Purification and characterization of plant dynamin from tobacco BY-2 cells.
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.
Hamada
Takahiro
T
Department of Life Science, Graduate School of Life Science, University of Hyogo, Harima Science Park City, Hyogo, 678-1297 Japan.
Igarashi
Hisako
H
Yao
Maki
M
Hashimoto
Takashi
T
Shimmen
Teruo
T
Sonobe
Seiji
S
D029681:Arabidopsis Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D002478:Cells, Cultured; D034281:Dynamins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008869:Microtubule-Associated Proteins / Q000737:chemistry / Q000302:isolation & purification; D014026:Nicotiana / Q000166:cytology*
D029681:Arabidopsis Proteins; D008869:Microtubule-Associated Proteins; C486924:dynamin-related protein DRP3A, Arabidopsis; D034281:Dynamins