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BTB-BACK Domain E3 Ligase MdPOB1 Suppresses Plant Pathogen Defense against Botryosphaeria dothidea by Ubiquitinating and Degrading MdPUB29 Protein in Apple  ( SCI-EXPANDED收录)   被引量:28

文献类型:期刊文献

英文题名:BTB-BACK Domain E3 Ligase MdPOB1 Suppresses Plant Pathogen Defense against Botryosphaeria dothidea by Ubiquitinating and Degrading MdPUB29 Protein in Apple

作者:Han, Peng-Liang[1] Wang, Chu-Kun[1] Liu, Xiao-Juan[2] Dong, Yuan-Hua[1] Jiang, Han[3] Hu, Da-Gang[1] Hao, Yu-Jin[1]

第一作者:Han, Peng-Liang

通信作者:Hu, DG[1];Hao, YJ[1]

机构:[1]Shandong Agr Univ, Coll Hort Sci & Engn, Natl Key Lab Crop Biol, MOA Key Lab Hort Crop Biol & Germplasm Innovat, Tai An 271018, Shandong, Peoples R China;[2]Chinese Acad Forestry, Res Inst Forestry, Beijing 100091, Peoples R China;[3]Northwest A&F Univ, Coll Hort, Shaanxi Key Lab Apple, State Key Lab Crop Stress Biol Arid Areas, Yangling 712100, Shaanxi, Peoples R China

年份:2019

卷号:60

期号:10

起止页码:2129-2140

外文期刊名:PLANT AND CELL PHYSIOLOGY

收录:;Scopus(收录号:2-s2.0-85073183767);WOS:【SCI-EXPANDED(收录号:WOS:000504330500002)】;

基金:The National Key Research and Development Program [2018YFD1000200]; National Natural Science Foundation of China [31601728]; Ministry of Education of China [IRT15R42]; Shandong Province [ZR2016CQ13 and SDAIT-06-03]; and Nanjing Agricultural University [ZW201805].

语种:英文

外文关键词:Apple; B; dothidea; BTB-BACK domain; E3 ligase; MdPOB1; MdPUB29

摘要:Apple ring rot is a severe disease that affects the yield and quality of apple fruits worldwide. However, the underlying molecular mechanism that involved in this process still remains largely unexplored. Here, we report that apple POZ/BTB CONTAINING-PROTEIN 1 (MdPOB1), a BTB-BACK domain E3 ligase protein, functions to suppress apple pathogen defense against Botryosphaeria dothidea (B. dothidea). Both in vitro and in vivo assays indicated that MdPOB1 interacted directly with and degraded apple U-box E3 ligase MdPUB29, a well-established positive regulator of plant innate immunity, through the ubiquitin/26S proteasome pathway. A series of transgenic analyses in apple fruits demonstrated that MdPOB1 affected apple pathogen defense against B. dothidea at least partially, if not completely, via regulating MdPUB29. Additionally, it was found that the apple pathogen defense against B. dothidea was correlated with the H2O2 contents and the relative expression of salicylic acid (SA) synthesis- and SA signaling-related genes, which might be regulated via degradation of MdPUB29 by MdPOB1. Overall, our findings provide new insights into the mechanism of the MdPOB1 modulation of apple ring rot resistance, which occur by directly regulating potential downstream target protein MdPUB29 for proteasomal degradation in apple.

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