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J. Biol. Chem., Vol. 276, Issue 24, 21601-21607, June 15, 2001
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Department of Biochemistry and Cell Biology and the Institute for
Cell and Developmental Biology, State University of New York at Stony
Brook, Stony Brook, New York 11794-5215
In addition to a role in DNA repair events in
yeast, several lines of evidence indicate that the Rad23 protein
(Rad23p) may regulate the activity of the 26 S proteasome. We report
evidence that a de-N-glycosylating enzyme, Png1p, may be
involved in the proteasomal degradation pathway via its binding to
Rad23p. Interaction of Rad23p and Png1p was first detected by
two-hybrid screening, and this interaction in vivo was
confirmed by biochemical analyses. The Png1p-Rad23p complex was shown
to be distinct from the well established DNA repair complex,
Rad4p-Rad23p. We propose a model in which Rad23p functions as an escort
protein to link the 26 S proteasome with proteins such as Rad4p or
Png1p to regulate their cellular activities.
Rad23 Provides a Link between the Png1
Deglycosylating Enzyme and the 26 S Proteasome in Yeast*
*
This work was supported by National Institutes of Health
Grant GM33184 (to W. J. L.).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.
To whom correspondence should be addressed. Tel.: 631-632-8560;
Fax: 631-632-8575; E-mail: wlennarz@notes.cc.sunysb.edu.
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