Phosphoproteomic Analysis of Paper Mulberry Reveals Phosphorylation Functions in Chilling Tolerance
文献类型:期刊论文
作者 | Pi, Zhi; Zhao, Mei-Ling; Peng, Xian-Jun; Shen, Shi-Hua![]() |
刊名 | JOURNAL OF PROTEOME RESEARCH
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出版日期 | 2017 |
卷号 | 16期号:5页码:1944-1961 |
关键词 | chilling tolerance phosphorylation paper mulberry hub protein CBF/DREB-responsive pathway |
ISSN号 | 1535-3893 |
DOI | 10.1016/j.scitotenv.2017.07.082 |
文献子类 | Article |
英文摘要 | Paper mulberry is a valuable woody species with a good chilling tolerance. In this study, phosphoproteomic analysis, physiological measurement, and mRNA quantification were employed to explore the molecular mechanism of chilling (4 degrees C) tolerance in paper mulberry. After chilling for 6 h, 427 significantly changed phosphoproteins were detected in paper mulberry seedlings without obvious physiological injury. When obvious physiological injury occurred after chilling for 48 h, a total of 611 phosphoproteins were found to be significantly changed at the phosphorylation level. Several protein kinases, especially CKII, were possibly responsible for these changes according to conserved sequence analysis. The results of Gene Ontology analysis showed that phosphoproteins were mainly responsible for signal transduction, protein modification, and translation during chilling. Additionally, transport and cellular component organization were enriched after chilling for 6 and 48 h, respectively. On the basis of the protein protein interaction network analysis, a protein kinase and phosphatases hub protein (P1959) were found to be involved in cross-talk between Ca2+, BR, ABA, and ethylene-mediated signaling pathways. We also highlighted the phosphorylation of BpSIZ1 and BpICE1 possibly impacted on the CBF/DREB-responsive pathway. From these results, we developed a schematic for the chilling tolerance mechanism at phosphorylation level. |
学科主题 | Environmental Sciences & Ecology |
出版地 | WASHINGTON |
电子版国际标准刊号 | 1535-3907 |
WOS关键词 | BLUE-LIGHT RECEPTOR ; ABSCISIC-ACID ABA ; LOW-TEMPERATURE ; CHLOROPLAST MOVEMENT ; COLD-ACCLIMATION ; QUANTITATIVE PHOSPHOPROTEOMICS ; PROTEIN-KINASE ; COMPREHENSIVE ANALYSIS ; PROTEOMIC ANALYSIS ; PROFILING REVEALS |
语种 | 英语 |
WOS记录号 | WOS:000408755300117 |
出版者 | AMER CHEMICAL SOC |
资助机构 | Poverty Relief Project of the Chinese Academy of Sciences [KFJ-FP-24] ; Huimin Technology Demonstration Project of the National Modern Agricultural Science and Technology Achievements City [Z151100001015008] ; Knowledge Innovation Program through the Chinese Academy of SciencesKnowledge Innovation Program of the Chinese Academy of Sciences [KZCX2-YW-359-2] ; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31270653] |
源URL | [http://ir.ibcas.ac.cn/handle/2S10CLM1/22072] ![]() |
专题 | 中科院北方资源植物重点实验室 |
作者单位 | 1.Zhao, Mei-Ling 2.Peng, Xian-Jun 3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 4.Chinese Acad Sci, Inst Bot, Key Lab Plant Resources, Beijing 100093, Peoples R China 5.[Pi, Zhi |
推荐引用方式 GB/T 7714 | Pi, Zhi,Zhao, Mei-Ling,Peng, Xian-Jun,et al. Phosphoproteomic Analysis of Paper Mulberry Reveals Phosphorylation Functions in Chilling Tolerance[J]. JOURNAL OF PROTEOME RESEARCH,2017,16(5):1944-1961. |
APA | Pi, Zhi,Zhao, Mei-Ling,Peng, Xian-Jun,&Shen, Shi-Hua.(2017).Phosphoproteomic Analysis of Paper Mulberry Reveals Phosphorylation Functions in Chilling Tolerance.JOURNAL OF PROTEOME RESEARCH,16(5),1944-1961. |
MLA | Pi, Zhi,et al."Phosphoproteomic Analysis of Paper Mulberry Reveals Phosphorylation Functions in Chilling Tolerance".JOURNAL OF PROTEOME RESEARCH 16.5(2017):1944-1961. |
入库方式: OAI收割
来源:植物研究所
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