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Plant Physiol, November 2001, Vol. 127, pp. 1243-1255
Arabidopsis Dynamin-Like 2 That Binds Specifically to
Phosphatidylinositol 4-Phosphate Assembles into a High-Molecular
Weight Complex in Vivo and in Vitro1
Yong-Woo
Kim,
Dae-Sup
Park,
Seung-Cheol
Park,
Sung Hee
Kim,
Gang-Won
Cheong, and
Inhwan
Hwang*
Department of Life Science and Center for Plant Intracellular
Trafficking, Pohang University of Science and Technology, Pohang,
790-784, Korea (Y.-W.K., D.-S.P., I.H.); and Departments of
Biochemistry (S.-C.P., G.-W.C.) and Molecular Biology (S.H.K.),
Gyeongsang National University, Chinju, 660-701, Korea
Arabadopsis dynamin-like (ADL) 2, a member of the
high-molecular weight (Mr) dynamin family
found in Arabidopsis, has been shown to be targeted to the plastid. In
the chloroplast, most of the ADL2 was present in the fraction
containing the envelope membranes when analyzed by suborganellar
fractionation. Sucrose gradient and gel filtration experiments showed
that when associated with membranes, ADL2 existed as a
high-Mr complex, whereas the soluble form
existed as a monomer. The recombinant ADL2 expressed in
Escherichia coli was present as a
high-Mr form and showed higher GTPase
activity at a low NaCl concentration, whereas ADL2 existed as a
low-Mr form with a low level of GTPase
activity at a high NaCl concentration. Electron microscopy studies
revealed that the purified recombinant ADL2 formed spiral-coiled
structures or rings. In the presence of
guanosine-5'-O-(3-thio)triphosphate, these
structures were transformed into a long rod structure. In contrast, in
the presence of GDP, these structures disassembled into oligomers that
were shown to be tetramer with 4-fold symmetry. Finally, a
lipid-binding assay revealed that recombinant ADL2 purified from
E. coli bound specifically to phosphatidylinositol 4-phosphate. Together, these results demonstrated that the biochemical properties of ADL2 were very similar to those of dynamin and other related proteins. Based on this similarity, we propose that ADL2 may be
involved in vesicle formation at the chloroplast envelope membrane.
1
This work was supported by a grant from National
Creative Research Initiatives from the Ministry of Science and Technology.
*
Corresponding author; e-mail ihhwang{at}postech.ac.kr; fax
82-54-279-8159.
© 2001 American Society of Plant Physiologists
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