Vashisht, Ajay Amar ; Pradhan, Arun ; Tuteja, Renu ; Tuteja, Narendra (2005) Cold- and salinity stress-induced bipolar pea DNA helicase 47 is involved in protein synthesis and stimulated by phosphorylation with protein kinase C The Plant Journal, 44 (1). pp. 76-87. ISSN 0960-7412
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Official URL: http://onlinelibrary.wiley.com/doi/10.1111/j.1365-...
Related URL: http://dx.doi.org/10.1111/j.1365-313X.2005.02511.x
Abstract
Helicases are involved in the metabolism of nucleic acid; this is very sensitive to the abiotic stresses that reduce plant growth and productivity. However, the molecular targets responsible for this sensitivity have not been well studied. Here we report on the isolation and characterization of cold- and salinity stress-induced pea DNA helicase 47 (PDH47). The transcript of PDH47 was induced in both shoots and roots under cold (4°C) and salinity (300 mm NaCl) stress, but there was no change in response to drought stress. Tissue-specific differential regulation was observed under heat (37°C) stress. ABA treatment did not alter expression of PDH47 in shoots but induced its mRNA in roots, indicating a role for PDH47 in both the ABA-independent and ABA-dependent pathways in abiotic stress. The purified recombinant protein (47 kDa) contains ATP-dependent DNA and RNA helicase and DNA-dependent ATPase activities. With the help of photoaffinity labeling, PDH47 was labeled by [α-32P]-ATP. PDH47 is a unique bipolar helicase that contains both 3' to 5' and 5' to 3' directional helicase activities. Anti-PDH47 antibodies immunodeplete the activities of PDH47 and inhibit in vitro translation of protein. Furthermore, the PDH47 protein showed upregulation of protein synthesis. The activities of PDH47 are stimulated after phosphorylation by protein kinase C at Ser and Thr residues. Western blot analysis and in vivo immunostaining, followed by confocal microscopy, showed PDH47 to be localized in both the nucleus and cytosol. The discovery of cold- and salinity stress-induced DNA helicase should make an important contribution to a better understanding of DNA metabolism and stress signaling in plants. Its bipolar helicase activities may also be involved in distinct cellular processes in stressed conditions.
Item Type: | Article |
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Source: | Copyright of this article belongs to John Wiley and Sons. |
Keywords: | Abiotic Stress; DEAD-box Protein; DNA-dependent ATPase; Pisum sativum; Plant DNA Helicase; Translation Initiation Factor; Unwinding Enzyme |
ID Code: | 52757 |
Deposited On: | 04 Aug 2011 12:02 |
Last Modified: | 18 May 2016 06:10 |
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