ArticleThe Journal of biological chemistry2010
GTP-dependent heteropolymer formation and bundling of chloroplast FtsZ1 and FtsZ2.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Dual Cytoplasmic and Chloroplastic Mechanisms Fine-Tune Chloroplast Division through ARC3 Protein Stability.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Differential GTP-dependent in-vitro polymerization of recombinant Physcomitrella FtsZ proteins.Scientific reports · 2025Article
- Chloroplast Z-ring dynamics is governed by conserved core regions of evolutionarily divergent FtsZs.Frontiers in plant science · 2025Article
- Evolution and Functional Differentiation of the C-terminal Motifs of FtsZs During Plant Evolution.Molecular biology and evolution · 2024Article
- Article
- A novel amphiphilic motif at the C-terminus of FtsZ1 facilitates chloroplast division.The Plant cell · 2022Article
- Assembly properties of the bacterial tubulin homolog FtsZ from the cyanobacteriumThe Journal of biological chemistry · 2019Article
- Allelic Variation in the Chloroplast Division GenePlant physiology · 2019Article
- Agrobacterium tumefaciens divisome proteins regulate the transition from polar growth to cell division.Molecular microbiology · 2019Article
- ARC3 Activation by PARC6 Promotes FtsZ-Ring Remodeling at the Chloroplast Division Site.The Plant cell · 2019Article
- MCD1 Associates with FtsZ Filaments via the Membrane-Tethering Protein ARC6 to Guide Chloroplast Division.The Plant cell · 2018Article
- The chloroplast division protein ARC6 acts to inhibit disassembly of GDP-bound FtsZ2.The Journal of biological chemistry · 2018Article
- Bacterial Heterologous Expression System for Reconstitution of Chloroplast Inner Division Ring and Evaluation of Its Contributors.International journal of molecular sciences · 2018Review
- The Molecular Machinery of Chloroplast Division.Plant physiology · 2018Review
- Conserved Dynamics of Chloroplast Cytoskeletal FtsZ Proteins Across Photosynthetic Lineages.Plant physiology · 2018Article
- Article
- Variations in chloroplast movement and chlorophyll fluorescence among chloroplast division mutants under light stress.Journal of experimental botany · 2017Article
- ARC6-mediated Z ring-like structure formation of prokaryote-descended chloroplast FtsZ in Escherichia coli.Scientific reports · 2017Article
- The Chloroplast Tubulin Homologs FtsZA and FtsZB from the Red AlgaThe Journal of biological chemistry · 2017Article
- PDV2 has a dosage effect on chloroplast division in Arabidopsis.Plant cell reports · 2017Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteria and chloroplasts require the ring-forming cytoskeletal protein FtsZ for division. Although bacteria accomplish division with a single FtsZ, plant chloroplasts require two FtsZ types for division, FtsZ1 and FtsZ2. These proteins colocalize to a mid-plastid Z ring, but their biochemical relationship is poorly understood. We investigated the in vitro behavior of recombinant FtsZ1 and FtsZ2 separately and together. Both proteins bind and hydrolyze GTP, although GTPase activities are low compared with the activity of Escherichia coli FtsZ. Each protein undergoes GTP-dependent assembly into thin protofilaments in the presence of calcium as a stabilizing agent, similar to bacterial FtsZ. In contrast, when mixed without calcium, FtsZ1 and FtsZ2 exhibit slightly elevated GTPase activity and coassembly into extensively bundled protofilaments. Coassembly is enhanced by FtsZ1, suggesting that it promotes lateral interactions between protofilaments. Experiments with GTPase-deficient mutants reveal that FtsZ1 and FtsZ2 form heteropolymers. Maximum coassembly occurs in reactions containing equimolar FtsZ1 and FtsZ2, but significant coassembly occurs at other stoichiometries. The FtsZ1:FtsZ2 ratio in coassembled structures mirrors their input ratio, suggesting plasticity in protofilament and/or bundle composition. This behavior contrasts with that of alpha- and beta-tubulin and the bacterial tubulin-like proteins BtubA and BtubB, which coassemble in a strict 1:1 stoichiometry. Our findings raise the possibility that plasticity in FtsZ filament composition and heteropolymerization-induced bundling could have been a driving force for the coevolution of FtsZ1 and FtsZ2 in the green lineage, perhaps arising from an enhanced capacity for the regulation of Z ring composition and activity in vivo.
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