Phosphorylation of 399S at CsHsp70 of Cymbidium sinense is essential to maintain chlorophyll stability

Copyright © 2024 The Authors. Published by Elsevier Masson SAS.. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 211(2024) vom: 12. Juni, Seite 108518
1. Verfasser: Gao, Jie (VerfasserIn)
Weitere Verfasser: Lu, Chuqiao, Wei, Yonglu, Xie, Qi, Jin, Jianpeng, Li, Jie, Yang, Fengxi, Zhu, Genfa
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2024
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Cymbidium sinense Heat-shock protein 70 Leaf variegation Phosphoproteomics Proteomics Chlorophyll 1406-65-1 Plant Proteins Phosphoproteins
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520 |a The Chinese orchids symbolise nobility and gentility in China, and the variation of leaf color makes Cymbidium sinense more diversified and valuable. However, its color variations especially at the protein level still remain largely unexplored. In this study, the proteomics and phosphoproteomics of Cymbidium sinense leaf color variation mutants were studied. A total of 1059 differentially abundant proteins (DAPs) and 1127 differentially abundant phosphorylation sites belonging to 644 phosphoproteins (DAPPs) were identified in the yellow section of leaf variegation mutant of Cymbidium sinense (MY) compared with the green section (MG). Moreover, 349 co-expressing proteins were found in both omics' datasets, while only 26 proteins showed the same expression patterns in the two omics. The interaction network analysis of kinases and phosphatases showed that DAPs and DAPPs in photosynthesis, response to hormones, pigment metabolic process, phosphorylation, glucose metabolic process, and dephosphorylation might contribute to leaf color variation. The abundance of 28 Hsps and 28 phosphorylation sites belonging to 10 Hsps showed significant differences between MG and MY. CsHsp70 was selected to explore the function in Cymbidium sinense leaf variegation. The results showed CsHsp70 is essential for maintaining photosynthetic pigment content and the 399S phosphorylation site is crucial to the function of CsHsp70. Collectively, our findings construct a comprehensive coverage of protein and protein phosphorylation in leaf variegation of C. sinense, providing valuable insights into its formation mechanisms 
650 4 |a Journal Article 
650 4 |a Cymbidium sinense 
650 4 |a Heat-shock protein 70 
650 4 |a Leaf variegation 
650 4 |a Phosphoproteomics 
650 4 |a Proteomics 
650 7 |a Chlorophyll  |2 NLM 
650 7 |a 1406-65-1  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Phosphoproteins  |2 NLM 
700 1 |a Lu, Chuqiao  |e verfasserin  |4 aut 
700 1 |a Wei, Yonglu  |e verfasserin  |4 aut 
700 1 |a Xie, Qi  |e verfasserin  |4 aut 
700 1 |a Jin, Jianpeng  |e verfasserin  |4 aut 
700 1 |a Li, Jie  |e verfasserin  |4 aut 
700 1 |a Yang, Fengxi  |e verfasserin  |4 aut 
700 1 |a Zhu, Genfa  |e verfasserin  |4 aut 
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773 1 8 |g volume:211  |g year:2024  |g day:12  |g month:06  |g pages:108518 
856 4 0 |u http://dx.doi.org/10.1016/j.plaphy.2024.108518  |3 Volltext 
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