Fig. 1: Alignment of Lot5 with pICln homologs and identification of proteins interacting with Lot5 and Brr1.

a Sequence alignment of Lot5 (Yeast_Sc) with pICln homologs from various species. Secondary structures (β0-β7 strands, 3₁₀ and α helices) are annotated based on the crystal structure of fruit fly pICln (PDB: 4F7U). Conserved residues are highlighted in blue, with the intensity of the color reflecting the level of conservation. b Structural alignment between the AlphaFold structure model of Lot5 (residues 1–227) (β0-β7 strands are colored in blue, α helix in purple, other α helices in pink, and loops in orange) and the structure of fruit fly pICln (in grey); c, d Identification of proteins interacting with the N-terminally TAP-tagged Lot5 or Brr1 by a pull-down assay followed by Western blot analysis probed with a FLAG-antibody (c) and silver staining (d), as well as mass spectrometry analysis (Supplementary Table 1). EGFP served as a control. For each set, a representative result from two independent experiments is shown.