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The Arabidopsis Dynamin-Like Proteins ADL1C and ADL1E Play a Critical Role in Mitochondrial Morphogenesis

^a Center for Plant Intracellular Trafficking, Pohang University of Science and Technology, Pohang 790-784, Korea
^b Division of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Korea
^c Department of Biology, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China

¹ To whom correspondence should be addressed. E-mail ihhwang{at}postech.ac.kr; fax 82-54-279-8159

Dynamin-related proteins are high molecular weight GTP binding proteins and have been implicated in various biological processes. Here, we report the functional characterization of two dynamin homologs in Arabidopsis, Arabidopsis dynamin-like 1C (ADL1C) and Arabidopsis dynamin-like 1E (ADL1E). ADL1C and ADL1E show a high degree of amino acid sequence similarity with members of the dynamin family. However, both proteins lack the C-terminal Pro-rich domain and the pleckstrin homology domain. Expression of the dominant-negative mutant ADL1C[K48E] in protoplasts obtained from leaf cells caused abnormal mitochondrial elongation. Also, a T-DNA insertion mutation at the ADL1E gene caused abnormal mitochondrial elongation that was rescued by the transient expression of ADL1C and ADL1E in protoplasts. In immunohistochemistry and in vivo targeting experiments in Arabidopsis protoplasts, ADL1C and ADL1E appeared as numerous speckles and the two proteins colocalized. These speckles were partially colocalized with F1-ATPase-:RFP, a mitochondrial marker, and ADL2b localized at the tip of mitochondria. These results suggest that ADL1C and ADL1E may play a critical role in mitochondrial fission in plant cells.

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