Fig. 1: S. coelicolor encodes three degenerate repeat-containing polymorphic toxins that interact with paralogous proteins.
From: Streptomyces umbrella toxin particles block hyphal growth of competing species
a, Domain architecture of the UmbC proteins of S. coelicolor. Protein accession numbers and definitions of the variable C-terminal domains are available in Supplementary Tables 1 and 2. CH, connecting helix; Deam, deaminase; 4TM, 4TM tox; LII-phos, lipid II phosphatase, AA, amino acids. b, AlphaFold-predicted structural models of S. coelicolor UmbC proteins. UmbC1 and UmbC2 models were generated using template mode with UmbC3 as the reference. Colours correspond to a. ALF repeat numbering and location of the CH shown for UmbC1. The variable C-terminal domains, predicted to localize to the end of the stalk, could not be confidently modelled and are therefore not shown. c, IP–MS identification of proteins that interact with UmbC1, UmbC2 or UmbC3 from S. coelicolor. Top, average fold enrichment of proteins detected in both IP and control samples. Bottom, abundance (average spectral counts (SC)) for proteins detected only in IP samples. Colours indicate paralogous proteins; non-Umb proteins shown in grey. Note that additional background interacting proteins were identified for UmbC2, which we attribute to the lower abundance of this protein (46.5 SC) relative to UmbC1 (134.5 SC) and UmbC3 (781 SC) n = 2 biological replicates. V, VSV-G epitope. d, Loci encoding Umb protein complex components in S. coelicolor. Orphan umbA loci are those encoded distantly from other complex constituents. Colours consistent with c.
