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. 2023 Mar 14;34(4):ar33. doi: 10.1091/mbc.E22-11-0515

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© 2023 Neiman et al. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.

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FIGURE 1: — Ady4 interacts with Mss4 in the yeast two-hybrid system. (A) Schematic of the lexA-Mss4 fusions used for the yeast two-hybrid assay in panel B. Numbers indicate amino acid positions. The blue bar indicates a lysine-rich sequence, while the green bar indicates the kinase domain. (B) Strain L40 (lexA_op::HIS3) was transformed with plasmids carrying GAD-ADY4 or GAD-VPS13¹^–⁹⁶⁴ (as a specificity control) and the indicated lexA-MSS4 fusions. Cells were grown to saturation and 10-fold dilutions were spotted onto solid medium lacking tryptophan and leucine (left panel) or lacking tryptophan, leucine, and histidine (right panel). Growth in the absence of histidine indicates an interaction between the LexA and GAD fusion proteins. (C) Western blot of the LexA-Mss4 fusions used in panel B. Extracts from the cells used in the spotting assay were probed with antibodies to either LexA or Arp7 as a loading control.