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First published online 1 April 2003
doi: 10.1242/jcs.00423
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Research Article |

1 Department of NanoBiophotonics, Max Planck Institute for Biophysical
Chemistry, Am Fassberg 11, 37077 Göttingen, Germany
2 Institut für Physiologische Chemie, Universität München,
Butenandtstrasse 5, 81377 München, Germany
Author for correspondence (e-mail:
sjakobs{at}gwdg.de)
Accepted 11 February 2003
The mitochondrial compartment of budding yeast (Saccharomyces
cerevisiae) is a highly dynamic net-like structure of tubules that
constantly undergo fusion and fission. The outer membrane protein Fis1p plays
a crucial role in mitochondrial fission. Here we report on the temporal and
spatial dynamics of this organelle in wild-type cells and in
fis1
mutants. Mitochondria of fis1
mutants
adapt their mitochondrial network to a change in carbon source. We find that
the frequencies of apparent matrix separation and fusion events decrease in
both wild-type cells and in mutants lacking Fis1p upon glucose repression.
Matrix separation could be caused by matrix constriction and does not
necessarily require fission of the inner or outer membrane. Double-labelling
experiments demonstrated that some of these matrix separations in
fis1 mutants are due to genuine tubule fissions, whereas others do
not involve fission of the outer membrane. The rates of matrix separation in
fis1
mutants almost approach those of the wildtype,
demonstrating that, although apparently involved in outer membrane fission,
Fis1p is not crucial for the separation of the mitochondrial matrix. In
mutants lacking the GTPase Dnm1p no complete tubule fissions were recorded,
although dnm1
mutants display matrix separations as well. The
data suggest that different molecular machineries are responsible for the
separation of the matrix and the fission of the outer membrane in budding
yeast.
Key words: Saccharomyces cerevisiae, Fluorescence microscopy, Glucose repression, Membrane fission, Organelle morphology
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