TY - JOUR
T1 - The bacterial tubulin FtsZ requires its intrinsically disordered linker to direct robust cell wall construction
AU - Sundararajan, Kousik
AU - Miguel, Amanda
AU - Desmarais, Samantha M.
AU - Meier, Elizabeth L.
AU - Casey Huang, Kerwyn
AU - Goley, Erin D.
N1 - Funding Information:
We are grateful to Patrick Viollier for SpmX antiserum; to Yves Brun, Erkin Kuru and Michael van Nieuwenzhe for HADA and guidance in its use; to Matt Welch and Rebecca Lamason for R. parkeri genomic DNA; to Arash Komeili for M. magneticum AMB-1 genomic DNA; to Yves Brun and Ellen Quardokus for assistance with TEM and for hosting ELM; to Peter Chien for advice on protein turnover assays; and to Lucy Shapiro and Martin Thanbichler for strains. We also thank Jie Xiao and the Xiao laboratory for helpful discussions. This work was funded by the JHUSOM (to E.D.G.), an NIH Director’s New Innovator Award DP2OD006466 (to K.C.H.) and an NSF Graduate Research Fellowship (to A.M.).
Publisher Copyright:
© 2015 Macmillan Publishers Limited.
PY - 2015/6/23
Y1 - 2015/6/23
N2 - The bacterial GTPase FtsZ forms a cytokinetic ring at midcell, recruits the division machinery and orchestrates membrane and peptidoglycan cell wall invagination. However, the mechanism for FtsZ regulation of peptidoglycan metabolism is unknown. The FtsZ GTPase domain is separated from its membrane-anchoring C-terminal conserved (CTC) peptide by a disordered C-terminal linker (CTL). Here we investigate CTL function in Caulobacter crescentus. Strikingly, production of FtsZ lacking the CTL (δCTL) is lethal: cells become filamentous, form envelope bulges and lyse, resembling treatment with b-lactam antibiotics. This phenotype is produced by FtsZ polymers bearing the CTC and a CTL shorter than 14 residues. Peptidoglycan synthesis still occurs downstream of δCTL; however, cells expressing δCTL exhibit reduced peptidoglycan crosslinking and longer glycan strands than wild type. Importantly, midcell proteins are still recruited to sites of δCTL assembly. We propose that FtsZ regulates peptidoglycan metabolism through a CTL-dependent mechanism that extends beyond simple protein recruitment.
AB - The bacterial GTPase FtsZ forms a cytokinetic ring at midcell, recruits the division machinery and orchestrates membrane and peptidoglycan cell wall invagination. However, the mechanism for FtsZ regulation of peptidoglycan metabolism is unknown. The FtsZ GTPase domain is separated from its membrane-anchoring C-terminal conserved (CTC) peptide by a disordered C-terminal linker (CTL). Here we investigate CTL function in Caulobacter crescentus. Strikingly, production of FtsZ lacking the CTL (δCTL) is lethal: cells become filamentous, form envelope bulges and lyse, resembling treatment with b-lactam antibiotics. This phenotype is produced by FtsZ polymers bearing the CTC and a CTL shorter than 14 residues. Peptidoglycan synthesis still occurs downstream of δCTL; however, cells expressing δCTL exhibit reduced peptidoglycan crosslinking and longer glycan strands than wild type. Importantly, midcell proteins are still recruited to sites of δCTL assembly. We propose that FtsZ regulates peptidoglycan metabolism through a CTL-dependent mechanism that extends beyond simple protein recruitment.
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U2 - 10.1038/ncomms8281
DO - 10.1038/ncomms8281
M3 - Article
C2 - 26099469
AN - SCOPUS:84934901914
VL - 6
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
M1 - 7281
ER -