processes in plants, but its role in sucrose accumulation in sugarcane remains unexplored In this study, we conducted a comprehensive quantitative proteome and acetylated proteome analysis on the leaves of two sugarcane genotypes with high and low sucrose levels at early, middle, and late stages of sucrose accumulation. Quantitative proteome analysis identified 2363 differentially abundant proteins (DAPs), of which 165 were associated with sugar metabolism pathways, providing more targets for improving sucrose content in sugarcane. The acetylated proteome analysis identified 1397 differentially acetylated proteins (DAcPs) with 2377 acetylation sites. Many DAcPs were also involved in sugar metabolism, demonstrating that lysine acetylation is associated with sucrose accumulation. A comparison of the DAPs and DAcPs identified 650 overlapping proteins, with 73 of them related to sugar metabolism, confirming dual regulatory roles of protein abundance and acetylation in sucrose accumulation in sugarcane. These 73 proteins serve as targets for sucrose improvement with dual regulatory effects. Our data also suggest that histone acetylation and nitrogen metabolism may be related to sucrose accumulation. This work enhances our understanding of the mechanisms regulating sucrose accumulation and proposes targets for improving sucrose content in sugarcane through molecular breeding.</p>","PeriodicalId":20204,"journal":{"name":"Plant Cell Reports","volume":"44 4","pages":"74"},"PeriodicalIF":5.3000,"publicationDate":"2025-03-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Plant Cell Reports","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1007/s00299-025-03449-2","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"PLANT SCIENCES","Score":null,"Total":0}
引用次数: 0

Abstract

Key message: Lysine acetylation and protein abundance both play crucial roles in regulating sucrose accumulation in sugarcane, with 73 dual-function proteins identified as potential targets for molecular breeding to enhance sucrose levels. Lysine acetylation plays a crucial role in regulating various biological processes in plants, but its role in sucrose accumulation in sugarcane remains unexplored In this study, we conducted a comprehensive quantitative proteome and acetylated proteome analysis on the leaves of two sugarcane genotypes with high and low sucrose levels at early, middle, and late stages of sucrose accumulation. Quantitative proteome analysis identified 2363 differentially abundant proteins (DAPs), of which 165 were associated with sugar metabolism pathways, providing more targets for improving sucrose content in sugarcane. The acetylated proteome analysis identified 1397 differentially acetylated proteins (DAcPs) with 2377 acetylation sites. Many DAcPs were also involved in sugar metabolism, demonstrating that lysine acetylation is associated with sucrose accumulation. A comparison of the DAPs and DAcPs identified 650 overlapping proteins, with 73 of them related to sugar metabolism, confirming dual regulatory roles of protein abundance and acetylation in sucrose accumulation in sugarcane. These 73 proteins serve as targets for sucrose improvement with dual regulatory effects. Our data also suggest that histone acetylation and nitrogen metabolism may be related to sucrose accumulation. This work enhances our understanding of the mechanisms regulating sucrose accumulation and proposes targets for improving sucrose content in sugarcane through molecular breeding.

动态蛋白质组和乙酰基组分析揭示了甘蔗蔗糖积累的关键调控因子。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
Plant Cell Reports
Plant Cell Reports 生物-植物科学
CiteScore
10.80
自引率
1.60%
发文量
135
审稿时长
3.2 months
期刊介绍: Plant Cell Reports publishes original, peer-reviewed articles on new advances in all aspects of plant cell science, plant genetics and molecular biology. Papers selected for publication contribute significant new advances to clearly identified technological problems and/or biological questions. The articles will prove relevant beyond the narrow topic of interest to a readership with broad scientific background. The coverage includes such topics as: - genomics and genetics - metabolism - cell biology - abiotic and biotic stress - phytopathology - gene transfer and expression - molecular pharming - systems biology - nanobiotechnology - genome editing - phenomics and synthetic biology The journal also publishes opinion papers, review and focus articles on the latest developments and new advances in research and technology in plant molecular biology and biotechnology.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信