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Chem Biol. 2015 Sep 17;22(9):1217-27. doi: 10.1016/j.chembiol.2015.08.009. Epub 2015 Sep 10.

Disassembly of a Medial Transenvelope Structure by Antibiotics during Intracellular Division.

Author information

1
Department of Laboratories, Institute of Microbiology, University Hospital Center and University of Lausanne, Lausanne 1011, Switzerland.
2
Department of Microbiology & Molecular Medicine, Institute of Genetics & Genomics in Geneva (iGE3), Faculty of Medicine/CMU, University of Geneva, Geneva 1211, Switzerland.
3
Department of Microbiology & Molecular Medicine, Institute of Genetics & Genomics in Geneva (iGE3), Faculty of Medicine/CMU, University of Geneva, Geneva 1211, Switzerland. Electronic address: patrick.viollier@unige.ch.
4
Department of Laboratories, Institute of Microbiology, University Hospital Center and University of Lausanne, Lausanne 1011, Switzerland. Electronic address: gilbert.greub@chuv.ch.

Abstract

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.

KEYWORDS:

Waddlia chondrophila; cell division; cell wall; chlamydia-related bacteria; contractile ring; peptidoglycan; peptidoglycan associated lipoprotein

PMID:
26364930
DOI:
10.1016/j.chembiol.2015.08.009
[Indexed for MEDLINE]
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