Plant-Specific Protein MCD1 Determines the Site of Chloroplast Division in Concert with Bacteria-Derived MinD

Nakanishi, Hiromitsu; Suzuki, Kenji; Kabeya, Yukihiro; Miyagishima, Shin-ya

doi:10.1016/j.cub.2008.12.018

Cited by 73 publications

(89 citation statements)

References 42 publications

(94 reference statements)

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“…FtsZ, homolog of the tubulin-like bacterial division GTPase, self-assembles into a ring structure at the stromal side of the division site (Vitha et al, 2001;Kuroiwa et al, 2002). The positioning of the FtsZ ring mid-chloroplast is regulated by MinD, MinE, ARC3, and MCD1 (Colletti et al, 2000;Itoh et al, 2001;Shimada et al, 2004;Nakanishi et al, 2009). FtsZ filaments are stabilized by cyanobacteria-descended inner envelope spanning protein ARC6 (Vitha et al, 2003) through interaction with FtsZ .…”

Section: Resultsmentioning

confidence: 99%

The PLASTID DIVISION1 and 2 Components of the Chloroplast Division Machinery Determine the Rate of Chloroplast Division in Land Plant Cell Differentiation

et al. 2009

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In most algae, the chloroplast division rate is held constant to maintain the proper number of chloroplasts per cell. By contrast, land plants evolved cell and chloroplast differentiation systems in which the size and number of chloroplasts change along with their respective cellular function by regulation of the division rate. Here, we show that PLASTID DIVISION (PDV) proteins, land plant-specific components of the division apparatus, determine the rate of chloroplast division. Overexpression of PDV proteins in the angiosperm Arabidopsis thaliana and the moss Physcomitrella patens increased the number but decreased the size of chloroplasts; reduction of PDV levels resulted in the opposite effect. The level of PDV proteins, but not other division components, decreased during leaf development, during which the chloroplast division rate also decreased. Exogenous cytokinins or overexpression of the cytokinin-responsive transcription factor CYTOKININ RESPONSE FACTOR2 increased the chloroplast division rate, where PDV proteins, but not other components of the division apparatus, were upregulated. These results suggest that the integration of PDV proteins into the division machinery enabled land plant cells to change chloroplast size and number in accord with the fate of cell differentiation.

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Section: Resultsmentioning

confidence: 99%

The PLASTID DIVISION1 and 2 Components of the Chloroplast Division Machinery Determine the Rate of Chloroplast Division in Land Plant Cell Differentiation

et al. 2009

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“…But in many aspects, characters of AtMinD and AtMinE are diverged from their homologs in prokaryotes [26,46,47]. Recently, it was shown that a plant-specific protein, MCD1, is required for FtsZ ring positioning [48]. MCD1 recruits MinD to the chloroplast inner envelope by direct interaction.…”

Section: Discussionmentioning

confidence: 99%

CDP1, a novel component of chloroplast division site positioning system in Arabidopsis

Zhang

Jia

et al. 2009

Cell Res

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Chloroplasts are plant-specific organelles that evolved from endosymbiotic cyanobacteria. They divide through binary fission. Selection of the chloroplast division site is pivotal for the symmetric chloroplast division. In E. coli, positioning of the division site at the midpoint of the cell is regulated by dynamic oscillation of the Min system, which includes MinC, MinD and MinE. Homologs of MinD and MinE in plants are involved in chloroplast division. The homolog of MinC still has not been identified in higher plants. However, an FtsZ-like protein, ARC3, was found to be involved in chloroplast division site positioning. Here, we report that chloroplast division site positioning 1 (AtCDP1) is a novel chloroplast division protein involved in chloroplast division site placement in Arabidopsis. AtCDP1 was discovered by screening an Arabidopsis cDNA expression library in bacteria for colonies with a cell division phenotype. AtCDP1 is exclusively expressed in young green tissues in Arabidopsis. Elongated chloroplasts with multiple division sites were observed in the loss-of-function cdp1 mutant. Overexpression of AtCDP1 caused a chloroplast division phenotype too. Protein interaction assays suggested that AtCDP1 may mediate the chloroplast division site positioning through the interaction with ARC3. Overall, our results indicate that AtCDP1 is a novel component of the chloroplast division site positioning system, and the working mechanism of this system is different from that of the traditional MinCDE system in prokaryotic cells.

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“…Consistent with the origin of chloroplasts, several chloroplast division proteins are homologs of bacterial cell division proteins (Osteryoung and Vierling, 1995;Colletti et al, 2000;Itoh et al, 2001;Maple et al, 2002;Vitha et al, 2003), and models of bacterial cell division have guided studies and understanding of chloroplast division mechanisms in plants (Okazaki et al, 2010;Miyagishima, 2011). During evolution, plants have also acquired new chloroplast division components of eukaryotic origin (Gao et al, 2003;Miyagishima et al, 2006;Nakanishi et al, 2009).…”

Section: Introductionmentioning

confidence: 90%

Chloroplast Division Protein ARC3 Regulates Chloroplast FtsZ-Ring Assembly and Positioning in Arabidopsis through Interaction with FtsZ2

et al. 2013

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Chloroplast division is initiated by assembly of a mid-chloroplast FtsZ (Z) ring comprising two cytoskeletal proteins, FtsZ1 and FtsZ2. The division-site regulators ACCUMULATION AND REPLICATION OF CHLOROPLASTS3 (ARC3), MinD1, and MinE1 restrict division to the mid-plastid, but their roles are poorly understood. Using genetic analyses in Arabidopsis thaliana, we show that ARC3 mediates division-site placement by inhibiting Z-ring assembly, and MinD1 and MinE1 function through ARC3. ftsZ1 null mutants exhibited some mid-plastid FtsZ2 rings and constrictions, whereas neither constrictions nor FtsZ1 rings were observed in mutants lacking FtsZ2, suggesting FtsZ2 is the primary determinant of Z-ring assembly in vivo. arc3 ftsZ1 double mutants exhibited multiple parallel but no mid-plastid FtsZ2 rings, resembling the Z-ring phenotype in arc3 single mutants and showing that ARC3 affects positioning of FtsZ2 rings as well as Z rings. ARC3 overexpression in the wild type and ftsZ1 inhibited Z-ring and FtsZ2-ring assembly, respectively. Consistent with its effects in vivo, ARC3 interacted with FtsZ2 in two-hybrid assays and inhibited FtsZ2 assembly in a heterologous system. Our studies are consistent with a model wherein ARC3 directly inhibits Z-ring assembly in vivo primarily through interaction with FtsZ2 in heteropolymers and suggest that ARC3 activity is spatially regulated by MinD1 and MinE1 to permit Z-ring assembly at the mid-plastid.

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Plant-Specific Protein MCD1 Determines the Site of Chloroplast Division in Concert with Bacteria-Derived MinD

Cited by 73 publications

References 42 publications

The PLASTID DIVISION1 and 2 Components of the Chloroplast Division Machinery Determine the Rate of Chloroplast Division in Land Plant Cell Differentiation

The PLASTID DIVISION1 and 2 Components of the Chloroplast Division Machinery Determine the Rate of Chloroplast Division in Land Plant Cell Differentiation

CDP1, a novel component of chloroplast division site positioning system in Arabidopsis

Chloroplast Division Protein ARC3 Regulates Chloroplast FtsZ-Ring Assembly and Positioning in Arabidopsis through Interaction with FtsZ2

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