A periplasmic protein modulates the proteolysis of peptidoglycan hydrolases to maintain cell wall homeostasis in Escherichia coli

• DOI: 10.1073/pnas.2418854122
• Publication Date: 2025-01-22T15:54:23Z
• Authors: Sohee Park; Wook-Jong Jeon; Yeseul Lee; Chae Lim Lim; Eunyeong Lee; Han Byeol Oh; Gyu Sung Lee; Oh Hyun Kwon; Bumhan Ryu; Yong-Joon Cho; Chung Sub Kim; Sung-il Yoon; Jeong Min Chung; Hongbaek Cho
• Keywords: Proteolysis; Lytic cycle

Bacterial cell wall assembly and remodeling require activities of peptidoglycan (PG) hydrolases as well PG synthases. In particular, the activity DD-endopeptidases, which cleave 4-3 peptide crosslinks in PG, is essential for expansion gram-negative bacteria. Maintaining optimal levels DD-endopeptidases critical expanding without compromising its integrity. Escherichia coli , major MepS MepH, along with lytic transglycosylase MltD, are controlled by periplasmic protease Prc outer membrane adaptor NlpI. However, mechanisms regulating turnover these have remained unclear. this study, we identified a protein, BipP (formerly YhjJ), that negatively controls NlpI-Prc system. Further analyses indicate exerts control interacting NlpI inhibiting substrate recognition response to low DD-endopeptidase activity, providing insight into homeostatic hydrolysis expansion.