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

BACKGROUND: 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 govern...

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Autores principales: Jaiswal, Dinesh Kumar, Ray, Doel, Subba, Pratigya, Mishra, Poonam, Gayali, Saurabh, Datta, Asis, Chakraborty, Subhra, Chakraborty, Niranjan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3558352/
https://www.ncbi.nlm.nih.gov/pubmed/23031650
http://dx.doi.org/10.1186/1477-5956-10-59
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author Jaiswal, Dinesh Kumar
Ray, Doel
Subba, Pratigya
Mishra, Poonam
Gayali, Saurabh
Datta, Asis
Chakraborty, Subhra
Chakraborty, Niranjan
author_facet Jaiswal, Dinesh Kumar
Ray, Doel
Subba, Pratigya
Mishra, Poonam
Gayali, Saurabh
Datta, Asis
Chakraborty, Subhra
Chakraborty, Niranjan
author_sort Jaiswal, Dinesh Kumar
collection PubMed
description BACKGROUND: 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. RESULTS: 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. CONCLUSIONS: 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.
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spelling pubmed-35583522013-01-31 Proteomic analysis reveals the diversity and complexity of membrane proteins in chickpea (Cicer arietinum L.) Jaiswal, Dinesh Kumar Ray, Doel Subba, Pratigya Mishra, Poonam Gayali, Saurabh Datta, Asis Chakraborty, Subhra Chakraborty, Niranjan Proteome Sci Research BACKGROUND: 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. RESULTS: 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. CONCLUSIONS: 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. BioMed Central 2012-10-02 /pmc/articles/PMC3558352/ /pubmed/23031650 http://dx.doi.org/10.1186/1477-5956-10-59 Text en Copyright ©2012 Jaiswal et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research
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 (Cicer arietinum L.)
title Proteomic analysis reveals the diversity and complexity of membrane proteins in chickpea (Cicer arietinum L.)
title_full Proteomic analysis reveals the diversity and complexity of membrane proteins in chickpea (Cicer arietinum L.)
title_fullStr Proteomic analysis reveals the diversity and complexity of membrane proteins in chickpea (Cicer arietinum L.)
title_full_unstemmed Proteomic analysis reveals the diversity and complexity of membrane proteins in chickpea (Cicer arietinum L.)
title_short Proteomic analysis reveals the diversity and complexity of membrane proteins in chickpea (Cicer arietinum L.)
title_sort proteomic analysis reveals the diversity and complexity of membrane proteins in chickpea (cicer arietinum l.)
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3558352/
https://www.ncbi.nlm.nih.gov/pubmed/23031650
http://dx.doi.org/10.1186/1477-5956-10-59
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