Verma, Jitendra Kumar ; Gayali, Saurabh ; Dass, Suchismita ; Kumar, Amit ; Parveen, Shaista ; Chakraborty, Subhra ; Chakraborty, Niranjan (2014) OsAlba1, a dehydration-responsive nuclear protein of rice (Oryza sativa L. ssp. indica), participates in stress adaptation Phytochemistry, 100 . pp. 16-25. ISSN 0031-9422
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Official URL: http://www.sciencedirect.com/science/article/pii/S...
Related URL: http://dx.doi.org/10.1016/j.phytochem.2014.01.015
Abstract
Alba proteins have exhibited great functional plasticity through the course of evolution and constitute a superfamily that spans across three domains of life. Earlier, we had developed the dehydration-responsive nuclear proteome of an indica rice cultivar, screening of which led to the identification of an Alba protein. Here we describe, for the first time, the complete sequence of the candidate gene OsAlba1, its genomic organization, and possible function/s in plant. Phylogenetic analysis showed its close proximity to other monocots as compared to dicot Alba proteins. Protein–DNA interaction prediction indicates a DNA-binding property for OsAlba1. Confocal microscopy showed the localization of OsAlba1–GFP fusion protein to the nucleus, and also sparsely to the cytoplasm. Water-deficit conditions triggered OsAlba1 expression suggesting its function in dehydration stress, possibly through an ABA-dependent pathway. Functional complementation of the yeast mutant ΔPop6 established that OsAlba1 also functions in oxidative stress tolerance. The preferential expression of OsAlba1 in the flag leaves implies its role in grain filling. Our findings suggest that the Alba components such as OsAlba1, especially from a plant where there is no evidence for a major chromosomal role, might play important function in stress adaptation.
Item Type: | Article |
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Source: | Copyright of this article belongs to Elsevier Science. |
Keywords: | Alba Family Proteins; Dehydration Response; Dimer Modelling; DNA-Binding Proteins; Dual Localization; Transcriptional Regulation |
ID Code: | 100231 |
Deposited On: | 30 Nov 2016 11:54 |
Last Modified: | 30 Nov 2016 11:54 |
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