ArticleJournal of bacteriology2010
Multiple interaction domains in FtsL, a protein component of the widely conserved bacterial FtsLBQ cell division complex.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Defining the order of assembly of theJournal of bacteriology · 2026Article
- Structure and Membrane Interactions of Two Helices from Mycobacterium tuberculosis FtsL, One Transmembrane and One Amphipathic.Journal of the American Chemical Society · 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
- Molecular dissection of Class A PBP function uncovers novel features of the non-canonical Clostridioides difficile divisome complex.PLoS genetics · 2025Article
- Molecular dissection of Class A PBP function uncovers novel features of the non-canonicalbioRxiv : the preprint server for biology · 2025Article
- 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
- Plasticity in the cell division processes of obligate intracellular bacteria.Frontiers in cellular and infection microbiology · 2023Review
- Article
- The structural integrity of the membrane-embedded bacterial division complex FtsQBL studied with molecular dynamics simulations.Computational and structural biotechnology journal · 2023Article
- An Updated Model of the Divisome: Regulation of the Septal Peptidoglycan Synthesis Machinery by the Divisome.International journal of molecular sciences · 2022Review
- The coiled-coil domain of Escherichia coli FtsLB is a structurally detuned element critical for modulating its activation in bacterial cell division.The Journal of biological chemistry · 2022Article
- Mapping the FtsQBL divisome components in bacterial NTD pathogens as potential drug targets.Frontiers in 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
- Article
- Interrogating the Essential Bacterial Cell Division Protein FtsQ with Fragments Using Target Immobilized NMR Screening (TINS).International journal of molecular sciences · 2019Article
- Roles of the DedD Protein inJournal of bacteriology · 2019Article
- Article
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Authors and funding
4 authors.
Funding
Abstract
A bioinformatic analysis of nearly 400 genomes indicates that the overwhelming majority of bacteria possess homologs of the Escherichia coli proteins FtsL, FtsB, and FtsQ, three proteins essential for cell division in that bacterium. These three bitopic membrane proteins form a subcomplex in vivo, independent of the other cell division proteins. Here we analyze the domains of E. coli FtsL that are involved in the interaction with other cell division proteins and important for the assembly of the divisome. We show that FtsL, as we have found previously with FtsB, packs an enormous amount of information in its sequence for interactions with proteins upstream and downstream in the assembly pathway. Given their size, it is likely that the sole function of the complex of these two proteins is to act as a scaffold for divisome assembly.
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