中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
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
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
DOI10.1016/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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