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Characterization of the secretome of chickpea suspension culture reveals pathway abundance and the expected and unexpected secreted proteins

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Title Characterization of the secretome of chickpea suspension culture reveals pathway abundance and the expected and unexpected secreted proteins
 
Creator Gupta, Sonika
Wardhan, Vijay
Verma, Shikha
Gayali, Saurabh
Rajamani, Uma
Datta, Asis
Chakraborty, Subhra
Chakraborty, Niranjan
 
Subject Chickpea
unsequenced genome
callus culture
extracellular space
secretome
nonclassical secretion
 
Description The secretome of an organism is defined as a set of secreted proteins that encompasses all proteins exported to the extracellular space. To better understand the chickpea secretome, we used callus culture to isolate and identify secreted proteins as a step toward determining their functions. Proteins in the extracellular media of the suspension culture were examined using SDS-PAGE and mass spectrometry (LC-MS/MS). Proteomic analysis led to the identification of 773 proteins, presumably involved in a variety of functions including metabolism, signal transduction, transport, and cell defense, in addition to maintaining redox status of extracellular space. Bioinformatic analysis confirmed 724 proteins, accounting for 94% of the identified proteins, as constituents of the secretome. Analysis of the secretome revealed the presence of several proteins of unknown function and a large number of classical and nonclassical secreted proteins. This represents the first comprehensive secretome of a legume genome, which is yet to be sequenced. Comparative analysis of the chickpea secretome with those of Medicago, Arabidopsis, and rice revealed that the majority of identified proteins are seemingly species-specific. This study demonstrates that characterization of the chickpea secretome in vitro can be used to identify secreted proteins, which has implications for systems biology research.
This work was supported by grants from the Department of
Biotechnology (DBT), Govt. of India and the National Institute
of Plant Genome Research, New Delhi.
 
Date 2014-04-28T05:30:51Z
2014-04-28T05:30:51Z
2011
September 2011
 
Type Article
 
Identifier J. Proteome Res., 10(11): 5006-5015
http://hdl.handle.net/123456789/190
 
Language en
 
Publisher Am. Chemical Society