PMID- 26099469
OWN - NLM
STAT- MEDLINE
DCOM- 20160405
LR  - 20181113
IS  - 2041-1723 (Electronic)
IS  - 2041-1723 (Linking)
VI  - 6
DP  - 2015 Jun 23
TI  - The bacterial tubulin FtsZ requires its intrinsically disordered linker to direct 
      robust cell wall construction.
PG  - 7281
LID - 10.1038/ncomms8281 [doi]
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 (DeltaCTL) is lethal: cells become 
      filamentous, form envelope bulges and lyse, resembling treatment with beta-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 
      DeltaCTL; however, cells expressing DeltaCTL exhibit reduced peptidoglycan crosslinking 
      and longer glycan strands than wild type. Importantly, midcell proteins are still 
      recruited to sites of DeltaCTL assembly. We propose that FtsZ regulates peptidoglycan 
      metabolism through a CTL-dependent mechanism that extends beyond simple protein 
      recruitment.
FAU - Sundararajan, Kousik
AU  - Sundararajan K
AD  - Department of Biological Chemistry, Johns Hopkins University School of Medicine, 
      Baltimore, Maryland 21205, USA.
FAU - Miguel, Amanda
AU  - Miguel A
AD  - Department of Bioengineering, Stanford University, Stanford, California 94305, 
      USA.
FAU - Desmarais, Samantha M
AU  - Desmarais SM
AD  - Department of Bioengineering, Stanford University, Stanford, California 94305, 
      USA.
FAU - Meier, Elizabeth L
AU  - Meier EL
AD  - Department of Biological Chemistry, Johns Hopkins University School of Medicine, 
      Baltimore, Maryland 21205, USA.
FAU - Casey Huang, Kerwyn
AU  - Casey Huang K
AD  - 1] Department of Bioengineering, Stanford University, Stanford, California 94305, 
      USA [2] Department of Microbiology and Immunology, Stanford University School of 
      Medicine, Stanford, California 94305, USA.
FAU - Goley, Erin D
AU  - Goley ED
AUID- ORCID: 0000000285182303
AD  - Department of Biological Chemistry, Johns Hopkins University School of Medicine, 
      Baltimore, Maryland 21205, USA.
LA  - eng
GR  - DP2 OD006466/OD/NIH HHS/United States
GR  - T32 GM007445/GM/NIGMS NIH HHS/United States
GR  - T32 GM008294/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
DEP - 20150623
PL  - England
TA  - Nat Commun
JT  - Nature communications
JID - 101528555
RN  - 0 (Bacterial Proteins)
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (FtsZ protein, Bacteria)
RN  - 0 (Intrinsically Disordered Proteins)
RN  - 0 (Peptidoglycan)
SB  - IM
MH  - Bacterial Proteins/*metabolism/ultrastructure
MH  - *Caulobacter crescentus
MH  - *Cell Division
MH  - *Cell Shape
MH  - Cell Wall/*metabolism/ultrastructure
MH  - Cytoskeletal Proteins/*metabolism/ultrastructure
MH  - Immunoblotting
MH  - Intrinsically Disordered Proteins/*metabolism/ultrastructure
MH  - Microscopy
MH  - Microscopy, Electron, Transmission
MH  - Peptidoglycan/*metabolism/ultrastructure
MH  - Polymerization
PMC - PMC4532373
MID - NIHMS684980
COIS- Competing Financial interests The authors declare no competing financial 
      interests.
EDAT- 2015/06/24 06:00
MHDA- 2016/04/06 06:00
PMCR- 2015/12/23
CRDT- 2015/06/24 06:00
PHST- 2015/02/10 00:00 [received]
PHST- 2015/04/26 00:00 [accepted]
PHST- 2015/06/24 06:00 [entrez]
PHST- 2015/06/24 06:00 [pubmed]
PHST- 2016/04/06 06:00 [medline]
PHST- 2015/12/23 00:00 [pmc-release]
AID - ncomms8281 [pii]
AID - 10.1038/ncomms8281 [doi]
PST - epublish
SO  - Nat Commun. 2015 Jun 23;6:7281. doi: 10.1038/ncomms8281.