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FgMyo1 regulates translation of Tri1 via interacting with the ribosomal protein FgAsc1.

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posted on 2018-01-22, 18:36 authored by Guangfei Tang, Yun Chen, Jin-Rong Xu, H. Corby Kistler, Zhonghua Ma

(A) The interaction of FgMyo1-GFP and Asc1-RFP was verified by the Co-IP assay (left panel). FgMyo1-GFP was co-localized with FgAsc1-RFP under the toxin inducing conditions. Bar = 10 μm. (B) Localization of FgAsc1-RFP in hyphae of PH-1::FgAsc1-RFP+Tri1-GFP grown in toxin non-inducing medium PDB (upper panel) or toxin inducing medium TBI (lower panel) for 48 h. Bar = 10 μm. (C) ΔFgAsc1 exhibited dramatically reduced hyphal growth on PDA. (D) Toxisome formation was not detected in ΔFgAsc1 grown in TBI medium (left panel). Bar = 10 μm. The accumulation of Tri1-GFP protein in ΔFgAsc1 was determined by a western blot assay with the anti-GFP antibody (right panel). (E) DON production was under a detectable level in ΔFgAsc1. Values on the bars followed by the same letter are not significantly different according to a Fisher’s least significant difference (LSD) test at P = 0.05. (F) Comparisons in localization (left panel) and translation level (right panel) of the FK506-binding protein Fkbp54 tagged with GFP in the wild type and in the ΔFgAsc1 mutant. Bar = 10 μm.

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