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PMID: 17501919 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

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

Molecular microbiology ·Vol. 64 ·No. 4 ·2007-05-00 ·Pages 938-52

Aaron M, Charbon G, Lam H, Schwarz H, Vollmer W, Jacobs-Wagner C

Abstract

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.

MeSH Terms
Bacterial Outer Membrane Proteins/analysis,metabolism Bacterial Proteins/analysis,metabolism Caulobacter crescentus/cytology,growth & development,metabolism Cell Wall/chemistry,metabolism Cytoskeletal Proteins/analysis,metabolism Microscopy, Confocal Microscopy, Fluorescence N-Acetylglucosaminyltransferases/analysis,metabolism Silver Staining Uridine Diphosphate N-Acetylmuramic Acid/analogs & derivatives,biosynthesis
Chemicals
Bacterial Outer Membrane Proteins Bacterial Proteins Cytoskeletal Proteins FtsZ protein, Bacteria Uridine Diphosphate N-Acetylmuramic Acid muramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenol N-Acetylglucosaminyltransferases UDP-N-acetylglucosamine-N-acetylmuramyl-(pentapeptide)pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Aaron Michelle
Department of Molecular, Cellular, and Developmental Biology, and Microbiology Program, Yale University, New Haven, CT 06520, USA.
Charbon Godefroid
Lam Hubert
Schwarz Heinz
Vollmer Waldemar
Jacobs-Wagner Christine
Article Info
Journal
Molecular microbiology
Abbr.
Mol Microbiol
ISSN
0950-382X
Published
2007-05-00
Pages
938-52
Language
English
Region
England
NLM ID
8712028
Subset
IM
Grants
NIGMS NIH HHS · GM065835 · United States
NIGMS NIH HHS · GM076698 · United States
Corrections
CommentIn
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