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J. Biol. Chem., Vol. 276, Issue 45, 42422-42435, November 9, 2001
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From the Cells are capable of adapting to changes in their
environment by synthesizing needed proteins and degrading superfluous
ones. Pichia pastoris synthesizes peroxisomal enzymes to
grow in methanol medium. Upon adapting from methanol medium to one
containing glucose, this yeast rapidly and selectively degrades
peroxisomes by an autophagic process referred to as pexophagy. In this
study, we have utilized a novel approach to identify genes required for this degradative pathway. Our approach involves the random integration of a vector containing the Zeocin resistance gene into the yeast genome
by restriction enzyme-mediated integration. Cells unable to degrade
peroxisomes during glucose adaptation were isolated, and the genes that
were disrupted by the insertion of the vector were determined by
sequencing. By using this approach, we have identified a number of
genes required for glucose-induced selective autophagy of peroxisomes (GSA genes). We report here the
characterization of Gsa11, a unique 208-kDa protein. We found that this
protein is required for glucose-induced pexophagy and
starvation-induced autophagy. Gsa11 is a cytosolic protein that becomes
associated with one or more structures situated near the vacuole during
glucose adaptation. The punctate localization of Gsa11 was not observed in gsa10, gsa12, gsa14, and
gsa19 mutants. We have previously shown that Gsa9 appears
to relocate from a compartment at the vacuole surface to regions
between the vacuole and the peroxisomes being sequestered. In the
gsa11 mutants, the vacuole only partially surrounded the
peroxisomes, but Gsa9 was still distributed around the peroxisome
cluster. This suggests that Gsa9 binds to the peroxisomes independent
of the vacuole. The data also indicate that Gsa11 is not necessary for
Gsa9 to interact with peroxisomes but acts at an intermediate event
required for the vacuole to engulf the peroxisomes.
GSA11 Encodes a Unique 208-kDa
Protein Required for Pexophagy and Autophagy in Pichia
pastoris*
, Institute for Cancer Research, Department of
Cell Biology, The Norwegian Radium Hospital, Montebello,
N-0310 Oslo, Norway and the § Department of Anatomy and
Cell Biology, University of Florida College of Medicine,
Gainesville, Florida 32610-0235
*
This work was supported by National Science Foundation Grant
MCB-9817002 (to W. A. D.) and a grant from The Norwegian Cancer Society (to P. E. S.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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