Structure, Regulation, and Evolution of the Plastid Division Machinery

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

doi:10.1016/b978-0-12-386035-4.00004-5

Cited by 44 publications

(64 citation statements)

References 138 publications

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“…This interaction may facilitate Z-ring remodeling and disassembly during constriction (Johnson et al, 2015). Other details omitted for simplicity are reviewed by Miyagishima et al (2011) and Osteryoung and Pyke (2014). C, C terminus; N, N terminus; Z1, FtsZ1; Z2, FtsZ2.…”

Section: Discussionmentioning

confidence: 99%

“…1). Z-ring assembly is restricted to the midplastid by the chloroplast Min system, which includes ARC3 (Glynn et al, 2007;Maple et al, 2007;Zhang et al, 2013) as well as MinD1, MinE1, and MULTIPLE CHLOROPLAST DIVISION SITE1 (not shown; Miyagishima et al, 2011;Osteryoung and Pyke, 2014). The Z ring, composed of FtsZ1/FtsZ2 heteropolymers that may assemble with mixed stoichiometries (Olson et al, 2010), is tethered to the IEM by ARC6 through direct interaction with FtsZ2 in the stroma (Maple et al, 2005;Schmitz et al, 2009).…”

Section: Discussionmentioning

confidence: 99%

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Roles of Arabidopsis PARC6 in Coordination of the Chloroplast Division Complex and Negative Regulation of FtsZ Assembly

et al. 2015

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Chloroplast division is driven by the simultaneous constriction of the inner FtsZ ring (Z ring) and the outer DRP5B ring. The assembly and constriction of these rings in Arabidopsis (Arabidopsis thaliana) are coordinated partly through the inner envelope membrane protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS6 (ARC6). Previously, we showed that PARC6 (PARALOG OF ARC6), also in the inner envelope membrane, negatively regulates FtsZ assembly and acts downstream of ARC6 to position the outer envelope membrane protein PLASTID DIVISION1 (PDV1), which functions together with its paralog PDV2 to recruit DYNAMIN-RELATED PROTEIN 5B (DRP5B) from a cytosolic pool to the outer envelope membrane. However, whether PARC6, like ARC6, also functions in coordination of the chloroplast division contractile complexes was unknown. Here, we report a detailed topological analysis of Arabidopsis PARC6, which shows that PARC6 has a single transmembrane domain and a topology resembling that of ARC6. The newly identified stromal region of PARC6 interacts not only with ARC3, a direct inhibitor of Z-ring assembly, but also with the Z-ring protein FtsZ2. Overexpression of PARC6 inhibits FtsZ assembly in Arabidopsis but not in a heterologous yeast system (Schizosaccharomyces pombe), suggesting that the negative regulation of FtsZ assembly by PARC6 is a consequence of its interaction with ARC3. A conserved carboxyl-terminal peptide in FtsZ2 mediates FtsZ2 interaction with both PARC6 and ARC6. Consistent with its role in the positioning of PDV1, the intermembrane space regions of PARC6 and PDV1 interact. These findings provide new insights into the functions of PARC6 and suggest that PARC6 coordinates the inner Z ring and outer DRP5B ring through interaction with FtsZ2 and PDV1 during chloroplast division.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Roles of Arabidopsis PARC6 in Coordination of the Chloroplast Division Complex and Negative Regulation of FtsZ Assembly

et al. 2015

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“…The successful division of plastids requires a complex string of temporal and spatial events (Maple and Møller 2010;Miyagishima et al 2011;Miyagishima 2011). First, proteins involved in the division process have to be translated on cytosolic ribosomes.…”

Section: Introductionmentioning

confidence: 99%

“…Indeed, little is known how plastid division is inXuenced by endogenous cues during cellular diVerentiation, to what extent plastid biogenesis and division are interlinked and moreover how aspects of the division process is speciWcally controlled and regulated. During the past decade a number of plastid division components have been isolated, characterised and assembled into protein complexes (Table 1; Miyagishima et al 2011;Miyagishima 2011); however, reports describing new bone Wde division components are becoming less frequent. Perhaps most of the primary division players have now been identiWed and that it is timely to expand the horizon by overlaying our current plastid division knowledge onto other aspects of plant diVerentiation and development.…”

Section: Introductionmentioning

confidence: 99%

Emerging facets of plastid division regulation

Basak

Møller

2012

Planta

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Plastids are complex organelles that are integrated into the plant host cell where they diVerentiate and divide in tune with plant diVerentiation and development. In line with their prokaryotic origin, plastid division involves both evolutionary conserved proteins and proteins of eukaryotic origin where the host has acquired control over the process. The plastid division apparatus is spatially separated between the stromal and the cytosolic space but where clear coordination mechanisms exist between the two machineries. Our knowledge of the plastid division process has increased dramatically during the past decade and recent Wndings have not only shed light on plastid division enzymology and the formation of plastid division complexes but also on the integration of the division process into a multicellular context. This review summarises our current knowledge of plastid division with an emphasis on biochemical features, the functional assembly of protein complexes and regulatory features of the overall process.

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“…This process is powered by a macromolecular machine with ring-shaped contractile complexes on both the inner and outer envelope membranes (for review, see Miyagishima et al, 2011;Falconet, 2012;Yoshida et al, 2012;Osteryoung and Pyke, 2014). The division machinery is a mosaic of components of both endosymbiotic and host origin that must cooperate to divide the organelle (Fig.…”

mentioning

confidence: 99%