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Vol. 12, Issue 9, 2756-2766, September 2001
*Department of Biology, University of Utah, Salt Lake City, Utah
84112
Dnm1p belongs to a family of dynamin-related GTPases required to
remodel different cellular membranes. In budding yeast,
Dnm1p-containing complexes assemble on the cytoplasmic surface of the
outer mitochondrial membrane at sites where mitochondrial tubules
divide. Our previous genetic studies suggested that Dnm1p's GTPase
activity was required for mitochondrial fission and that Dnm1p
interacted with itself. In this study, we show that bacterially
expressed Dnm1p can bind and hydrolyze GTP in vitro.
Coimmunoprecipitation studies and yeast two-hybrid analysis suggest
that Dnm1p oligomerizes in vivo. With the use of the yeast two-hybrid
system, we show that this Dnm1p oligomerization is mediated, in part,
by a C-terminal sequence related to the GTPase effector domain (GED) in
dynamin. The Dnm1p interactions characterized here are similar to those
reported for dynamin and dynamin-related proteins that form higher
order structures in vivo, suggesting that Dnm1p assembles to form rings or collars that surround mitochondrial tubules. Based on previous findings, a K705A mutation in the Dnm1p GED is predicted to
interfere with GTP hydrolysis, stabilize active Dnm1p-GTP, and
stimulate a rate-limiting step in fission. Here we show that expression of the Dnm1 K705A protein in yeast enhances mitochondrial fission. Our
results provide evidence that the GED region of a dynamin-related protein modulates a rate-limiting step in membrane fission.
These authors contributed equally to this work.
Current address: Department of Biology, Minnesota
State University at Moorhead, Moorhead, MN 56563.
§
Corresponding author. E-mail address:
shaw{at}bioscience.utah.edu.
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