ArticleThe Journal of biological chemistry2018
The chloroplast division protein ARC6 acts to inhibit disassembly of GDP-bound FtsZ2.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Plant organelle division orchestrated by the mosaic machinery of endosymbiotic relics and eukaryotic host factors.Plant physiology · 2026Review
- Enhanced chloroplast FtsZ-ring constriction by the ARC6-ARC3 module inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Chloroplast Z-ring dynamics is governed by conserved core regions of evolutionarily divergent FtsZs.Frontiers in plant science · 2025Article
- Transcriptomic study of the role of MeFtsZ2-1 in pigment accumulation in cassava leaves.BMC genomics · 2024Article
- PDV1 and PDV2 Differentially Affect Remodeling and Assembly of the Chloroplast DRP5B Ring.Plant physiology · 2020Article
- ARC3 Activation by PARC6 Promotes FtsZ-Ring Remodeling at the Chloroplast Division Site.The Plant cell · 2019Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chloroplasts host photosynthesis and fulfill other metabolic functions that are essential to plant life. They have to divide by binary fission to maintain their numbers throughout cycles of cell division. Chloroplast division is achieved by a complex ring-shaped division machinery located on both the inner (stromal) and the outer (cytosolic) side of the chloroplast envelope. The inner division ring (termed the Z ring) is formed by the assembly of tubulin-like FtsZ1 and FtsZ2 proteins. ARC6 is a key chloroplast division protein that interacts with the Z ring. ARC6 spans the inner envelope membrane, is known to stabilize or maintain the Z ring, and anchors the Z ring to the inner membrane through interaction with FtsZ2. The underlying mechanism of Z ring stabilization is not well-understood. Here, biochemical and structural characterization of ARC6 was conducted using light scattering, sedimentation, and light and transmission EM. The recombinant protein was purified as a dimer. The results indicated that a truncated form of ARC6 (tARC6), representing the stromal portion of ARC6, affects FtsZ2 assembly without forming higher-order structures and exerts its effect via FtsZ2 dynamics. tARC6 prevented GDP-induced FtsZ2 disassembly and caused a significant net increase in FtsZ2 assembly when GDP was present. Single particle analysis and 3D reconstruction were performed to elucidate the structural basis of ARC6 activity. Together, the data reveal that a dimeric form of tARC6 binds to FtsZ2 filaments and does not increase FtsZ polymerization rates but rather inhibits GDP-associated FtsZ2 disassembly.
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