trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli

Fission of bacterial cells involves the co-ordinated invagination of the envelope layers. Invagination of the cytoplasmic membrane (IM) and peptidoglycan (PG) layer is likely driven by the septal ring organelle. Invagination of the outer membrane (OM) in Gram-negative species is thought to occur pas...

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Bibliographic Details
Published in:Molecular microbiology 2007-02, Vol.63 (4), p.1008-1025
Main Authors: Gerding, Matthew A, Ogata, Yasuyuki, Pecora, Nicole D, Niki, Hironori, de Boer, Piet A.J
Format: Article
Language:English
Subjects:
Bacterial Outer Membrane Proteins - genetics
Bacterial Outer Membrane Proteins - metabolism
Base Sequence
Biological and medical sciences
Cell Division
Cytoplasm - metabolism
E coli
Escherichia coli - cytology
Escherichia coli - physiology
Escherichia coli Proteins - genetics
Escherichia coli Proteins - metabolism
Fundamental and applied biological sciences. Psychology
Green Fluorescent Proteins - genetics
Green Fluorescent Proteins - metabolism
Intracellular Membranes - metabolism
Lipoproteins - genetics
Lipoproteins - metabolism
Membrane Proteins - genetics
Membrane Proteins - metabolism
Membranes
Microbiology
Molecular Sequence Data
Multiprotein Complexes
Mutation
Peptidoglycan - genetics
Peptidoglycan - metabolism
Periplasmic Proteins - genetics
Periplasmic Proteins - metabolism
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
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Summary:Fission of bacterial cells involves the co-ordinated invagination of the envelope layers. Invagination of the cytoplasmic membrane (IM) and peptidoglycan (PG) layer is likely driven by the septal ring organelle. Invagination of the outer membrane (OM) in Gram-negative species is thought to occur passively via its tethering to the underlying PG layer with generally distributed PG-binding OM (lipo)proteins. The Tol-Pal system is energized by proton motive force and is well conserved in Gram-negative bacteria. It consists of five proteins that can connect the OM to both the PG and IM layers via protein-PG and protein-protein interactions. Although the system is needed to maintain full OM integrity, and for class A colicins and filamentous phages to enter cells, its precise role has remained unclear. We show that all five components accumulate at constriction sites in Escherichia coli and that mutants lacking an intact system suffer delayed OM invagination and contain large OM blebs at constriction sites and cell poles. We propose that Tol-Pal constitutes a dynamic subcomplex of the division apparatus in Gram-negative bacteria that consumes energy to establish transient trans-envelope connections at/near the septal ring to draw the OM onto the invaginating PG and IM layers during constriction.
ISSN:0950-382X
1365-2958
DOI:10.1111/j.1365-2958.2006.05571.x