Journal
TRAFFIC
Volume 9, Issue 9, Pages 1471-1484Publisher
WILEY
DOI: 10.1111/j.1600-0854.2008.00772.x
Keywords
dynamin-related proteins; microbodies; organelle fission; yeast
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We show that Mdv1 and Caf4, two components of the mitochondrial fission machinery in Saccharomyces cerevisiae, also function in peroxisome proliferation. Deletion of MDV1, CAF4 or both, however, had only a minor effect on peroxisome numbers at peroxisome-inducing growth conditions, most likely related to the fact that Vps1 - and not Dnm1 - is the key player in peroxisome fission in this organism. In contrast, in Hansenula polymorpha, which has only a Dnm1-dependent peroxisome fission machinery, deletion of MDV1 led to a drastic reduction of peroxisome numbers. This phenotype was accompanied by a strong defect in mitochondrial fission. The MDV1 paralog CAF4 is absent in H. polymorpha. In wild-type H. polymorpha, cells Dnm1-mCherry and green fluorescent protein (GFP)-Mdv1 colocalize in spots that associate with both peroxisomes and mitochondria. Furthermore, Fis1 is essential to recruit Mdv1 to the peroxisomal and mitochondrial membrane. However, formation of GFP-Mdv1 spots - and related to this normal organelle fission - is strictly dependent on the presence of Dnm1. In dnm1 cells, GFP-Mdv1 is dispersed over the surface of peroxisomes and mitochondria. Also, in H. polymorpha mdv1 or fis1 cells, the number of Dnm1-GFP spots is strongly reduced. These spots still associate to organelles but are functionally inactive.
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