Abstract

Along with many adaptive strategies, dynamic changes in protein abundance seem to be the common strategy to cope up with abiotic stresses which can be best explored through proteomics. Understanding of drought response is the key to decipher regulatory mechanism of better adaptation. Rice (Oryza sativa L.) proteome represents a phenomenal source of proteins that govern traits of agronomic importance, such as drought tolerance. In this study, a comparison of root cytoplasmic proteome was done for a drought tolerant rice (Heena) cultivar in PEG induced drought conditions. A total of 510 protein spots were observed by PDQuest analysis and 125 differentially regulated spots were subjected for MALDI-TOF MS-MS analysis out of which 102 protein spots identified which further led to identification of 78 proteins with a significant score. These 78 differentially expressed proteins appeared to be involved in different biological pathways. The largest percentage of identified proteins was involved in bioenergy and metabolism (29%) and mainly consists of malate dehydrogenase, succinyl-CoA, putative acetyl-CoA synthetase, and pyruvate dehydrogenase etc. This was followed by proteins related to cell defense and rescue (22%) such as monodehydroascorbate reductase and stress-induced protein sti1, then by protein biogenesis and storage class (21%) e.g. putative thiamine biosynthesis protein, putative beta-alanine synthase, and cysteine synthase. Further, cell signaling (9%) proteins like actin and prolyl endopeptidase, and proteins with miscellaneous function (19%) like Sgt1 and some hypothetical proteins were also represented a large contribution toward drought regulatory mechanism in rice. We propose that protein biogenesis, cell defense, and superior homeostasis may render better drought-adaptation. These findings might expedite the functional determination of the drought-responsive proteins and their prioritization as potential molecular targets for perfect adaptation.

Highlights

  • Rice (Oryza sativa L.) is an important staple cereal crops ranked second after maize worldwide and considered as a primary source of food for more than half the world’s population including Asia

  • To understand the drought tolerance mechanism in rice, we carried out the comparative proteomic analysis of roots of the drought tolerance Heena cultivar of rice at various time points after drought induction in 10% PEG (Figure 1A). 2-Dimensional Gel Electrophoresis (2DE) was performed at pH 4–7 IpG strip from 21 days old hydroponically grown rice root tissue in three replicates and images were analyzed by the PDQuest software version 8.0.1 as described above (Figure 1B)

  • We report here a systematic proteomic analysis of the rice root proteins under PEG-simulated drought stress conditions

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Summary

INTRODUCTION

Rice (Oryza sativa L.) is an important staple cereal crops ranked second after maize worldwide and considered as a primary source of food for more than half the world’s population including Asia. As a consequence, understanding the stress mechanism at protein level may provide some more useful insights to study the actual biotic stress response In this context, evolution of proteomics is playing a crucial role as necessary and complementary approach to address such issues in the post-genomic era (Zivy and de Vienne, 2000; van Wijk, 2001). Serious effort has been made for functional identification of tissues, organs, and development specific rice gene under environmental changes like biotic and abiotic stresses using systematic studies in proteomic analysis (Khan and Komatsu, 2004; Komatsu, 2005; Ali and Komatsu, 2006) and knowledge of these proteins would help in understanding the stress tolerance related molecular mechanism in rice at the translation level. Proteins were separated by two-dimensional gel electrophoresis (2-DE) followed by PD Quest analysis and identified by MALDI-Mass Spectrometry (MS) using available proteome databases

MATERIALS AND METHODS
AND DISCUSSION
38. OsC-2313 Pathogenesis-related protein 1-like GI:115474481 472
47. OsC-3516 Alpha-tubulin
76. OsC-6607 PREDICTED: uncharacterized protein GI:571541740 45
Findings
CONCLUSION
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