Scientific article

Disassembly of a Medial Transenvelope Structure by Antibiotics during Intracellular Division

Published inChemistry & biology, vol. 22, no. 9, p. 1217-1227
Publication date2015

Chlamydiales possess a minimal but functional peptidoglycan precursor biosynthetic and remodeling pathway involved in the assembly of the division septum by an atypical cytokinetic machine and cryptic or modified peptidoglycan-like structure (PGLS). How this reduced cytokinetic machine collectively coordinates the invagination of the envelope has not yet been explored in Chlamydiales. In other Gram-negative bacteria, peptidoglycan provides anchor points that connect the outer membrane to the peptidoglycan during constriction using the Pal-Tol complex. Purifying PGLS and associated proteins from the chlamydial pathogen Waddlia chondrophila, we unearthed the Pal protein as a peptidoglycan-binding protein that localizes to the chlamydial division septum along with other components of the Pal-Tol complex. Together, our PGLS characterization and peptidoglycan-binding assays support the notion that diaminopimelic acid is an important determinant recruiting Pal to the division plane to coordinate the invagination of all envelope layers with the conserved Pal-Tol complex, even during osmotically protected intracellular growth.

Citation (ISO format)
JACQUIER, Nicolas et al. Disassembly of a Medial Transenvelope Structure by Antibiotics during Intracellular Division. In: Chemistry & biology, 2015, vol. 22, n° 9, p. 1217–1227. doi: 10.1016/j.chembiol.2015.08.009
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Article (Published version)
ISSN of the journal1074-5521

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