Subcellular proteome profiles of different latex fractions revealed washed solutions from rubber particles contain crucial enzymes for natural rubber biosynthesis
文献类型: 外文期刊
作者: Wang, Dan 1 ; Sun, Yong 1 ; Chang, Lili 1 ; Tong, Zheng 1 ; Xie, Quanliang 1 ; Jin, Xiang 1 ; Zhu, Liping 1 ; He, Peng 4 ; L 1 ;
作者机构: 1.Chinese Acad Trop Agr Sci, Inst Trop Biosci & Biotechnol, Haikou 571101, Hainan, Peoples R China
2.Hainan Normal Univ, Minist Educ, Key Lab Ecol Trop Isl, Coll Life Sci, Haikou 571158, Hainan, Peoples R China
3.Shihezi Univ, Key Lab Agrobiotechnol, Coll Life Sci, Shihezi 832003, Xinjiang, Peoples R China
4.Chinese Acad Trop Agr Sci, Rubber Res Inst, Danzhou 571737, Hainan, Peoples R China
关键词: Hevea brasiliensis; Natural rubber biosynthesis; Rubber latex; Rubber particles; Subcellular proteomics; Washing solutions
期刊名称:JOURNAL OF PROTEOMICS ( 影响因子:4.044; 五年影响因子:4.02 )
ISSN: 1874-3919
年卷期: 2018 年 182 卷
页码:
收录情况: SCI
摘要: Rubber particle (RP) is a specific organelle for natural rubber biosynthesis (NRB) and storage in rubber tree Hevea brasiliensis. NRB is processed by RP membrane-localized proteins, which were traditionally purified by repeated washing. However, we noticed many proteins in the discarded washing solutions (WS) from RP. Here, we compared the proteome profiles of WS, C-serum (CS) and RP by 2-DE, and identified 233 abundant proteins from WS by mass spectrometry. Many spots on 2-DE gels were identified as different protein species. We further performed shotgun analysis of CS, WS and RP and identified 1837, 1799 and 1020 unique proteins, respectively. Together with 2-DE, we finally identified 1825 proteins from WS, 246 were WS-specific. These WS-specific proteins were annotated in Gene Ontology, indicating most abundant pathways are organic substance metabolic process, protein degradation, primary metabolic process, and energy metabolism. Protein-protein interaction analysis revealed these WS-specific proteins are mainly involved in ribosomal metabolism, proteasome system, vacuolar protein sorting and endocytosis. Label free and Western blotting revealed many WS-specific proteins and protein complexes are crucial for NRB initiation. These findings not only deepen our understanding of WS proteome, but also provide new evidences on the roles of RP membrane proteins in NRB.
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