title: The dynamin-related GTPase, Dnm1p, controls mitochondrial morphology in yeast.
abstract: The Saccharomyces cerevisiae Dnm1 protein is structurally related to dynamin, a GTPase required for membrane scission during endocytosis. Here we show that Dnm1p is essential for the maintenance of mitochondrial morphology. Disruption of the DNM1 gene causes the wild-type network of tubular mitochondrial membranes to collapse to one side of the cell but does not affect the morphology or distribution of other cytoplasmic organelles. Dnm1 proteins containing point mutations in the predicted GTP-binding domain or completely lacking the GTP-binding domain fail to rescue mitochondrial morphology defects in a dnm1 mutant and induce dominant mitochondrial morphology defects in wild-type cells. Indirect immunofluorescence reveals that Dnm1p is distributed in punctate structures at the cell cortex that colocalize with the mitochondrial compartment. These Dnm1p-containing structures remain associated with the spherical mitochondria found in an mdm10 mutant strain. In addition, a portion of Dnm1p cofractionates with mitochondrial membranes during differential sedimentation and sucrose gradient fractionation of wild-type cells. Our results demonstrate that Dnm1p is required for the cortical distribution of the mitochondrial network in yeast, a novel function for a dynamin-related protein.
authors.affiliation: Department of Biology, University of Utah, Salt Lake City, Utah 84112, USA.
authors.forename: D
authors.initials: D
authors.lastname: Otsuga
authors.forename: B R
authors.initials: BR
authors.lastname: Keegan
authors.forename: E
authors.initials: E
authors.lastname: Brisch
authors.forename: J W
authors.initials: JW
authors.lastname: Thatcher
authors.forename: G J
authors.initials: GJ
authors.lastname: Hermann
authors.forename: W
authors.initials: W
authors.lastname: Bleazard
authors.forename: J M
authors.initials: JM
authors.lastname: Shaw
mesh_terms: D000199:Actins / Q000032:analysis; D002874:Chromosome Mapping; D004272:DNA, Mitochondrial / Q000032:analysis; D034284:Dynamin I; D034281:Dynamins; D004705:Endocytosis / Q000502:physiology; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D020558:GTP Phosphohydrolases / Q000235:genetics / Q000378:metabolism*; D017353:Gene Deletion; D007700:Kinetics; D008854:Microscopy, Electron; D008870:Microtubules / Q000737:chemistry / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology* / Q000648:ultrastructure; D024101:Mitochondrial Proteins; D016297:Mutagenesis, Site-Directed / Q000502:physiology; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000166:cytology / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins; D013347:Subcellular Fractions / Q000737:chemistry / Q000201:enzymology; D014404:Tubulin / Q000032:analysis; D014617:Vacuoles / Q000648:ultrastructure
chemical_list: D000199:Actins; D004272:DNA, Mitochondrial; D005656:Fungal Proteins; D024101:Mitochondrial Proteins; D029701:Saccharomyces cerevisiae Proteins; D014404:Tubulin; D034284:Dynamin I; D020558:GTP Phosphohydrolases; C094774:DNM1 protein, S cerevisiae; D034281:Dynamins