Proteomic analysis reveals the diversity and complexity of membrane proteins in chickpea (<it>Cicer arietinum</it> L.)

<p>Abstract</p> <p>Background</p> <p>Compartmentalization is a unique feature of eukaryotes that helps in maintaining cellular homeostasis not only in intra- and inter-organellar context, but also between the cells and the external environment. Plant cells are highly co...

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Main Authors: Jaiswal Dinesh Kumar, Ray Doel, Subba Pratigya, Mishra Poonam, Gayali Saurabh, Datta Asis, Chakraborty Subhra, Chakraborty Niranjan
Format: Article
Language:English
Published: BMC 2012-10-01
Series:Proteome Science
Subjects:
Online Access:http://www.proteomesci.com/content/10/1/59
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spelling doaj-a4c319707ab94154b453b7070a1a53822020-11-24T23:02:49ZengBMCProteome Science1477-59562012-10-011015910.1186/1477-5956-10-59Proteomic analysis reveals the diversity and complexity of membrane proteins in chickpea (<it>Cicer arietinum</it> L.)Jaiswal Dinesh KumarRay DoelSubba PratigyaMishra PoonamGayali SaurabhDatta AsisChakraborty SubhraChakraborty Niranjan<p>Abstract</p> <p>Background</p> <p>Compartmentalization is a unique feature of eukaryotes that helps in maintaining cellular homeostasis not only in intra- and inter-organellar context, but also between the cells and the external environment. Plant cells are highly compartmentalized with a complex metabolic network governing various cellular events. The membranes are the most important constituents in such compartmentalization, and membrane-associated proteins play diverse roles in many cellular processes besides being part of integral component of many signaling cascades.</p> <p>Results</p> <p>To obtain valuable insight into the dynamic repertoire of membrane proteins, we have developed a proteome reference map of a grain legume, chickpea, using two-dimensional gel electrophoresis. MALDI-TOF/TOF and LC-ESI-MS/MS analysis led to the identification of 91 proteins involved in a variety of cellular functions viz., bioenergy, stress-responsive and signal transduction, metabolism, protein synthesis and degradation, among others. Significantly, 70% of the identified proteins are putative integral membrane proteins, possessing transmembrane domains.</p> <p>Conclusions</p> <p>The proteomic analysis revealed many resident integral membrane proteins as well as membrane-associated proteins including those not reported earlier. To our knowledge, this is the first report of membrane proteome from aerial tissues of a crop plant. The findings may provide a better understanding of the biochemical machinery of the plant membranes at the molecular level that might help in functional genomics studies of different developmental pathways and stress-responses.</p> http://www.proteomesci.com/content/10/1/59Grain legumeMembrane-associated proteins2-DEMass spectrometryTransmembrane domain
collection DOAJ
language English
format Article
sources DOAJ
author Jaiswal Dinesh Kumar
Ray Doel
Subba Pratigya
Mishra Poonam
Gayali Saurabh
Datta Asis
Chakraborty Subhra
Chakraborty Niranjan
spellingShingle Jaiswal Dinesh Kumar
Ray Doel
Subba Pratigya
Mishra Poonam
Gayali Saurabh
Datta Asis
Chakraborty Subhra
Chakraborty Niranjan
Proteomic analysis reveals the diversity and complexity of membrane proteins in chickpea (<it>Cicer arietinum</it> L.)
Proteome Science
Grain legume
Membrane-associated proteins
2-DE
Mass spectrometry
Transmembrane domain
author_facet Jaiswal Dinesh Kumar
Ray Doel
Subba Pratigya
Mishra Poonam
Gayali Saurabh
Datta Asis
Chakraborty Subhra
Chakraborty Niranjan
author_sort Jaiswal Dinesh Kumar
title Proteomic analysis reveals the diversity and complexity of membrane proteins in chickpea (<it>Cicer arietinum</it> L.)
title_short Proteomic analysis reveals the diversity and complexity of membrane proteins in chickpea (<it>Cicer arietinum</it> L.)
title_full Proteomic analysis reveals the diversity and complexity of membrane proteins in chickpea (<it>Cicer arietinum</it> L.)
title_fullStr Proteomic analysis reveals the diversity and complexity of membrane proteins in chickpea (<it>Cicer arietinum</it> L.)
title_full_unstemmed Proteomic analysis reveals the diversity and complexity of membrane proteins in chickpea (<it>Cicer arietinum</it> L.)
title_sort proteomic analysis reveals the diversity and complexity of membrane proteins in chickpea (<it>cicer arietinum</it> l.)
publisher BMC
series Proteome Science
issn 1477-5956
publishDate 2012-10-01
description <p>Abstract</p> <p>Background</p> <p>Compartmentalization is a unique feature of eukaryotes that helps in maintaining cellular homeostasis not only in intra- and inter-organellar context, but also between the cells and the external environment. Plant cells are highly compartmentalized with a complex metabolic network governing various cellular events. The membranes are the most important constituents in such compartmentalization, and membrane-associated proteins play diverse roles in many cellular processes besides being part of integral component of many signaling cascades.</p> <p>Results</p> <p>To obtain valuable insight into the dynamic repertoire of membrane proteins, we have developed a proteome reference map of a grain legume, chickpea, using two-dimensional gel electrophoresis. MALDI-TOF/TOF and LC-ESI-MS/MS analysis led to the identification of 91 proteins involved in a variety of cellular functions viz., bioenergy, stress-responsive and signal transduction, metabolism, protein synthesis and degradation, among others. Significantly, 70% of the identified proteins are putative integral membrane proteins, possessing transmembrane domains.</p> <p>Conclusions</p> <p>The proteomic analysis revealed many resident integral membrane proteins as well as membrane-associated proteins including those not reported earlier. To our knowledge, this is the first report of membrane proteome from aerial tissues of a crop plant. The findings may provide a better understanding of the biochemical machinery of the plant membranes at the molecular level that might help in functional genomics studies of different developmental pathways and stress-responses.</p>
topic Grain legume
Membrane-associated proteins
2-DE
Mass spectrometry
Transmembrane domain
url http://www.proteomesci.com/content/10/1/59
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