Fig. 2: Amino acid residues V234, F235, and L238 in Erg11 contribute to the Erg11 -Ncp1 interaction.
a The energy decomposition diagram for the Erg11200-251 region revealed that the residues V234, F235, and L238 exhibited the highest energy contributions, with ΔGbind values of −0.85 kcal/mol, −1.95 kcal/mol, and −2.04 kcal/mol, respectively. b The MYTH system analyzed the interaction between Erg11m and Ncp1. “Erg11m” represents the yeast cells with the bait Erg11m and the prey vector (no inserting Ncp1); “Erg11m + Ncp1” is the co-transformation of the bait Erg11 and the prey Ncp1 to the yeast cells. c Co-IP assay analyzed the interaction between Erg11m and Ncp1. An anti-Myc antibody to precipitate Erg11m or Erg11 and utilizes an anti-HA antibody to precipitate Ncp1. The protein content of 3HA-Ncp1 was quantified relative to Erg11m-13Myc or Erg11-13Myc. “Input” refers to lysates without any other manipulations used for immunoblotting. “IP” stands for immunoprecipitate, and the Protein A columns are used to collect the antibody-protein complex. “+“ indicates co-incubation of lysates with anti-Myc antibody, and “−“ represents lysates not incubated with antibodies. d Co-IP assay analyzed the interaction between Erg11m and Ncp1. An anti-HA antibody to precipitate Ncp1. The protein content of Erg11m-13Myc or Erg11-13Myc was quantified relative to 3HA-Ncp1. “+“ indicates co-incubation of lysates with anti-HA antibody, and “−“ represents lysates not incubated with antibodies. Three biological replicates were carried out. One of the representative images is shown (c, d). Data were presented as mean ± standardized variance (SD) (n = 3). Two-tailed unpaired t-test (c, d). Source data including uncropped and unprocessed scans with molecular weight markers are provided as Source Data file (c, d).
