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PMID: 9622350 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Control of cell shape and elongation by the rodA gene in Bacillus subtilis.

Molecular microbiology ·Vol. 28 ·No. 2 ·1998-04-00 ·Pages 235-47

Henriques AO, Glaser P, Piggot PJ, Moran CP

Abstract

The Escherichia coli rodA and ftsW genes and the spoVE gene of Bacillus subtilis encode membrane proteins that control peptidoglycan synthesis during cellular elongation, division and sporulation respectively. While rodA and ftsW are essential genes in E. coli, the B. subtilis spoVE gene is dispensable for growth and is only required for the synthesis of the spore cortex peptidoglycan. In this work, we report on the characterization of a B. subtilis gene, designated rodA, encoding a homologue of E. coli RodA. We found that the growth of a B. subtilis strain carrying a fusion of rodA to the IPTG-inducible Pspac promoter is inducer dependent. Limiting concentrations of inducer caused the formation of spherical cells, which eventually lysed. An increase in the level of IPTG induced a sphere-to-short rod transition that re-established viability. Higher levels of inducer restored normal cell length. Staining of the septal or polar cap peptidoglycan by a fluorescent lectin was unaffected during growth of the mutant under restrictive conditions. Our results suggest that rodA functions in maintaining the rod shape of the cell and that this function is essential for viability. In addition, RodA has an irreplaceable role in the extension of the lateral walls of the cell. Electron microscopy observations support these conclusions. The ultrastructural analysis further suggests that the growth arrest that accompanies loss of the rod shape is caused by the cell's inability to construct a division septum capable of spanning the enlarged cell. RodA is similar over its entire length to members of a large protein family (SEDS, for shape, elongation, division and sporulation). Members of the SEDS family are probably present in all eubacteria that synthesize peptidoglycan as part of their cell envelope.

MeSH Terms
Artificial Gene Fusion Bacillus subtilis/cytology,genetics,growth & development,ultrastructure Bacterial Proteins/genetics Escherichia coli/genetics Escherichia coli Proteins Genes, Bacterial/genetics,physiology Membrane Proteins Microscopy, Electron Microscopy, Fluorescence Molecular Sequence Data Soil Microbiology Time Factors
Chemicals
Bacterial Proteins Escherichia coli Proteins Membrane Proteins mrdB protein, E coli
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Henriques A O
Emory University, School of Medicine, Department of Microbiology and Immunology, Atlanta, GA 30322, USA.
Glaser P
Piggot P J
Moran C P
Article Info
Journal
Molecular microbiology
Abbr.
Mol Microbiol
ISSN
0950-382X
Published
1998-04-00
Pages
235-47
Language
English
Region
England
NLM ID
8712028
Subset
IM
Grants
NIGMS NIH HHS · GM43577 · United States
NIGMS NIH HHS · GM54395 · United States
Databases
GENBANK
D90913, M22857, U30821, U32688, U32793, U58049, X51419, X55034, X96685, Z70722, Z80233, Z95388
SWISSPROT
P39604
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