Proteome quantification of cotton xylem sap suggests the mechanisms of potassiumdeficiency-induced changes in plant resistance to environmental stresses
- ECU Author/Contributor (non-ECU co-authors, if there are any, appear on document)
- Zhiyong,Chao,Maoni,Wang,Sufang,Bu,Jingjing,Tang,Ju Zhang (Creator)
- Institution
- East Carolina University (ECU )
- Web Site: http://www.ecu.edu/lib/
Abstract: Proteomics was employed to investigate the molecular mechanisms of apoplastic response to potassium(K)-deficiency in cotton. Low K (LK) treatment significantly decreased the K and protein contents of xylem sap. Totally, 258 peptides were qualitatively identified in the xylem sap of cotton seedlings, of which, 90.31% were secreted proteins. Compared to the normal K (NK), LK significantly decreased the expression of most environmental-stress-related proteins and resulted in a lack of protein isoforms in the characterized proteins. For example, the contents of 21 Class è peroxidase isoforms under the LK were 6 to 44% of those under the NK and 11 its isoforms were lacking under the LK treatment; the contents of 3 chitinase isoforms under LK were 11-27% of those under the NK and 2 its isoforms were absent under LK. In addition, stress signaling and recognizing proteins were significantly down-regulated or disappeared under the LK. In contrast, the LK resulted in at least 2-fold increases of only one peroxidase, one protease inhibitor, one non-specific lipid-transfer protein and histone H4 and in the appearance of H2 A. Therefore, K deficiency decreased plant tolerance to environmental stresses, probably due to the significant and pronounced decrease or disappearance of a myriad of stress-related proteins.
Additional Information
- Publication
- Other
- Language: English
- Date: 2016
Title | Location & Link | Type of Relationship |
Proteome quantification of cotton xylem sap suggests the mechanisms of potassiumdeficiency-induced changes in plant resistance to environmental stresses | http://hdl.handle.net/10342/7980 | The described resource references, cites, or otherwise points to the related resource. |