ArticleThe Journal of biological chemistry2015
The Soluble Periplasmic Domains of Escherichia coli Cell Division Proteins FtsQ/FtsB/FtsL Form a Trimeric Complex with Submicromolar Affinity.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Structure and Membrane Interactions of Two Helices from Mycobacterium tuberculosis FtsL, One Transmembrane and One Amphipathic.Journal of the American Chemical Society · 2026Article
- Structure and function of Salmonella inner membrane.Archives of microbiology · 2026Review
- In Silico Druggability Assessment ofAntibiotics (Basel, Switzerland) · 2026Article
- The structural integrity of the membrane-embedded bacterial division complex FtsQBL studied with molecular dynamics simulations.Computational and structural biotechnology journal · 2023Article
- Peptide-based covalent inhibitors of protein-protein interactions.Journal of peptide science : an official publication of the European Peptide Society · 2023Review
- Covalent Proteomimetic Inhibitor of the Bacterial FtsQB Divisome Complex.Journal of the American Chemical Society · 2022Article
- 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
- Regulation of Lytic Machineries by the FtsEX Complex in the Bacterial Divisome.Sub-cellular biochemistry · 2022Article
- Computational Identification of Essential Enzymes as Potential Drug Targets inJournal of microbiology and biotechnology · 2021Article
- Treadmilling FtsZ polymers drive the directional movement of sPG-synthesis enzymes via a Brownian ratchet mechanism.Nature communications · 2021Article
- PersistenteLife · 2019Article
- 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
- Superfolder mTurquoise2Molecular microbiology · 2019Article
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- Structural Insights into the FtsQ/FtsB/FtsL Complex, a Key Component of the Divisome.Scientific reports · 2018Article
- 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
- The FtsLB subcomplex of the bacterial divisome is a tetramer with an uninterrupted FtsL helix linking the transmembrane and periplasmic regions.The Journal of biological chemistry · 2018Article
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Authors and funding
13 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cell division in Escherichia coli involves a set of essential proteins that assembles at midcell to form the so-called divisome. The divisome regulates the invagination of the inner membrane, cell wall synthesis, and inward growth of the outer membrane. One of the divisome proteins, FtsQ, plays a central but enigmatic role in cell division. This protein associates with FtsB and FtsL, which, like FtsQ, are bitopic inner membrane proteins with a large periplasmic domain (denoted FtsQp, FtsBp, and FtsLp) that is indispensable for the function of each protein. Considering the vital nature and accessible location of the FtsQBL complex, it is an attractive target for protein-protein interaction inhibitors intended to block bacterial cell division. In this study, we expressed FtsQp, FtsBp, and FtsLp individually and in combination. Upon co-expression, FtsQp was co-purified with FtsBp and FtsLp from E. coli extracts as a stable trimeric complex. FtsBp was also shown to interact with FtsQp in the absence of FtsLp albeit with lower affinity. Interactions were mapped at the C terminus of the respective domains by site-specific cross-linking. The binding affinity and 1:1:1 stoichiometry of the FtsQpBpLp complex and the FtsQpBp subcomplex were determined in complementary surface plasmon resonance, analytical ultracentrifugation, and native mass spectrometry experiments.
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