Fig. 1 | Nature Communications

Fig. 1

From: The Ustilago maydis repetitive effector Rsp3 blocks the antifungal activity of mannose-binding maize proteins

Fig. 1

Rsp3 shows length polymorphisms in field isolates and is induced after plant colonization. a The domain architecture of Rsp3 from U. maydis (Um) strains (FB1, FB2, and Toluca-6) and S. reilianum (Sr) as well as of C terminally truncated (Δ412–869), the 9CA mutant protein and chimeric proteins is depicted. aa amino acids, SP signal peptide, Cys cysteine-rich region (amino acids 244–333). This region is shown enlarged above. QP: glutamine and proline rich region. The different types of repeats are colored using the code shown below. The four degenerate repeats detected in U. maydis and S. reilianum have the same colors. Invariant amino acids in the consensus sequence are highlighted in red. Numbers 2, 3, and 4 in the yellow repeat indicate overlapping extensions of the short yellow repeat. b Expression analysis of rsp3 by quantitative RT-PCR. Maize plants were infected with a mixture of FB1xFB2 and segments of infected leaves were harvested at the indicated time points. RNA was prepared and subjected to qRT-PCR. RNAs prepared from FB1 and FB2 grown in YEPSL were mixed to provide the sample labeled axenic culture. Expression levels of rsp3 were normalized relative to the constitutively expressed peptidyl-prolyl isomerase (ppi). The expression level of rsp3 in axenic culture was set to 1.0. Three biological replicates were analyzed. Values represent mean ± sd

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