ArticleJournal of bacteriology2000
Analysis of the essential cell division gene ftsL of Bacillus subtilis by mutagenesis and heterologous complementation.
Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Defining the order of assembly of theJournal of bacteriology · 2026Article
- Defining the order of assembly of thebioRxiv : the preprint server for biology · 2026Article
- Repression of mab_1999 impairs growth and alters cellular morphology of Mycobacterium abscessus.BMC microbiology · 2025Article
- Control of morphogenesis during theScience advances · 2025Article
- Proline substitutions in a Mip-like peptidyl-prolylBiochimie open · 2015Article
- DNA repair and genome maintenance in Bacillus subtilis.Microbiology and molecular biology reviews : MMBR · 2012Review
- Role of leucine zipper motifs in association of the Escherichia coli cell division proteins FtsL and FtsB.Journal of bacteriology · 2011Article
- Assembly of the Caulobacter cell division machine.Molecular microbiology · 2011Article
- Bacterial growth and cell division: a mycobacterial perspective.Microbiology and molecular biology reviews : MMBR · 2008Review
- Streptomyces coelicolor genes ftsL and divIC play a role in cell division but are dispensable for colony formation.Journal of bacteriology · 2007Article
- Domain architecture and structure of the bacterial cell division protein DivIB.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Cytokinesis in bacteria.Microbiology and molecular biology reviews : MMBR · 2003Review
- Search for potential vaccine candidate open reading frames in the Bacillus anthracis virulence plasmid pXO1: in silico and in vitro screening.Infection and immunity · 2002Article
- Cell Cycle Machinery in Bacillus subtilis.Sub-cellular biochemistryReview
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2 authors.
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Abstract
The ftsL gene is required for the initiation of cell division in a broad range of bacteria. Bacillus subtilis ftsL encodes a 13-kDa protein with a membrane-spanning domain near its N terminus. The external C-terminal domain has features of an alpha-helical leucine zipper, which is likely to be involved in the heterodimerization with another division protein, DivIC. To determine what residues are important for FtsL function, we used both random and site-directed mutagenesis. Unexpectedly, all chemically induced mutations fell into two clear classes, those either weakening the ribosome-binding site or producing a stop codon. It appears that the random mutagenesis was efficient, so many missense mutations must have been generated but with no phenotypic effect. Substitutions affecting hydrophobic residues in the putative coiled-coil domain, introduced by site-directed mutagenesis, also gave no observable phenotype except for insertion of a helix-breaking proline residue, which destroyed FtsL function. ftsL homologues cloned from three diverse Bacillus species, Bacillus licheniformis, Bacillus badius, and Bacillus circulans, could complement an ftsL null mutation in B. subtilis, even though up to 66% of the amino acid residues of the predicted proteins were different from B. subtilis FtsL. However, the ftsL gene from Staphylococcus aureus (whose product has 73% of its amino acids different from those of the B. subtilis ftsL product) was not functional. We conclude that FtsL is a highly malleable protein that can accommodate a large number of sequence changes without loss of function.
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