MCD1 Associates with FtsZ Filaments via the Membrane-Tethering Protein ARC6 to Guide Chloroplast Division

Chen, Li; Sun, Bai Tao; Wei, Gao; Zhang, Qi-yang; Yuan, Huan; Zhang, Min

doi:10.1105/tpc.18.00189

Cited by 17 publications

(23 citation statements)

References 58 publications

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“…Among the known mid-plastid-localizing proteins, DRP5B (ARC5) and PDV1 clearly show a discontinuous, "array-of-dot"-like localization pattern surrounding the division site, as revealed by GFP tagging (for DRP5B and PDV1) and immunofluorescence microcopy (for DRP5B) (Miyagishima et al, 2006;Okazaki et al, 2009;Miyagishima et al, 2011). Components of the chloroplast division site-determining Min system, including AtMinD1, AtMinE1, and MCD1 (Osteryoung and Pyke, 2014), also appear to exhibit a punctate pattern, as revealed by immunofluorescence microcopy (Nakanishi et al, 2009;Fujiwara et al, 2009a;Miyagishima et al, 2011;Chen et al, 2018b). Nevertheless, the observed punctate signals of AtMinD1, AtMinE1, and MCD1 were generally smaller, more varied in size, and more irregularly aligned along the division plane than those of DRP5B and PDV1 (e.g., Figure 4.3 in Miyagishima et al, 2011).…”

Section: Dynamics Of Parc6 At the Plastid Division Sitementioning

confidence: 95%

Arabidopsis PARC6 Is Critical for Plastid Morphogenesis in Pavement, Trichome, and Guard Cells in Leaf Epidermis

et al. 2020

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Recently, a recessive Arabidopsis thaliana mutant with abundant stromules in leaf epidermal pavement cells was visually screened and isolated. The gene responsible for this mutant phenotype was identified as PARC6, a chloroplast division site regulator gene. The mutant allele parc6-5 carried two point mutations (G62R and W700stop) at the N-and C-terminal ends of the coding sequence, respectively. Here, we further characterized parc6-5 and other parc6 mutant alleles, and showed that PARC6 plays a critical role in plastid morphogenesis in all cell types of the leaf epidermis: pavement cells, trichome cells, and guard cells. Transient expression of PARC6 transit peptide (TP) fused to the green fluorescent protein (GFP) in plant cells showed that the G62R mutation has no or little effect on the TP activity of the PARC6 Nterminal region. Then, plastid morphology was microscopically analyzed in the leaf epidermis of wild-type (WT) and parc6 mutants (parc6-1, parc6-3, parc6-4 and parc6-5) with the aid of stroma-targeted fluorescent proteins. In parc6 pavement cells, plastids often assumed aberrant grape-like morphology, similar to those in severe plastid division mutants, atminE1, and arc6. In parc6 trichome cells, plastids exhibited extreme grape-like aggregations, without the production of giant plastids (>6 µm diameter), as a general phenotype. In parc6 guard cells, plastids exhibited a variety of abnormal phenotypes, including reduced number, enlarged size, and activated stromules, similar to those in atminE1 and arc6 guard cells. Nevertheless, unlike atminE1 and arc6, parc6 exhibited a low number of mini-chloroplasts (< 2 µm diameter) and rarely produced chloroplast-deficient guard cells. Importantly, unlike parc6, the chloroplast division site mutant arc11 exhibited WT-like plastid phenotypes in trichome and guard cells. Finally, observation of parc6 complementation lines expressing a functional PARC6-GFP protein indicated that PARC6-GFP formed a ring-like structure in both constricting and non-constricting chloroplasts, and that PARC6 dynamically changes its configuration during the process of chloroplast division.

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Section: Dynamics Of Parc6 At the Plastid Division Sitementioning

confidence: 95%

Arabidopsis PARC6 Is Critical for Plastid Morphogenesis in Pavement, Trichome, and Guard Cells in Leaf Epidermis

et al. 2020

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“…The Z ring is confined to the mid-chloroplast, and the formation of the Z ring requires the chloroplast Min system, which includes ARC3, MinD1, and MinE1 9 , 24 , 27 , 29 – 32 . Multiple chloroplast division site 1 (MCD1) is another plant-specific protein that is required for Z ring positioning 33 , 34 . It was previously shown that MCD1 interacted with ARC6 in the stroma and interacted with FtsZ2 in an ARC6-dependent manner 33 .…”

Section: Introductionmentioning

confidence: 99%

“…Multiple chloroplast division site 1 (MCD1) is another plant-specific protein that is required for Z ring positioning 33 , 34 . It was previously shown that MCD1 interacted with ARC6 in the stroma and interacted with FtsZ2 in an ARC6-dependent manner 33 .…”

