The tubulin homologue FtsZ contributes to cell elongation by guiding cell wall precursor synthesis in Caulobacter crescentus

TY - JOUR

T1 - The tubulin homologue FtsZ contributes to cell elongation by guiding cell wall precursor synthesis in Caulobacter crescentus

AU - Aaron, Michelle

AU - Charbon, Godefroid

AU - Lam, Hubert

AU - Schwarz, Heinz

AU - Vollmer, Waldemar

AU - Jacobs-Wagner, Christine

PY - 2007/5

Y1 - 2007/5

N2 - The tubulin homologue FtsZ is well known for its essential function in bacterial cell division. Here, we show that in Caulobacter crescentus, FtsZ also plays a major role in cell elongation by spatially regulating the location of MurG, which produces the essential lipid II peptidoglycan cell wall precursor. The early assembly of FtsZ into a highly mobile ring-like structure during cell elongation is quickly followed by the recruitment of MurG and a major redirection of peptidoglycan precursor synthesis to the midcell region. These FtsZ-dependent events occur well before cell constriction and contribute to cell elongation. In the absence of FtsZ, MurG fails to accumulate near midcell and cell elongation proceeds unperturbed in appearance by insertion of peptidoglycan material along the entire sidewalls. Evidence suggests that bacteria use both a FtsZ-independent and a FtsZ-dependent mode of peptidoglycan synthesis to elongate, the importance of each mode depending on the timing of FtsZ assembly during elongation.

AB - The tubulin homologue FtsZ is well known for its essential function in bacterial cell division. Here, we show that in Caulobacter crescentus, FtsZ also plays a major role in cell elongation by spatially regulating the location of MurG, which produces the essential lipid II peptidoglycan cell wall precursor. The early assembly of FtsZ into a highly mobile ring-like structure during cell elongation is quickly followed by the recruitment of MurG and a major redirection of peptidoglycan precursor synthesis to the midcell region. These FtsZ-dependent events occur well before cell constriction and contribute to cell elongation. In the absence of FtsZ, MurG fails to accumulate near midcell and cell elongation proceeds unperturbed in appearance by insertion of peptidoglycan material along the entire sidewalls. Evidence suggests that bacteria use both a FtsZ-independent and a FtsZ-dependent mode of peptidoglycan synthesis to elongate, the importance of each mode depending on the timing of FtsZ assembly during elongation.

KW - Bacterial Outer Membrane Proteins/analysis

KW - Bacterial Proteins/analysis

KW - Caulobacter crescentus/cytology

KW - Cell Wall/chemistry

KW - Cytoskeletal Proteins/analysis

KW - Microscopy, Confocal

KW - Microscopy, Fluorescence

KW - N-Acetylglucosaminyltransferases/analysis

KW - Silver Staining

KW - Uridine Diphosphate N-Acetylmuramic Acid/analogs & derivatives

U2 - 10.1111/j.1365-2958.2007.05720.x

DO - 10.1111/j.1365-2958.2007.05720.x

M3 - Journal article

C2 - 17501919

SN - 0950-382X

VL - 64

SP - 938

EP - 952

JO - Molecular Microbiology

JF - Molecular Microbiology

IS - 4

ER -