DJDonald James

Donald James

*This is an algorithmically generated author record based on publicly available information.

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Previous Organizations / Institutes

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Donald James has a total of 29 co-authors. Here are the top co-authors by number of shared publications:


Latest Publications

  • Xanthomonas oryzae pv. oryzae Type III Effector Tal9b Targets a Broadly Conserved Disease Susceptibility Locus to Promote Pathogenesis in Rice

    by Gokulan C. G., Sohini Deb, Namami Gaur, Apoorva Masade, Niranjan Gattu, Rennya P. R., Nisha Sao, Donald James, Ramesh V. Sonti, Hitendra K. Patel

    Xanthomonas oryzae pv. oryzae ( Xoo), the causal agent of bacterial blight of rice, translocates multiple transcription activator-like effectors (TALEs) into rice cells. The TALEs localize to the host cell nucleus, where they bind to the DNA in a sequence-specific manner and enhance gene expression to promote disease susceptibility. Xoo strain PXO99A encodes 19 TALEs, but the host targets of all these TALEs have not been defined. A meta-analysis of rice transcriptome profiles revealed a gene annotated as flavonol synthase/flavanone-3 hydroxylase (henceforth OsS5H/FNS-03g) to be highly induced upon Xoo infection. Further analyses revealed that this gene is induced by PXO99A using Tal9b, a broadly conserved TALE of Xoo. Disruption of tal9b rendered PXO99A less virulent. OsS5H/FNS-03g functionally complemented its Arabidopsis homologue AtDMR6, a well-studied disease susceptibility locus. Biochemical analyses suggested that OsS5H/FNS-03g is a bifunctional protein with salicylic acid 5′ hydroxylase (S5H) and flavone synthase-I (FNS-I) activities. Further, an exogenous application of apigenin, the flavone that is enzymatically produced by OsS5H/FNS-03g, on rice leaves promoted virulence of PXO99A tal9b–. Overall, our study suggests that OsS5H/FNS-03g is a bifunctional enzyme, and its product, apigenin, is potentially involved in promoting Xoo virulence. [ ] Copyright © 2025 The Author(s). This is an open access article distributed under the CC BY-NC-ND 4.0 International license .


  • Open Access

    Xanthomonas oryzae pv. oryzae type-III effector TAL9b targets a broadly conserved disease susceptibility locus to promote pathogenesis in rice

    by C.G. Gokulan, Sohini Deb, Namami Gaur, Apoorva Masade, Niranjan Gattu, P.R. Rennya, Nisha Sao, Donald James, Ramesh V. Sonti, Hitendra K. Patel

    SUMMARY: Xanthomonas oryzae pv. oryzae (Xoo), the causal agent of bacterial blight of rice, translocates multiple Transcription Activator-Like Effectors (TALEs) into rice cells. The TALEs localize to the host cell nucleus, where they bind to the DNA in a sequence-specific manner and enhance gene expression to promote disease susceptibility. Xoo strain PXO99 A encodes nineteen TALEs, but the host targets of all these TALEs have not been defined. A meta-analysis of rice transcriptome profiles revealed a gene annotated as flavonol synthase/flavanone-3 hydroxylase (henceforth OsS5H/FNS-03g ) to be highly induced upon Xoo infection. Further analyses revealed that this gene is induced by PXO99 A using TAL9b, a broadly conserved TALE of Xoo. Disruption of tal9b rendered PXO99 A less virulent. OsS5H/FNS-03g functionally complemented its Arabidopsis homologue AtDMR6, a well-studied disease susceptibility locus. Biochemical analyses suggested that OsS5H/FNS-03g is a bifunctional protein with Salicylic Acid 5’ Hydroxylase (S5H) and Flavone Synthase-I (FNS-I) activities. Further, an exogenous application of apigenin on rice leaves, the flavone that is enzymatically produced by OsS5H/FNS-03g, promoted virulence of PXO99 A tal9b -. Overall, our study suggests that OsS5H/FNS-03g is a bifunctional enzyme and its product apigenin is potentially involved in promoting Xoo virulence.

  • Open Access

    Photosynthetic machinery under salinity stress: Trepidations and adaptive mechanisms

    by T.V. Vineeth, G.K. Krishna, P.H. Pandesha, L. Sathee, S. Thomas, D. James, K.T. Ravikiran, S. Taria, C. John, N.M. Vinaykumar, et al.

    Photosynthetica covers wide range of photosynthesis research or research including photosynthetic parameters of both experimental and theoretical nature.