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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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 |
work_keys_str_mv |
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