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Plant and Cell Physiology Advance Access originally published online on July 18, 2006
Plant and Cell Physiology 2006 47(8):1175-1181; doi:10.1093/pcp/pcj086
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© The Author 2006. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

Short Communication

Purification and Characterization of Plant Dynamin from Tobacco BY-2 Cells

Takahiro Hamada1, Hisako Igarashi2, Maki Yao3, Takashi Hashimoto3, Teruo Shimmen1 and Seiji Sonobe1,*

1 Department of Life Science, Graduate School of Life Science, University of Hyogo, Harima Science Park City, Hyogo, 678-1297 Japan
2 Plant Science Center, RIKEN, 1-7-22 Suehiro, Turumi, Yokohama, Kanagawa, 230-0043 Japan
3 Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, 630-0192 Japan

* Corresponding author: E-mail, sonobe{at}sci.u-hyogo.ac.jp; Fax, +81-791-58-0175.

We purified an 84 kDa polypeptide from the MAP (microtubule-associated protein) fraction of tobacco BY-2 cultured cells. LC/MS/MS (liquid chromatography–tandem mass spectrometry) analysis revealed that this polypeptide is a tobacco homolog of AtDRP3 (Arabidopsis thaliana dynamin-related protein 3). Electron microscopy revealed that NtDRP3 (Nicotiana tabacum dynamin-related protein 3) assembles to form a filamentous structure. When GDP was added to the NtDRP3 fraction, the filaments disappeared and many particles appeared. Biochemical analysis revealed that NtDRP3 could bind to and bundle both microtubules and actin filaments in vitro.

(Received April 7, 2006; Accepted July 1, 2006)
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