文献类型： 外文期刊

作者： Zhang, Bin ¹ ; Guo, Mingliang ¹ ; Liu, Xiangpei ¹ ; Zhang, Bintao ¹ ; Cui, Yan ¹ ; Cao, Xinglan ¹ ; Zhang, Zhipeng ¹ ; Shi, Chuanlin ¹ ; Wei, Hua ¹ ; He, Huiying ¹ ; Zhang, Hong ¹ ; Zhu, Yiwang ¹ ; Wang, Xianmeng ¹ ; Lv, Yang ¹ ; Yu, Xiaoman ¹ ; Chen, Dandan ¹ ; Yuan, Qiaoling ¹ ; Teng, Sheng ³ ; Sun, Tongjun ¹ ; Qian, Qian ¹ ; Shang, Lianguang ¹ ;

作者机构： 1.Chinese Acad Agr Sci, Agr Genom Inst Shenzhen, Minist Agr & Rural Affairs, Shenzhen Branch,Guangdong Lab Lingnan Modern Agr,G, Shenzhen 518124, Peoples R China

2.Yazhouwan Natl Lab, 8 Huanjin Rd, Sanya City 572024, Hainan Province, Peoples R China

3.China Jiliang Univ, Coll Life Sci, Key Lab Microbiol Metrol Measurement & Bioprod Qua, State Adm Market Regulat, Hangzhou 310018, Peoples R China

4.China Natl Rice Res Inst, State Key Lab Rice Biol, Hangzhou 310000, Zhejiang, Peoples R China

5.Chinese Acad Agr Sci, Nanfan Res Inst, Sanya 572024, Hainan, Peoples R China

关键词： crop genetics; molecular biology; disease resistance; glycosylation modification

期刊名称：JOURNAL OF INTEGRATIVE PLANT BIOLOGY （ 影响因子：9.3； 五年影响因子：10.8 ）

ISSN： 1672-9072

年卷期： 2025 年 67 卷 2 期

页码：

收录情况： SCI

摘要： Glycosylation, a prevalent post-translational modification in eukaryotic secreted and membrane-associated proteins, plays a pivotal role in diverse physiological and pathological processes. Although UDP-N-acetylglucosamine (UDP-GlcNAc) is essential for this modification, the specific glycosylation mechanisms during plant leaf senescence and defense responses remain poorly understood. In our research, we identified a novel rice mutant named rbb1 (resistance to blast and bacterial blight1), exhibiting broad-spectrum disease resistance. This mutant phenotype results from a loss-of-function mutation in the gene encoding glucosamine-6-phosphate acetyltransferase, an important enzyme in D-glucosamine 6-phosphate acetylation. The rbb1 mutant demonstrates enhanced defense responses, evident in increased resistance to rice blast and bacterial blight, along with the upregulation of defense-response genes. Various biochemical markers indicate an activated defense mechanism in the rbb1 mutant, such as elevated levels of reactive oxygen species and malondialdehyde, reduced enzyme activity and UDP-GlcNAc content, and decreased expression of N-glycan and O-glycan modifying proteins. Moreover, proteome analysis of N-glycosylation modifications reveals alterations in the N-glycosylation of several disease-resistance-related proteins, with a significant reduction in Prx4 and Prx13 in rbb1-1. Additionally, the knockout of Prx4 or Prx13 also enhances resistance to Xanthomonas oryzae pv. oryzae (Xoo) and Magnaporthe oryzae (M. oryzae). This study uncovers a novel mechanism of defense response in rice, suggesting potential targets for the development of disease-resistant varieties.