Open Access Research

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

Dinesh Kumar Jaiswal, Doel Ray, Pratigya Subba, Poonam Mishra, Saurabh Gayali, Asis Datta, Subhra Chakraborty and Niranjan Chakraborty*

Author Affiliations

National Institute of Plant Genome Research, JNU Campus, Aruna Asaf Ali Marg, New Delhi, 110067, India

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Proteome Science 2012, 10:59  doi:10.1186/1477-5956-10-59

Published: 2 October 2012

Abstract

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.

Keywords:
Grain legume; Membrane-associated proteins; 2-DE; Mass spectrometry; Transmembrane domain