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Comparative proteomics reveals a role for seed storage protein, AmA1 in cellular growth, development and nutrient accumulation

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Title Comparative proteomics reveals a role for seed storage protein, AmA1 in cellular growth, development and nutrient accumulation
 
Creator Agrawal, Lalit
Narula, Kanika
Basu, Swaraj
Shekhar, Shubhendu
Ghosh, Sudip
Datta, Asis
Chakraborty, Niranjan
Chakraborty, Subhra
 
Subject seed storage protein
AmA1
potato
comparative proteomics
metabolomics
nutrient accumulation
2-DE
mass spectrometry
protein network
 
Description Accepted date: September 11, 2013
Seed storage proteins are known to be utilized as carbon and nitrogen source for growing seedlings and thus are considered as potential candidates for nutritional improvement. However, their precise function remains unknown. We have earlier shown that ectopic expression of a seed storage protein, AmA1, leads to increase in protein besides high tuber yield in potato. To elucidate the AmA1-regulated molecular mechanism affecting increased protein synthesis, reserve accumulation, and enhanced growth, a comparative proteomics approach has been applied to tuber life-cycle between wild-type and AmA1 potato. The differential display of proteomes revealed 150 AmA1-responsive protein spots (ARPs) that change their intensities more than 2.5-fold. The LC-ESI-MS/MS analyses led to the identification of 80 ARPs presumably associated with cell differentiation, regulating diverse functions, viz., protein biogenesis and storage, bioenergy and metabolism, and cell signaling. Metabolome study indicated up-regulation of amino acids paralleling the proteomics analysis. To validate this, we focused our attention on anatomical study that showed differences in cell size in the cortex, premedullary zone and pith of the tuber, coinciding with AmA1 expression and localization. Further, we interrogated the proteome data using one-way analysis of variance, cluster, and partial correlation analysis that identified two significant protein modules and six small correlation groups centered around isoforms of cysteine protease inhibitor, actin, heat shock cognate protein 83 and 14-3-3, pointing toward AmA1-regulated overlapping processes of protein enhancement and cell growth perhaps through a common mechanism of function. A model network was constructed using the protein data sets, which aim to show how target proteins might work in coordinated fashion and attribute to increased protein synthesis and storage reserve accumulation in AmA1 tubers on one hand and organ development on the other.
We thank Dr. Evert Jacobsen for providing the plasmid pPGB1.
This work was supported by grants (BT/PR/11676/PBD/16/
831/2008) from the Department of Biotechnology (DBT),
Government of India and the National Institute of Plant
Genome Research, New Delhi, India. L.A. and K.N. are the
recipients of predoctoral fellowship from the Council of
Scientific and Industrial research (CSIR), Govt. of India.
Authors also thank Mr. Jasbeer Singh for illustrations and
graphical representations in the manuscript.
 
Date 2015-11-02T05:39:12Z
2015-11-02T05:39:12Z
2013
 
Type Article
 
Identifier J. Proteome Res., 12(11): 4904-4930
1535-3893
http://pubs.acs.org/doi/abs/10.1021/pr4007987
http://172.16.0.77:8080/jspui/handle/123456789/293
 
Language en_US
 
Publisher American Chemical Society