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Alanine Glyoxylate Aminotransferase

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CJ Danpure – One of the best experts on this subject based on the ideXlab platform.

Yangdou Wei – One of the best experts on this subject based on the ideXlab platform.

Vijai Bhadauria – One of the best experts on this subject based on the ideXlab platform.

  • Alanine: Glyoxylate Aminotransferase 1 is required for mobilization and utilization of triglycerides during infection process of the rice blast pathogen, Magnaporthe oryzae.
    Plant signaling & behavior, 2012
    Co-Authors: Vijai Bhadauria, Sabine Banniza, Albert Vandenberg, Gopalan Selvaraj, Yangdou Wei
    Abstract:

    The rice blast pathogen, Magnaporthe oryzae has been widely used as a model pathogen to study plant infection-related fungal morphogenesis, such as penetration via appressorium and plant-microbe interactions at the molecular level. Previously, we identified a gene encoding peroxisomal Alanine: Glyoxylate Aminotransferase 1 (AGT1) in M. oryzae and demonstrated that the AGT1 was indispensable for pathogenicity. The AGT1 knockout mutants were unable to penetrate the host plants, such as rice and barley, and therefore were non-pathogenic. The inability of ∆Moagt1 mutants to penetrate the susceptible plants was likely due to the disruption in coordination of the β-oxidation and the Glyoxylate cycle resulted from a blockage in lipid droplet mobilization and eventually utilization during conidial germination and appressorium morphogenesis, respectively. Here, we further demonstrate the role of AGT1 in lipid mobilization by in vitro germination assays and confocal microscopy.

  • peroxisomal Alanine Glyoxylate Aminotransferase agt1 is indispensable for appressorium function of the rice blast pathogen magnaporthe oryzae
    PLOS ONE, 2012
    Co-Authors: Vijai Bhadauria, Sabine Banniza, Albert Vandenberg, Gopalan Selvaraj, Yangdou Wei
    Abstract:

    The role of β-oxidation and the Glyoxylate cycle in fungal pathogenesis is well documented. However, an ambiguity still remains over their interaction in peroxisomes to facilitate fungal pathogenicity and virulence. In this report, we characterize a gene encoding an Alanine, Glyoxylate Aminotransferase 1 (AGT1) in Magnaporthe oryzae, the causative agent of rice blast disease, and demonstrate that AGT1 is required for pathogenicity of M. oryzae. Targeted deletion of AGT1 resulted in the failure of penetration via appressoria; therefore, mutants lacking the gene were unable to induce blast symptoms on the hosts rice and barley. This penetration failure may be associated with a disruption in lipid mobilization during conidial germination as turgor generation in the appressorium requires mobilization of lipid reserves from the conidium. Analysis of enhanced green fluorescent protein expression using the transcriptional and translational fusion with the AGT1 promoter and open reading frame, respectively, revealed that AGT1 expressed constitutively in all in vitro grown cell types and during in planta colonization, and localized in peroxisomes. Peroxisomal localization was further confirmed by colocalization with red fluorescent protein fused with the peroxisomal targeting signal 1. Surprisingly, conidia produced by the Δagt1 mutant were unable to form appressoria on artificial inductive surfaces, even after prolonged incubation. When supplemented with nicotinamide adenine dinucleotide (NAD+)+pyruvate, appressorium formation was restored on an artificial inductive surface. Taken together, our data indicate that AGT1-dependent pyruvate formation by transferring an amino group of Alanine to Glyoxylate, an intermediate of the Glyoxylate cycle is required for lipid mobilization and utilization. This pyruvate can be converted to non-fermentable carbon sources, which may require reoxidation of NADH generated by the β-oxidation of fatty acids to NAD+ in peroxisomes. Therefore, it may provide a means to maintain redox homeostasis in appressoria.

Yinai Zhang – One of the best experts on this subject based on the ideXlab platform.

Roman N. Rodionov – One of the best experts on this subject based on the ideXlab platform.