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. 2011 Jan 22;5(8):336-40.
doi: 10.6026/97320630005336.

Analysis of osmotin, a PR protein as metabolic modulator in plants

Analysis of osmotin, a PR protein as metabolic modulator in plants

Malik Zainul Abdin et al. Bioinformation. .

Abstract

Osmotin is an abundant cationic multifunctional protein discovered in cells of tobacco (Nicotiana tabacum L. var Wisconsin 38) adapted to an environment of low osmotic potential. Beside its role as osmoregulator, it provides plants protection from pathogens, hence also placed in the PRP family of proteins. The osmotin induced proline accumulation has been reported to confer tolerance against both biotic and abiotic stresses in plants including transgenic tomato and strawberry overexpressing osmotin gene. The exact mechanism of induction of proline by osmotin is however, not known till date. These observations have led us to hypothesize that osmotin could be regulating these plant responses through its involvement either as transcription factor, cell signal pathway modulator or both in plants. We have therefore, undertaken the present investigation to analyze the osmotin protein as transcription factor using bioinformatics tools. The results of available online DNA binding motif search programs revealed that osmotin does not contain DNAbinding motifs. The alignment results of osmotin protein with the protein sequence from DATF showed the homology in the range of 0-20%, suggesting that it might not contain a DNA binding motif. Further to find unique DNA-binding domain, the superimposition of osmotin 3D structure on modeled Arabidopsis transcription factors using Chimera also suggested absence of the same. However, evidence implicating osmotin in cell signaling were found during the study. With these results, we therefore, concluded that osmotin is not a transcription factor, but regulating plant responses to biotic and abiotic stresses through cell signaling.

Keywords: Alignment; DNA binding motifs; Osmoregulator; Osmotin.

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Figures

Figure 1
Figure 1
The domain architecture of Osmotin/thaumatin-like protein superfamily present in Arabidopsis thaliana
Figure 2
Figure 2
3D structure of 1pcvA downloaded from RCSB PDB and visualised by Rasmol
Figure 3
Figure 3
The Protein kinases signature domains present in Osmotin/thaumatin-like protein superfamily

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