Extended Data Fig. 1: dCTP deaminases protect against phage infection.
From: Bacteria deplete deoxynucleotides to defend against bacteriophage infection
(A) Superposition of the C-terminal region (residues 351-550) of the AlphaFold-predicted structure of E. coli AW1.7 dCTP deaminase (turquoise), aligned with Streptococcus mutans cytosine deaminase (PDB: 2hvw) (grey). Zn2+ ions are depicted as blue spheres. Alignment was performed by PDBeFOLD61, with a Q score = 0.33, Z score = 9.0 and RMSD = 2.72 Å between the two structures. (B) Representative instances of cytidine deaminase genes (in turquoise) and their genomic neighborhoods. Genes known to be involved in defense are shown in yellow. RM, restriction modification; TAs, toxin-antitoxin systems; Septu and Hachiman are recently described defense systems14. The bacterial species and the accession of the relevant genomic scaffold in the Integrated Microbial Genomes (IMG) database47 are indicated on the left. (C) Bacteria expressing dCTP deaminases from E. coli U09 or E. coli AW1.7, as well as a negative control that contains an empty vector, were grown on agar plates in room temperature. Tenfold serial dilutions of the phage lysate were dropped on the plates. Data represent plaque-forming units per milliliter for ten phages tested in this study. Each bar graph represents average of three replicates, with individual data points overlaid. (D) Growth curves of cells expressing E. coli AW1.7 dCTP deaminase (turquoise), and control cells (grey). Results of three replicates are presented as individual curves.
