A sorghum F-box protein induces an oxidative burst in the defense against Colletotrichum sublineola

Author:

Wolf Emily Sue Ann1,Vela Saddie1,Cuevas Hugo Eduardo2,Vermerris Wilfred3

Affiliation:

1. University of Florida, 3463, Graduate Program in Plant Molecular & Cellular Biology, Gainesville, Florida, United States;

2. USDA ARS, 17123, Mayagüez, PR, United States;

3. University of Florida, 3463, Microbiology & Cell Science, Cancer/Genetics Research Complex 302, 2033 Mowry Road, Gainesville, Florida, United States, 32610;

Abstract

The hemibiotrophic fungal pathogen Colletotrichum sublineola is the causal agent of anthracnose in sorghum (Sorghum bicolor (L.) Moench), resulting in leaf blight, stalk rot, and head blight in susceptible genotypes, with yield losses of up to 50%. The development of anthracnose-resistant cultivars can reduce reliance on fungicides and provide a more sustainable and economical means for disease management. A previous genome-wide association study of the sorghum association panel identified the candidate resistance gene Sobic.005G172300 encoding an F-box protein. To better understand the role of this gene in the defense against C. sublineola, gene expression following infection with C. sublineola was monitored by RNA-sequencing in seedlings of sorghum accession SC110, which harbored the resistance allele, and three accessions that harbored a susceptible allele. Only in SC110 did the expression of Sobic.005G172300 increase during the biotrophic phase of infection. Subsequent transcriptome analysis, gene co-expression networks, and gene regulatory networks of inoculated and mock-inoculated seedlings of resistant and susceptible accessions suggest that the increase in expression of Sobic.005G172300 induces an oxidative burst by lowering the concentration of ascorbic acid during the biotrophic phase of infection. Based on gene regulatory network analysis, the protein encoded by Sobic.005G172300 is proposed to target proteins involved in the biosynthesis of ascorbic acid for polyubiquitination through the SCF E3 ubiquitin ligase, causing their degradation via the proteasome.

Publisher

Scientific Societies

Subject

Plant Science,Agronomy and Crop Science

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