Amidation of glutamate residues in mycobacterial peptidoglycan is essential for cell wall cross-linking.

ABSTRACT:

Introduction

Mycobacteria assemble a complex cell wall with cross-linked peptidoglycan (PG) which plays an essential role in maintenance of cell wall integrity and tolerance to osmotic pressure. We previously demonstrated that various hydrolytic enzymes are required to remodel PG during essential processes such as cell elongation and septal hydrolysis. Here, we explore the chemistry associated with PG cross-linking, specifically the requirement for amidation of the D-glutamate residue found in PG precursors.

Methods

Synthetic fluorescent probes were used to assess PG remodelling dynamics in live bacteria. Fluorescence microscopy was used to assess protein localization in live bacteria and CRISPR-interference was used to construct targeted gene knockdown strains. Time-lapse m

SUBMITTER: Shaku MT 

PROVIDER: S-EPMC10484409 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature