Faculty Opinions recommendation of A plant-specific dynamin-related protein forms a ring at the chloroplast division site.

2003 ◽  
Author(s):  
John Browse
Keyword(s):  
Chloroplast Division ◽  
Related Protein ◽  
Division Site

scholarly journals A Plant-Specific Dynamin-Related Protein Forms a Ring at the Chloroplast Division Site

2003 ◽  
Vol 15 (3) ◽  
pp. 655-665 ◽  
Author(s):  
Shin-ya Miyagishima ◽  
Keiji Nishida ◽  
Toshiyuki Mori ◽  
Motomichi Matsuzaki ◽  
Tetsuya Higashiyama ◽  
...  
Keyword(s):  
Chloroplast Division ◽  
Related Protein ◽  
Division Site

scholarly journals Chloroplast division checkpoint in eukaryotic algae

2016 ◽  
Vol 113 (47) ◽  
pp. E7629-E7638 ◽  
Author(s):  
Nobuko Sumiya ◽  
Takayuki Fujiwara ◽  
Atsuko Era ◽  
Shin-ya Miyagishima
Keyword(s):  
Cell Cycle ◽  
Host Cell ◽  
Cell Cycle Progression ◽  
Chloroplast Division ◽  
Dominant Negative ◽  
Cyanidioschyzon Merolae ◽  
Temperature Sensitive ◽  
Specific Expression ◽  
Cycle Progression ◽  
Division Site

Chloroplasts evolved from a cyanobacterial endosymbiont. It is believed that the synchronization of endosymbiotic and host cell division, as is commonly seen in existing algae, was a critical step in establishing the permanent organelle. Algal cells typically contain one or only a small number of chloroplasts that divide once per host cell cycle. This division is based partly on the S-phase–specific expression of nucleus-encoded proteins that constitute the chloroplast-division machinery. In this study, using the red alga Cyanidioschyzon merolae, we show that cell-cycle progression is arrested at the prophase when chloroplast division is blocked before the formation of the chloroplast-division machinery by the overexpression of Filamenting temperature-sensitive (Fts) Z2-1 (Fts72-1), but the cell cycle progresses when chloroplast division is blocked during division-site constriction by the overexpression of either FtsZ2-1 or a dominant-negative form of dynamin-related protein 5B (DRP5B). In the cells arrested in the prophase, the increase in the cyclin B level and the migration of cyclin-dependent kinase B (CDKB) were blocked. These results suggest that chloroplast division restricts host cell-cycle progression so that the cell cycle progresses to the metaphase only when chloroplast division has commenced. Thus, chloroplast division and host cell-cycle progression are synchronized by an interactive restriction that takes place between the nucleus and the chloroplast. In addition, we observed a similar pattern of cell-cycle arrest upon the blockage of chloroplast division in the glaucophyte alga Cyanophora paradoxa, raising the possibility that the chloroplast division checkpoint contributed to the establishment of the permanent organelle.

scholarly journals Cell Cycle-regulated, Microtubule-independent Organelle Division in Cyanidioschyzon merolae

2005 ◽  
Vol 16 (5) ◽  
pp. 2493-2502 ◽  
Author(s):  
Keiji Nishida ◽  
Fumi Yagisawa ◽  
Haruko Kuroiwa ◽  
Toshiyuki Nagata ◽  
Tsuneyoshi Kuroiwa
Keyword(s):  
Cell Cycle ◽  
Spindle Pole ◽  
Chloroplast Division ◽  
Mitochondrial Morphology ◽  
Cyanidioschyzon Merolae ◽  
Microtubule Organization ◽  
Mitochondrial Division ◽  
Protein Levels ◽  
Division Site ◽  
Organelle Division

Mitochondrial and chloroplast division controls the number and morphology of organelles, but how cells regulate organelle division remains to be clarified. Here, we show that each step of mitochondrial and chloroplast division is closely associated with the cell cycle in Cyanidioschyzon merolae. Electron microscopy revealed direct associations between the spindle pole bodies and mitochondria, suggesting that mitochondrial distribution is physically coupled with mitosis. Interconnected organelles were fractionated under microtubule-stabilizing condition. Immunoblotting analysis revealed that the protein levels required for organelle division increased before microtubule changes upon cell division, indicating that regulation of protein expression for organelle division is distinct from that of cytokinesis. At the mitochondrial division site, dynamin stuck to one of the divided mitochondria and was spatially associated with the tip of a microtubule stretching from the other one. Inhibition of microtubule organization, proteasome activity or DNA synthesis, respectively, induced arrested cells with divided but shrunk mitochondria, with divided and segregated mitochondria, or with incomplete mitochondrial division restrained at the final severance, and repetitive chloroplast division. The results indicated that mitochondrial morphology and segregation but not division depend on microtubules and implied that the division processes of the two organelles are regulated at distinct checkpoints.

scholarly journals Fission Yeast mto2p Regulates Microtubule Nucleation by the Centrosomin-related Protein mto1p

