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Volumn 16, Issue 1, 2004, Pages 24-31

Structural/functional homology between the bacterial and eukaryotic cytoskeletons

Author keywords

5 adenylyl imidodiphosphate; AMPPNP; Electron microscopy; EM; GFP; Green fluorescent protein; GTP; Guanosine 5 triphosphate; MAPs; MD; Microtubule associated proteins; Mitochondrion dividing; PD; PH; Plastid dividing; Pleckstrin homology

Indexed keywords

BACTERIAL PROTEIN; DYNAMIN; FTSZ PROTEIN; MIND PROTEIN; SYNTAXIN;

EID: 1642344759     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2003.11.005     Document Type: Review
Times cited : (67)

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    • ••]. The MreB and MinCDE coiled arrays do not appear identical but this point needs to be confirmed by co-labeling the proteins in the same cells.
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    • Overexpression of the Arabidopsis thaliana MinE1 bacterial division inhibitor homologue gene alters chloroplast size and morphology in transgenic Arabidopsis and tobacco plants
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    • ARC5, a cytosolic dynamin-like protein from plants, is part of the chloroplast division machinery
    • •]) show that a requirement for a dynamin-related protein, with no obvious counterparts in prokaryotes, is common to both types of endosymbiotic organelle. ARC5 is related to a group of dynamin-like proteins that are unique to plants. A GFP-ARC5 fusion protein localizes to a ring at the chloroplast division site and ARC5 mutations cause enlarged, dumbbell-shaped chloroplasts. Import and protease protection assays indicate that the ARC5 ring is positioned on the outer surface of the chloroplast.
    • •]) show that a requirement for a dynamin-related protein, with no obvious counterparts in prokaryotes, is common to both types of endosymbiotic organelle. ARC5 is related to a group of dynamin-like proteins that are unique to plants. A GFP-ARC5 fusion protein localizes to a ring at the chloroplast division site and ARC5 mutations cause enlarged, dumbbell-shaped chloroplasts. Import and protease protection assays indicate that the ARC5 ring is positioned on the outer surface of the chloroplast.
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    • A plant-specific dynamin-related protein forms a ring at the chloroplast division site
    • Analysis of synchronized chloroplasts showed the time at which a dynamin-like protein is recruited to chloroplasts, forming a ring on the cytosolic side of the division site in the late stage of division. The ring constricts until division is complete and then disappears.
    • Miyagishima S.Y., Nishida K., Mori T., Matsuzaki M., Higashiyama T., Kuroiwa H., Kuroiwa T. A plant-specific dynamin-related protein forms a ring at the chloroplast division site. Plant Cell. 15:2003;655-665 Analysis of synchronized chloroplasts showed the time at which a dynamin-like protein is recruited to chloroplasts, forming a ring on the cytosolic side of the division site in the late stage of division. The ring constricts until division is complete and then disappears.
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    • Dynamic recruitment of dynamin for final mitochondrial severance in a primitive red alga
    • Previously, FtsZ was shown to localize to mitochondria in primitive algae on the inside surface of the division site. Here, it is shown that FtsZ, dynamin and the MD ring, an electron-dense structure on the cytoplasmic side of the mitochondrial membrane, act during different phases of division. Before final separation, dynamin patches are recruited externally, to the midpoint of the constricted MD ring.
    • Nishida K., Takahara M., Miyagishima S., Kuroiwa H., Matsuzaki M., Kuroiwa T. Dynamic recruitment of dynamin for final mitochondrial severance in a primitive red alga. Proc Natl Acad Sci USA. 100:2003;2146-2151 Previously, FtsZ was shown to localize to mitochondria in primitive algae on the inside surface of the division site. Here, it is shown that FtsZ, dynamin and the MD ring, an electron-dense structure on the cytoplasmic side of the mitochondrial membrane, act during different phases of division. Before final separation, dynamin patches are recruited externally, to the midpoint of the constricted MD ring.
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    • Chloroplast division machinery as revealed by immunofluorescence and electron microscopy
    • The behaviour of FtsZ and PD rings, both components of the chloroplast division machinery, was followed during the course of division. FtsZ forms a ring on the stromal division site before invagination starts. Then the inner (stromal) and outer (cytosolic) PD rings appear. The FtsZ ring remains at the leading edge of the constriction but does not change width although the volume of the outer PD ring gradually increases. The FtsZ ring disappears before the final stage of chloroplast constriction.
    • Kuroiwa H., Mori T., Takahara M., Miyagishima S., Kuroiwa T. Chloroplast division machinery as revealed by immunofluorescence and electron microscopy. Planta. 215:2002;185-190 The behaviour of FtsZ and PD rings, both components of the chloroplast division machinery, was followed during the course of division. FtsZ forms a ring on the stromal division site before invagination starts. Then the inner (stromal) and outer (cytosolic) PD rings appear. The FtsZ ring remains at the leading edge of the constriction but does not change width although the volume of the outer PD ring gradually increases. The FtsZ ring disappears before the final stage of chloroplast constriction.
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    • Dysfunctional MreB inhibits chromosome segregation in Escherichia coli
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.