Skip Navigation


Plant and Cell Physiology Advance Access originally published online on April 28, 2009
Plant and Cell Physiology 2009 50(6):1116-1126; doi:10.1093/pcp/pcp063
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplementary Data
Right arrow All Versions of this Article:
50/6/1116    most recent
pcp063v1
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 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 arrowRequest Permissions
Google Scholar
Right arrow Articles by Fujiwara, M. T.
Right arrow Articles by Itoh, R. D.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fujiwara, M. T.
Right arrow Articles by Itoh, R. D.
Agricola
Right arrow Articles by Fujiwara, M. T.
Right arrow Articles by Itoh, R. D.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2009. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

Live Imaging of Chloroplast FtsZ1 Filaments, Rings, Spirals, and Motile Dot Structures in the AtMinE1 Mutant and Overexpressor of Arabidopsis thaliana

Makoto T. Fujiwara1,2, Kohsuke Sekine2, Yoshiharu Y. Yamamoto1,4, Tomoko Abe1, Naoki Sato2 and Ryuuichi D. Itoh3,*

1RIKEN, Hirosawa 2-1, Wako, Saitama, 351-0198 Japan
2Department of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo, Komaba 3-8-1, Meguro, Tokyo, 153-8902 Japan
3Department of Chemistry, Biology and Marine Science, Faculty of Science, University of the Ryukyus, Senbaru 1, Nishihara, Okinawa, 903-0213 Japan

*Corresponding authors: Ryuuichi D. Itoh, E-mail, ryuitoh{at}sci.u-ryukyu.ac.jp; Fax, +81-98-895-8576; Makoto T. Fujiwara, E-mail, mtf1{at}mac.com; Fax, +81-3-5454-6998.


  Abstract

Chloroplast division involves the tubulin-related GTPase FtsZ that assembles into a ring structure (Z-ring) at the mid-chloroplast division site, which is where invagination and constriction of the envelope membranes occur. Z-ring assembly is usually confined to the mid-chloroplast site by a well balanced counteraction of the stromal proteins MinD and MinE. The in vivo mechanisms by which FtsZ nucleates at specific sites, polymerises into a protofil-ament and organises a closed ring of filament bundles remain largely unknown. To clarify the dynamic aspects of FtsZ, we developed a living cell system for simultaneous visualisation of various FtsZ configurations, utilising the Arabidopsis thaliana overexpressor and mutant of the MinE (AtMinE1) gene, which were modified to weakly express green fluorescent protein (GFP) fused to AtFtsZ1-1. Time-lapse observation in the chloroplasts of both plants revealed disorderly movement of the dots and short filaments of FtsZ. The short filaments often appeared to emanate from the dots and to converge with a long filament, producing a thick cable. In the AtMinE1 overexpressor, we also observed spirals along the longitudinal axis of the organelle that often rolled the closed rings together. In the atminE1 mutant, we visualised the ‘isolated’ rings with a maximum diameter of ~2 µm that did not encircle the organelle periphery, but appeared to be suspended in the stroma. Our observations further demonstrated heterogeneity in chloroplast shapes and concurrently altered configurations of FtsZ in the mutant.

Keywords: Chloroplast division - FtsZ filament - FtsZ ring - GFP - Min system - Plastid division

Abbreviations: CaMV35S, cauliflower mosaic virus 35 S; GFP, green fluorescent protein; WT, wild type; YFP, yellow fluorescent protein.

4 Present address: Faculty of Applied Biological Sciences, Gifu University, Yanagido 1-1, Gifu, 501-1193 Japan.

(Received March 7, 2009; Accepted April 24, 2009)
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




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.