2005 ◽  
Vol 16 (6) ◽  
pp. 3040-3051 ◽  
Author(s):  
Itaru Samejima ◽  
Paula C. C. Lourenço ◽  
Hilary A. Snaith ◽  
Kenneth E. Sawin
Keyword(s):  
Fission Yeast ◽  
Insertional Mutagenesis ◽  
Spindle Pole ◽  
Related Protein ◽  
Microtubule Nucleation ◽  
Microtubule Organization ◽  
Cytoplasmic Microtubule ◽  
Division Site ◽  
Cell Extracts

From an insertional mutagenesis screen, we isolated a novel gene, mto2+, involved in microtubule organization in fission yeast. mto2Δ strains are viable but exhibit defects in interphase microtubule nucleation and in formation of the postanaphase microtubule array at the end of mitosis. The mto2Δ defects represent a subset of the defects displayed by cells deleted for mto1+ (also known as mod20+ and mbo1+), a centrosomin-related protein required to recruit the γ-tubulin complex to cytoplasmic microtubule-organizing centers (MTOCs). We show that mto2p colocalizes with mto1p at MTOCs throughout the cell cycle and that mto1p and mto2p coimmunoprecipitate from cytoplasmic extracts. In vitro studies suggest that mto2p binds directly to mto1p. In mto2Δ mutants, although some aspects of mto1p localization are perturbed, mto1p can still localize to spindle pole bodies and the cell division site and to “satellite” particles on interphase microtubules. In mto1Δ mutants, localization of mto2p to all of these MTOCs is strongly reduced or absent. We also find that in mto2Δ mutants, cytoplasmic forms of the γ-tubulin complex are mislocalized, and the γ-tubulin complex no longer coimmunoprecipitates with mto1p from cell extracts. These experiments establish mto2p as a major regulator of mto1p-mediated microtubule nucleation by the γ-tubulin complex.

scholarly journals The Assembly of the FtsZ Ring at the Mid-Chloroplast Division Site Depends on a Balance Between the Activities of AtMinE1 and ARC11/AtMinD1

2008 ◽  
Vol 49 (3) ◽  
pp. 345-361 ◽  
Author(s):  
Makoto T. Fujiwara ◽  
Haruki Hashimoto ◽  
Yusuke Kazama ◽  
Tomoko Abe ◽  
Shigeo Yoshida ◽  
...  
Keyword(s):  
Chloroplast Division ◽  
Ftsz Ring ◽  
Division Site

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

Cell Research ◽  
2009 ◽  
Vol 19 (7) ◽  
pp. 877-886 ◽  
Author(s):  
Min Zhang ◽  
Yong Hu ◽  
Jingjing Jia ◽  
Dapeng Li ◽  
Runjie Zhang ◽  
...  
Keyword(s):  
Chloroplast Division ◽  
Positioning System ◽  
Division Site

scholarly journals ARC3 Activation by PARC6 Promotes FtsZ-Ring Remodeling at the Chloroplast Division Site

2019 ◽  
Vol 31 (4) ◽  
pp. 862-885
Author(s):  
Cheng Chen ◽  
Lingyan Cao ◽  
Yue Yang ◽  
Katie J. Porter ◽  
Katherine W. Osteryoung
Keyword(s):  
Chloroplast Division ◽  
Ftsz Ring ◽  
Division Site

scholarly journals Ftsz Ring Formation at the Chloroplast Division Site in Plants

2001 ◽  
Vol 153 (1) ◽  
pp. 111-120 ◽  
Author(s):  
Stanislav Vitha ◽  
Rosemary S. McAndrew ◽  
Katherine W. Osteryoung
Keyword(s):  
Cell Division ◽  
Fluorescent Protein ◽  
Higher Plants ◽  
Chloroplast Division ◽  
Ring Formation ◽  
Protein Fusion ◽  
Cell Recruitment ◽  
Division Site ◽  
Filament Networks ◽  
Green Fluorescent

Among the events that accompanied the evolution of chloroplasts from their endosymbiotic ancestors was the host cell recruitment of the prokaryotic cell division protein FtsZ to function in chloroplast division. FtsZ, a structural homologue of tubulin, mediates cell division in bacteria by assembling into a ring at the midcell division site. In higher plants, two nuclear-encoded forms of FtsZ, FtsZ1 and FtsZ2, play essential and functionally distinct roles in chloroplast division, but whether this involves ring formation at the division site has not been determined previously. Using immunofluorescence microscopy and expression of green fluorescent protein fusion proteins in Arabidopsis thaliana, we demonstrate here that FtsZ1 and FtsZ2 localize to coaligned rings at the chloroplast midpoint. Antibodies specific for recognition of FtsZ1 or FtsZ2 proteins in Arabidopsis also recognize related polypeptides and detect midplastid rings in pea and tobacco, suggesting that midplastid ring formation by FtsZ1 and FtsZ2 is universal among flowering plants. Perturbation in the level of either protein in transgenic plants is accompanied by plastid division defects and assembly of FtsZ1 and FtsZ2 into filaments and filament networks not observed in wild-type, suggesting that previously described FtsZ-containing cytoskeletal-like networks in chloroplasts may be artifacts of FtsZ overexpression.

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