A novel peptidoglycan deacetylase modulates daughter cell separation inE. coli

• DOI: 10.1101/2025.02.18.638797
• Publication Date: 2025-02-20T03:05:17Z
• Authors: Victor Hernandez-...; Alessandra M. Mar...; Aitana Belloso; Daniel Ballesteros; Marta Zaccaria; Amilcar J. Perez; Bogdan I. Iorga; David Abia; Joe Gray; Eefjan Breukink; Jie Xiao; Manuel Pazos; Alessandra Polissi; Waldemar Vollmer
• Keywords: Amidase

ABSTRACT Peptidoglycan hydrolases facilitate bacterial cell wall growth by creating space for insertion of new material and allowing physical separation daughter cells. In Escherichia coli , three peptidoglycan amidases, AmiA, AmiB AmiC, cleave septal during division. The LytM-domain proteins EnvC NlpD activate these amidases either from inside the or outer membrane: binds to cytoplasmic membrane-anchored divisome components FtsEX, ActS are membrane lipoproteins. Here we report identification a novel periplasmic deacetylase called SddA that removes acetyl groups denuded glycan strands, products amidases. is substrate protease Prc, suggesting regulation via protein degradation. sddA gene co-expressed with encoding EnvC, linking function amidase activation. Consistent this link, deletion alleviates phenotypes associated lack activation, while overexpression related defective Tol-Pal system causes chaining due reduced septum cleavage unless envC co-expressed. We present model according which modulates activation septum-splitting AUTHOR SUMMARY Bacteria surround their essential (cell wall) layer prevent bursting open turgor. During division, bacteria produce at midcell, must be cleaved cells separate. Here, enzyme, SddA, modifies particular type material, chains released splitting separation, in Gram-negative . propose switch splitting, ensuring activated early stages division late stages.