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Tilletia horrida glycoside hydrolase family 128 protein, designated ThGhd_7, modulates plant immunity by blocking reactive oxygen species production
CONFLICT OF INTEREST STATEMENT The authors declare no conflicts of interest. Supporting Information Filename Description pce14893-sup-0001-Supplementary_Figures.docx3.5 MB Figure S1 Nicotiana benthamiana leaves were inoculated with purified ThGhd_7 protein in 5 μM and 1 μM, respectively. Buffer was used as control. Treated N. benthamiana leaves were photographed at 48 h post inoculation. Figure S2 Constructed phylogeny tree of ThGhd_7 and its homologous proteins.
Integrated Genome Sequencing and Transcriptome Analysis Identifies Candidate Pathogenicity Genes from Ustilago crameri
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The pathogenic mechanisms of <i>Tilletia horrida</i> as revealed by comparative and functional genomics
The genome of the T. horrida strain JY-521 was sequenced using a PacBio RS II sequencing strategy and three single-molecule real-time (SMRT) sequence cells were obtained (Supplementary Table S1). The three SMRT cells were assembled into scaffolds using MinHasf Alignment Process (MHAP) assemble, resulting in longer sequences with a total assembly size of 23.2 Mbp; 84 contigs and 84 scaffolds (no gaps within them) were assembled. The N50 size of the scaffold and contigs was 538,348 bp.
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