1. In silico identification of copper-binding proteins of Xanthomonas translucens pv. undulosa for their probable role in plant-pathogen interactions.
- Author
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Sharma, Ankita, Sharma, Dixit, and Verma, Shailender Kumar
- Subjects
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PLANT-pathogen relationships , *PROTEOMICS , *XANTHOMONAS , *AMINO acid residues , *HISTIDINE , *GLUTAMIC acid - Abstract
Xanthomonas translucens pv. undulosa (Xtu) is a bacterial pathogen that infects wheat and barley. Copper, with its unique redox properties, acts as an essential micronutrient, which plays important role in the bacterial physiology and virulence. The current study is based on a systematic computational approach to identify the copper-binding proteins of Xtu and propose their probable role in Xtu 's pathogenesis. We found that ∼0.9% of the Xtu proteome contains copper-binding sequence motifs. A total of 12 putative copper-binding proteins were shortlisted which could play important role in pathogen-host interactions. Out of these 12 proteins, three are considered to be putatively secretory in nature based on the in silico analysis. The identified copper-binding proteins may play imperative roles in cellular metabolism, transport, protein folding, response to oxidative stress, transcription regulation, and cell signaling. This study will further assist towards the understanding of the copper homeostasis in Xtu and the probable roles of copper-binding proteins in plant-pathogen interactions. Image 1 • Approximately 0.9% proteome of Xtu has copper binding motifs. • Cysteine, histidine, aspartic acid and glutamic acid are the commonly interacting amino acid residues with copper ion(s). • A total of 12 proteins were found to be critical for the plant-pathogen interactions. • Copper-binding proteins perform diverse range of biological and molecular functions. [ABSTRACT FROM AUTHOR]
- Published
- 2019
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