ArticleJournal of bacteriology2007
Mutants, suppressors, and wrinkled colonies: mutant alleles of the cell division gene ftsQ point to functional domains in FtsQ and a role for domain 1C of FtsA in divisome assembly.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Conformational changes in the essential E. coli septal cell wall synthesis complex suggest an activation mechanism.Nature communications · 2023Article
- Structure of the heterotrimeric membrane protein complex FtsB-FtsL-FtsQ of the bacterial divisome.Nature communications · 2023Article
- Article
- Identification of the potential active site of the septal peptidoglycan polymerase FtsW.PLoS genetics · 2022Article
- Localization, Assembly, and Activation of the Escherichia coli Cell Division Machinery.EcoSal Plus · 2021Review
- FtsA acts through FtsW to promote cell wall synthesis during cell division inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Cell division is antagonized by the activity of peptidoglycan endopeptidases that promote cell elongation.Molecular microbiology · 2020Article
- Article
- Structural Analysis of the Interaction between the Bacterial Cell Division Proteins FtsQ and FtsB.mBio · 2018Article
- Delineating FtsQ-mediated regulation of cell division inThe Journal of biological chemistry · 2018Article
- Guiding divisome assembly and controlling its activity.Current opinion in microbiology · 2015Review
- A role for the FtsQLB complex in cytokinetic ring activation revealed by an ftsL allele that accelerates division.Molecular microbiology · 2015Article
- Roles for both FtsA and the FtsBLQ subcomplex in FtsN-stimulated cell constriction in Escherichia coli.Molecular microbiology · 2015Article
- A role for FtsA in SPOR-independent localization of the essential Escherichia coli cell division protein FtsN.Molecular microbiology · 2014Article
- Fine-mapping the contact sites of the Escherichia coli cell division proteins FtsB and FtsL on the FtsQ protein.The Journal of biological chemistry · 2013Article
- The early divisome protein FtsA interacts directly through its 1c subdomain with the cytoplasmic domain of the late divisome protein FtsN.Journal of bacteriology · 2012Article
- FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins.Molecular microbiology · 2012Article
- Role of leucine zipper motifs in association of the Escherichia coli cell division proteins FtsL and FtsB.Journal of bacteriology · 2011Article
- A model for the Escherichia coli FtsB/FtsL/FtsQ cell division complex.BMC structural biology · 2011Article
- Evidence from artificial septal targeting and site-directed mutagenesis that residues in the extracytoplasmic β domain of DivIB mediate its interaction with the divisomal transpeptidase PBP 2B.Journal of bacteriology · 2010Article
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4 authors.
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Abstract
Cell division in Escherichia coli requires the concerted action of at least 10 essential proteins. One of these proteins, FtsQ, is physically associated with multiple essential division proteins, including FtsK, FtsL, FtsB, FtsW, and FtsI. In this work we performed a genetic analysis of the ftsQ gene. Our studies identified C-terminal residues essential for FtsQ's interaction with two downstream proteins, FtsL and FtsB. Here we also describe a novel screen for cell division mutants based on a wrinkled-colony morphology, which yielded several new point mutations in ftsQ. Two of these mutations affect localization of FtsQ to midcell and together define a targeting role for FtsQ's alpha domain. Further characterization of one localization-defective mutant protein [FtsQ(V92D)] revealed an unexpected role in localization for the first 49 amino acids of FtsQ. Finally, we found a suppressor of FtsQ(V92D) that was due to a point mutation in domain 1C of FtsA, a domain previously implicated in the recruitment of divisome proteins. However, despite reports of a potential interaction between FtsA and FtsQ, suppression by FtsA(I143L) is not mediated via direct contact with FtsQ. Rather, this mutation acts as a general suppressor of division defects, which include deletions of the normally essential genes zipA and ftsK and mutations in FtsQ that affect both localization and recruitment. Together, these results reveal increasingly complex connections within the bacterial divisome.
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