ArticleCommunications biology2023
An Arg/Ala-rich helix in the N-terminal region of M. tuberculosis FtsQ is a potential membrane anchor of the Z-ring.
Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Article
- Structure and Membrane Interactions of Two Helices from Mycobacterium tuberculosis FtsL, One Transmembrane and One Amphipathic.Journal of the American Chemical Society · 2026Article
- A membrane insertion code for intrinsically disordered proteins.bioRxiv : the preprint server for biology · 2026Article
- Membrane Association of Intrinsically Disordered Proteins.Annual review of biophysics · 2025Review
- Article
- Article
- Predicting the sequence-dependent backbone dynamics of intrinsically disordered proteins.eLife · 2024Article
- Predicting the Sequence-Dependent Backbone Dynamics of Intrinsically Disordered Proteins.bioRxiv : the preprint server for biology · 2024Article
- Elucidating the Membrane Binding Process of a Disordered Protein: Dynamic Interplay of Anionic Lipids and the Polybasic Region.ACS physical chemistry Au · 2024Article
- Insights into the assembly and regulation of the bacterial divisome.Nature reviews. Microbiology · 2024Review
- Conformational ensemble-dependent lipid recognition and segregation by prenylated intrinsically disordered regions in small GTPases.Communications biology · 2023Article
- Leaflet Tensions Control the Spatio-Temporal Remodeling of Lipid Bilayers and Nanovesicles.Biomolecules · 2023Review
- Why Does Synergistic Activation of WASP, but Not N-WASP, by Cdc42 and PIPJournal of molecular biology · 2023Article
- N-WASP is competent for downstream signaling before full release from autoinhibition.The Journal of chemical physics · 2023Article
- Partial mimicry of the microtubule binding of tau by its membrane binding.Protein science : a publication of the Protein Society · 2023Article
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Authors and funding
5 authors.
Funding
Abstract
Mtb infects a quarter of the worldwide population. Most drugs for treating tuberculosis target cell growth and division. With rising drug resistance, it becomes ever more urgent to better understand Mtb cell division. This process begins with the formation of the Z-ring via polymerization of FtsZ and anchoring of the Z-ring to the inner membrane. Here we show that the transmembrane protein FtsQ is a potential membrane anchor of the Mtb Z-ring. In the otherwise disordered cytoplasmic region of FtsQ, a 29-residue, Arg/Ala-rich α-helix is formed that interacts with upstream acidic residues in solution and with acidic lipids at the membrane surface. This helix also binds to the GTPase domain of FtsZ, with implications for drug binding and Z-ring formation.
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