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J. Biol. Chem., Vol. 276, Issue 2, 1618-1625, January 12, 2001
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From the Department of Cell Biology, University of Alberta,
Edmonton, Alberta T6G 2H7, Canada
Peroxins are proteins required for peroxisome
assembly. The cytosolic peroxin Pex20p binds directly to the
A Role for the Peroxin Pex8p in Pex20p-dependent
Thiolase Import into Peroxisomes of the Yeast Yarrowia
lipolytica*
and
-oxidation enzyme thiolase and is necessary for its dimerization and
peroxisomal targeting. The intraperoxisomal peroxin Pex8p has a role in
the import of peroxisomal matrix proteins, including thiolase. We report the results of yeast two-hybrid analyses with various peroxins of the yeast Yarrowia lipolytica and characterize more
fully the interaction between Pex8p and Pex20p. Coimmunoprecipitation
showed that Pex8p and Pex20p form a complex, while in vitro
binding studies demonstrated that the interaction between Pex8p and
Pex20p is specific, direct, and autonomous. Pex8p fractionates with
peroxisomes in cells of a PEX20 disruption strain,
indicating that Pex20p is not necessary for the targeting of Pex8p to
peroxisomes. In cells of a PEX8 disruption strain, thiolase
is mostly cytosolic, while Pex20p and a small amount of thiolase
associate with peroxisomes, suggesting the involvement of Pex8p in the
import of thiolase after docking of the Pex20p-thiolase complex to the
membrane. In the absence of Pex8p, peroxisomal thiolase and Pex20p are
protected from the action of externally added protease. This finding,
together with the fact that Pex8p is intraperoxisomal, suggests that
Pex20p may accompany thiolase into peroxisomes during import.
*
This work was supported by grant MT-9208 from the Medical
Research Council of Canada (MRC) (to R. A. R.).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.
Recipient of an MRC studentship.
§
An MRC Senior Scientist and an International Research Scholar of
the Howard Hughes Medical Institute. To whom all correspondence should
be addressed: Dept. of Cell Biology, 5-14 Medical Sciences Bldg.,
University of Alberta, Edmonton, Alberta T6G 2H7, Canada. Tel.:
780-492-9868; Fax: 780-492-9278; E-mail:
rick.rachubinski@ualberta.ca.
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