The caulobacter Tol-Pal complex is essential for outer membrane integrity and the positioning of a polar localization factor.
Cell division in Caulobacter crescentus involves constriction and fission of the inner membrane (IM) followed about 20 min later by fission of the outer membrane (OM) and daughter cell separation. In contrast to Escherichia coli, the Caulobacter Tol-Pal complex is essential. Cryo-electron microscopy images of the Caulobacter cell envelope exhibited outer membrane disruption, and cells failed to complete cell division in TolA, TolB, or Pal mutant strains. In wild-type cells, components of the Tol-Pal complex localize to the division plane in early predivisional cells and remain predominantly at the new pole of swarmer and stalked progeny upon completion of division. The Tol-Pal complex is required to maintain the position of the transmembrane TipN polar marker, and indirectly the PleC histidine kinase, at the cell pole, but it is not required for the polar maintenance of other transmembrane and membrane-associated polar proteins tested. Coimmunoprecipitation experiments show that both TolA and Pal interact directly or indirectly with TipN. We propose that disruption of the trans-envelope Tol-Pal complex releases TipN from its subcellular position. The Caulobacter Tol-Pal complex is thus a key component of cell envelope structure and function, mediating OM constriction at the final step of cell division as well as the positioning of a protein localization factor.
Yeh
Yi-Chun
YC
Department of Developmental Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Comolli
Luis R
LR
Downing
Kenneth H
KH
Shapiro
Lucy
L
McAdams
Harley H
HH
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D016935:Caulobacter crescentus / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure*; D002455:Cell Division / Q000235:genetics / Q000502:physiology; D020285:Cryoelectron Microscopy; D015151:Immunoblotting; D047468:Immunoprecipitation; D008855:Microscopy, Electron, Scanning; D008856:Microscopy, Fluorescence; D010457:Peptidoglycan / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D011485:Protein Binding
D001426:Bacterial Proteins; D010457:Peptidoglycan