Section: Introductionmentioning

confidence: 99%

Mutation of SlARC6 leads to tissue-specific defects in chloroplast development in tomato

et al. 2021

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The proliferation and development of chloroplasts are important for maintaining the normal chloroplast population in plant tissues. Most studies have focused on chloroplast maintenance in leaves. In this study, we identified a spontaneous mutation in a tomato mutant named suffulta (su), in which the stems appeared albinic while the leaves remained normal. Map-based cloning showed that Su encodes a DnaJ heat shock protein that is a homolog of the Arabidopsis gene AtARC6, which is involved in chloroplast division. Knockdown and knockout of SlARC6 in wild-type tomato inhibit chloroplast division, indicating the conserved function of SlARC6. In su mutants, most mesophyll cells contain only one or two giant chloroplasts, while no chloroplasts are visible in 60% of stem cells, resulting in the albinic phenotype. Compared with mature tissues, the meristem of su mutants suggested that chloroplasts could partially divide in meristematic cells, suggesting the existence of an alternative mechanism in those dividing cells. Interestingly, the adaxial petiole cells of su mutants contain more chloroplasts than the abaxial cells. In addition, prolonged lighting can partially rescue the albinic phenotypes in su mutants, implying that light may promote SlACR6-independent chloroplast development. Our results verify the role of SlACR6 in chloroplast division in tomato and uncover the tissue-specific regulation of chloroplast development.

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“…In chloroplasts, the Z-ring is formed by the association of FtsZ1 and FtsZ2 heteropolymers on the stromal side of the inner envelope at the division plane via the membrane tethering protein ARC6, a bitopic inner transmembrane protein that stabilizes the plastid FtsZ ring and coordinates the internal and external division machineries ( Vitha et al, 2003 ). There are currently two known stroma-division proteins reported to interact with ARC6: FtsZ2 ( Lohse et al, 2006 ) and MCD1 ( Chen L. et al, 2018 ).…”

Section: Introductionmentioning

confidence: 99%

Residue 49 of AtMinD1 Plays a Key Role in the Guidance of Chloroplast Division by Regulating the ARC6-AtMinD1 Interaction

Zhang

Cui

et al. 2021

Front. Plant Sci.

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Chloroplasts evolved from a free-living cyanobacterium through endosymbiosis. Similar to bacterial cell division, chloroplasts replicate by binary fission, which is controlled by the Minicell (Min) system through confining FtsZ ring formation at the mid-chloroplast division site. MinD, one of the most important members of the Min system, regulates the placement of the division site in plants and works cooperatively with MinE, ARC3, and MCD1. The loss of MinD function results in the asymmetric division of chloroplasts. In this study, we isolated one large dumbbell-shaped and asymmetric division chloroplast Arabidopsis mutant Chloroplast Division Mutant 75 (cdm75) that contains a missense mutation, changing the arginine at residue 49 to a histidine (R49H), and this mutant point is located in the N-terminal Conserved Terrestrial Sequence (NCTS) motif of AtMinD1, which is only typically found in terrestrial plants. This study provides sufficient evidence to prove that residues 1–49 of AtMinD1 are transferred into the chloroplast, and that the R49H mutation does not affect the function of the AtMinD1 chloroplast transit peptide. Subsequently, we showed that the point mutation of R49H could remove the punctate structure caused by residues 1–62 of the AtMinD1 sequence in the chloroplast, suggesting that the arginine in residue 49 (Arg49) is essential for localizing the punctate structure of AtMinD11–62 on the chloroplast envelope. Unexpectedly, we found that AtMinD1 could interact directly with ARC6, and that the R49H mutation could prevent not only the previously observed interaction between AtMinD1 and MCD1 but also the interaction between AtMinD1 and ARC6. Thus, we believe that these results show that the AtMinD1 NCTS motif is required for their protein interaction. Collectively, our results show that AtMinD1 can guide the placement of the division site to the mid chloroplast through its direct interaction with ARC6 and reveal the important role of AtMinD1 in regulating the AtMinD1-ARC6 interaction.

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MCD1 Associates with FtsZ Filaments via the Membrane-Tethering Protein ARC6 to Guide Chloroplast Division

Cited by 17 publications

References 58 publications

Arabidopsis PARC6 Is Critical for Plastid Morphogenesis in Pavement, Trichome, and Guard Cells in Leaf Epidermis

Arabidopsis PARC6 Is Critical for Plastid Morphogenesis in Pavement, Trichome, and Guard Cells in Leaf Epidermis

Mutation of SlARC6 leads to tissue-specific defects in chloroplast development in tomato

Residue 49 of AtMinD1 Plays a Key Role in the Guidance of Chloroplast Division by Regulating the ARC6-AtMinD1 Interaction

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