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M513530200v1
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Papers In Press, published online ahead of print April 6, 2006
J. Biol. Chem, 10.1074/jbc.M513530200
Submitted on December 20, 2005
Revised on February 27, 2006
Accepted on April 6, 2006

Dimeric DNM1-G385D interacts with MDV1 on mitochondria and can be stimulated to assemble into fission complexes containing MDV1 and FIS1

Debjani Bhar, Mary Anne Karren, Markus Babst, and Janet M. Shaw

Biochemistry Dept., University of Utah, Salt Lake City, Utah 84112-5650

Corresponding Author: shaw{at}biochem.utah.edu

Interactions between yeast Dnm1p, Mdv1p and Fis1p are required to form fission complexes that catalyze division of the mitochondrial compartment. During the formation of mitochondrial fission complexes, the Dnm1p GTPase self-assembles into large multimeric complexes on the outer mitochondrial membrane that are visualized as punctate structures by fluorescent labeling. Although it is clear that Fis1p-Mdv1p complexes on mitochondria are required for the initial recruitment of Dnm1p, it is not clear whether Dnm1p puncta assemble before or after this recruitment step. Here we show that the minimum oligomeric form of cytoplasmic Dnm1p is a dimer. The middle domain mutant protein Dnm1G385Dp forms dimers in vivo but fails to assemble into punctate structures. However, this dimeric mutant stably interacts with Mdv1p on the outer mitochondrial membrane, demonstrating that assembly of stable Dnm1p multimers is not required for Dnm1p-Mdv1p association or for mitochondrial recruitment of Dnm1p. Dnm1G385Dp is reported to be a terminal dimer in vitro. We describe conditions that allow assembly of Dnm1G385Dp into functional fission complexes on mitochondria in vivo. Using these conditions, we demonstrate that multimerization of Dnm1p is required to promote reorganization of Mdv1p from a uniform mitochondrial localization into punctate fission complexes. Our studies also reveal that Fis1p is present in these assembled fission complexes. Based on our results, we propose that Dnm1p dimers are initially recruited to the membrane via interaction with Mdv1p-Fis1p complexes. These dimers then assemble into multimers that subsequently promote the reorganization of Mdv1p into punctate fission complexes.


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