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DC Field | Value | Language |
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dc.contributor.author | Gupta, Sonika | - |
dc.contributor.author | Wardhan, Vijay | - |
dc.contributor.author | Kumar, Amit | - |
dc.contributor.author | Rathi, Divya | - |
dc.contributor.author | Pandey, Aarti | - |
dc.contributor.author | Chakraborty, Subhra | - |
dc.contributor.author | Chakraborty, Niranjan | - |
dc.date.accessioned | 2016-01-05T07:23:02Z | - |
dc.date.available | 2016-01-05T07:23:02Z | - |
dc.date.issued | 2015 | - |
dc.identifier.citation | Scientific Reports, 5: 18427 | en_US |
dc.identifier.issn | 2045-2322 | - |
dc.identifier.uri | http://172.16.0.77:8080/jspui/handle/123456789/512 | - |
dc.description | Accepted date: 16 November 2015 | en_US |
dc.description.abstract | Secreted proteins maintain cell structure and biogenesis besides acting in signaling events crucial for cellular homeostasis during stress adaptation. To understand the underlying mechanism of stress-responsive secretion, the dehydration-responsive secretome was developed from suspension-cultured cells of chickpea. Cell viability of the suspension culture remained unaltered until 96 h, which gradually declined at later stages of dehydration. Proteomic analysis led to the identification of 215 differentially regulated proteins, involved in a variety of cellular functions that include metabolism, cell defence, and signal transduction suggesting their concerted role in stress adaptation. One-third of the secreted proteins were devoid of N-terminal secretion signals suggesting a non-classical secretory route. Screening of the secretome identified a leaderless Bet v 1-like protein, designated CaRRP1, the export of which was inhibited by brefeldin A. We investigated the gene structure and genomic organization and demonstrated that CaRRP1 may be involved in stress response. Its expression was positively associated with abiotic and biotic stresses. CaRRP1 could complement the aberrant growth phenotype of yeast mutant, deficient in vesicular transport, indicating a partial overlap of protein secretion and stress response. Our study provides the most comprehensive analysis of dehydration-responsive secretome and the complex metabolic network operating in plant extracellular space. | en_US |
dc.description.sponsorship | This work was supported by grants (BT/PR12919/AGR/02/676 and BT/PR4016/AGR/16/327) from the Department of Biotechnology (DBT), Govt. of India. S.G., V.W. and D.R. were supported by the predoctoral fellowship from the Council of Scientific and Industrial Research (CSIR), Govt. of India and A.P. received postdoctoral fellowship from the National Institute of Plant Genome Research, New Delhi. Dr. Suchismita Dass is thanked for assistance with writing the manuscript. We thank Mr. Shankar Acharya for technical assistance and Mr. Jasbeer Singh for illustrations and graphical representation in the manuscript. | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | Nature Publishing Group | en_US |
dc.subject | Plant molecular biology | en_US |
dc.subject | Plant stress responses | en_US |
dc.title | Secretome analysis of chickpea reveals dynamic extracellular remodeling and identifies a Bet v1- like protein, CaRRP1 that participates in stress response | en_US |
dc.type | Article | en_US |
dc.identifier.officialurl | http://www.nature.com/articles/srep18427 | en_US |
dc.identifier.doi | 10.1038/srep18427 | en_US |
Appears in Collections: | Institutional Publications |
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File | Description | Size | Format | |
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Chakraborty N_2015_3.pdf | 2.19 MB | Adobe PDF | View/Open |
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