Skip Navigation

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (30)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Mori, T.
Right arrow Articles by Kuroiwa, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mori, T.
Right arrow Articles by Kuroiwa, T.
Agricola
Right arrow Articles by Mori, T.
Right arrow Articles by Kuroiwa, T.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Plant and Cell Physiology, 2001, Vol. 42, No. 6 555-559
© 2001 Oxford University Press

Visualization of an FtsZ Ring in Chloroplasts of Lilium longiflorum Leaves

Toshiyuki Mori1, Haruko Kuroiwa, Manabu Takahara, Shin-ya Miyagishima and Tsuneyoshi Kuroiwa Department of Biological Sciences, Graduate School of Science, University of Tokyo, Hongo, Tokyo, 113-0033 Japan

FtsZ is a bacterial division protein which forms a ring at the leading edge of the cell division site. To date, a hypothesis that the plant FtsZ forms the same structure in chloroplast division is proposed, but has not been demonstrated yet. In this study, recombinant LlFtsZ (Lilium longiflorum FtsZ) protein was produced from a previously isolated ftsZ cDNA clone [Mori and Tanaka (2000) Protoplasma 214: 57] and used to raise polyclonal anti-LlFtsZ antibodies in rabbits. In immunoblot analysis with the total protein extracted from L. longiflorum leaves, purified antibodies specifically recognized LlFtsZ whose molecular mass was approximately 43 kDa. This size corresponded to that of the recombinant LlFtsZ protein lacking N-terminal sequence, which suggests that the full-length LlFtsZ translation product has a putative N-terminal signal peptide. Moreover, fluorescent and electron microscopy revealed that the anti-LlFtsZ antibodies recognized ring structures at stromal side of the constriction point of dividing chloroplasts. Here, we show direct evidence that FtsZ ring is involved in chloroplast division.

1 Corresponding author: E-mail, tossy@biol.s.u-tokyo.ac.jp; Fax, +81-3-3814-1408; Phone, +81-3-5841-4471.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Plant Cell PhysiolHome page
Y. Hu, Q. Zhang, G. Rao, and Sodmergen
Occurrence of Plastids in the Sperm Cells of Caprifoliaceae: Biparental Plastid Inheritance in Angiosperms is Unilaterally Derived from Maternal Inheritance
Plant Cell Physiol., June 1, 2008; 49(6): 958 - 968.
[Abstract] [Full Text] [PDF]

Home page
 Plant Cell PhysiolHome page
M. T. Fujiwara, H. Hashimoto, Y. Kazama, T. Abe, S. Yoshida, N. Sato, and R. D. Itoh
The Assembly of the FtsZ Ring at the Mid-Chloroplast Division Site Depends on a Balance Between the Activities of AtMinE1 and ARC11/AtMinD1
Plant Cell Physiol., March 1, 2008; 49(3): 345 - 361.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
S.-y. Miyagishima, J. E. Froehlich, and K. W. Osteryoung
PDV1 and PDV2 Mediate Recruitment of the Dynamin-Related Protein ARC5 to the Plastid Division Site
PLANT CELL, October 1, 2006; 18(10): 2517 - 2530.
[Abstract] [Full Text] [PDF]

Home page
 Plant Cell PhysiolHome page
S. Lohse, B. Hause, G. Hause, and T. Fester
FtsZ Characterization and Immunolocalization in the Two Phases of Plastid Reorganization in Arbuscular Mycorrhizal Roots of Medicago truncatula
Plant Cell Physiol., August 1, 2006; 47(8): 1124 - 1134.
[Abstract] [Full Text] [PDF]

Home page
 Plant Cell PhysiolHome page
H. Shimada, M. Koizumi, K. Kuroki, M. Mochizuki, H. Fujimoto, H. Ohta, T. Masuda, and K.-i. Takamiya
ARC3, a Chloroplast Division Factor, is a Chimera of Prokaryotic FtsZ and Part of Eukaryotic Phosphatidylinositol-4-phosphate 5-kinase
Plant Cell Physiol., August 15, 2004; 45(8): 960 - 967.
[Abstract] [Full Text] [PDF]

Home page
 J. Histochem. Cytochem.Home page
K. Nishida, O. Misumi, F. Yagisawa, H. Kuroiwa, T. Nagata, and T. Kuroiwa
Triple Immunofluorescent Labeling of FtsZ, Dynamin, and EF-Tu Reveals a Loose Association Between the Inner and Outer Membrane Mitochondrial Division Machinery in the Red Alga Cyanidioschyzon merolae
J. Histochem. Cytochem., July 1, 2004; 52(7): 843 - 849.
[Abstract] [Full Text] [PDF]

Home page
 Eukaryot CellHome page
P. R. Gilson, X.-C. Yu, D. Hereld, C. Barth, A. Savage, B. R. Kiefel, S. Lay, P. R. Fisher, W. Margolin, and P. L. Beech
Two Dictyostelium Orthologs of the Prokaryotic Cell Division Protein FtsZ Localize to Mitochondria and Are Required for the Maintenance of Normal Mitochondrial Morphology
Eukaryot. Cell, December 1, 2003; 2(6): 1315 - 1326.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
S. Vitha, J. E. Froehlich, O. Koksharova, K. A. Pyke, H. van Erp, and K. W. Osteryoung
ARC6 Is a J-Domain Plastid Division Protein and an Evolutionary Descendant of the Cyanobacterial Cell Division Protein Ftn2
PLANT CELL, August 1, 2003; 15(8): 1918 - 1933.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
H. Gao, D. Kadirjan-Kalbach, J. E. Froehlich, and K. W. Osteryoung
From the Cover: ARC5, a cytosolic dynamin-like protein from plants, is part of the chloroplast division machinery
PNAS, April 1, 2003; 100(7): 4328 - 4333.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
S.-y. Miyagishima, K. Nishida, T. Mori, M. Matsuzaki, T. Higashiyama, H. Kuroiwa, and T. Kuroiwa
A Plant-Specific Dynamin-Related Protein Forms a Ring at the Chloroplast Division Site
PLANT CELL, March 1, 2003; 15(3): 655 - 665.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
S.-y. Miyagishima, M. Takahara, T. Mori, H. Kuroiwa, T. Higashiyama, and T. Kuroiwa
Plastid Division Is Driven by a Complex Mechanism That Involves Differential Transition of the Bacterial and Eukaryotic Division Rings
PLANT CELL, October 1, 2001; 13(10): 2257 - 2268.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.