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Chloroplast Division in Higher Plants Requires Members of Two Functionally Divergent Gene Families with Homology to Bacterial ftsZ
- K. Osteryoung, K. D. Stokes, S. Rutherford, A. L. Percival, Won Y. Lee
- Biology, Environmental SciencePlant Cell
- 1 December 1998
The identification of a second nuclear-encoded FtsZ-type protein from Arabidopsis that does not contain a chloroplast targeting sequence or other obvious sorting signals and is not imported into isolated chloroplasts, which strongly suggests that it is localized in the cytosol.
Ftsz Ring Formation at the Chloroplast Division Site in Plants
Using immunofluorescence microscopy and expression of green fluorescent protein fusion proteins in Arabidopsis thaliana, it is demonstrated that FtsZ1 andFtsZ2 localize to coaligned rings at the chloroplast midpoint, suggesting that midplastid ring formation by Fts Z1 and Ftsz2 is universal among flowering plants.
ARC6 Is a J-Domain Plastid Division Protein and an Evolutionary Descendant of the Cyanobacterial Cell Division Protein Ftn2 Online version contains Web-only data. Article, publication date, and…
- S. Vitha, J. Froehlich, O. Koksharova, K. Pyke, H. Van Erp, K. Osteryoung
- BiologyThe Plant Cell Online
- 1 August 2003
The mutation in arc6 is identified and it is shown that the ARC6 gene encodes a chloroplast-targeted DnaJ-like protein localized to the plastid envelope membrane, and an ARC6–green fluorescent protein fusion protein was localized to a ring at the center of the chloroplasts and rescued thechloroplast division defect in the arc6 mutant.
ARC5, a cytosolic dynamin-like protein from plants, is part of the chloroplast division machinery
- Hongbo Gao, Deena K. Kadirjan-Kalbach, J. Froehlich, K. Osteryoung
- BiologyProceedings of the National Academy of Sciences…
- 17 March 2003
The results indicate that the chloroplast division apparatus is of mixed evolutionary origin and that it shares structural and mechanistic similarities with both the cell division machinery of bacteria and the dynamin-mediated organellar fission machineries of eukaryotes.
PDV1 and PDV2 Mediate Recruitment of the Dynamin-Related Protein ARC5 to the Plastid Division Site
- S. Miyagishima, J. Froehlich, K. Osteryoung
- Environmental ScienceThe Plant Cell Online
- 22 September 2006
The results indicate that plastid division involves the stepwise localization of FtsZ, PDV1, and ARC5 at the division site and that PDV 1 and PDV2 together mediate the recruitment of ARC5 to the midplastid constriction at a late stage of division.
A homologue of the bacterial cell division site-determining factor MinD mediates placement of the chloroplast division apparatus
The Division of Endosymbiotic Organelles
This work has shown that mitochondria and chloroplasts universally require dynamin-related guanosine triphosphatases to divide, and provides fundamental insights into the molecular events driving the division, and possibly the evolution, of organelles in eukaryotes.
Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis.
This proteomic study enabled us to identify 392 nonredundant proteins and applied two alternative methodologies, off-line multidimensional protein identification technology and one-dimensional gel electrophoresis followed by proteolytic digestion and liquid chromatography coupled with tandem mass spectrometry (Gel-C-MS/MS), to identify envelope membrane proteins.
Exceptional sensitivity of Rubisco activase to thermal denaturation in vitro and in vivo.
Loss of activase activity during heat stress is caused by an exceptional sensitivity of the protein to thermal denaturation and is responsible, in part, for deactivation of Rubisco.
Colocalization of plastid division proteins in the chloroplast stromal compartment establishes a new functional relationship between FtsZ1 and FtsZ2 in higher plants.
- R. McAndrew, J. Froehlich, S. Vitha, K. D. Stokes, K. Osteryoung
- BiologyPlant physiology
- 1 December 2001
New questions concerning the functional and evolutionary significance of two distinct but colocalized forms of FtsZ in plants are raised and a revised framework within which to understand the molecular architecture of the plastid division apparatus in higher plants is established.