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J. Biol. Chem., Vol. 275, Issue 49, 38929-38937, December 8, 2000
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From the Ubiquitin-dependent proteolysis of
specific target proteins is required for several important steps during
the cell cycle. Degradation of such proteins is strictly cell
cycle-regulated and triggered by two large ubiquitin ligases, termed
anaphase-promoting complex (APC) and Skp1/Cullin/F-box complex (SCF).
Here we show that yeast Ran-binding protein 1 (Yrb1p), a predominantly
cytoplasmic protein implicated in nucleocytoplasmic transport, is
required for cell cycle regulated protein degradation. Depletion of
Yrb1p results in the accumulation of unbudded G1
cells and of cells arrested in mitosis implying a function of Yrb1p in
the G1/S transition and in the progression through mitosis.
Temperature-sensitive yrb1-51 mutants are defective in
APC-mediated degradation of the anaphase inhibitor protein Pds1p and in
degradation of the cyclin-dependent kinase inhibitor Sic1p,
a target of SCF. Thus, Yrb1p is crucial for efficient APC- and
SCF-mediated proteolysis of important cell cycle regulatory proteins.
We have identified the UBS1 gene as a multicopy suppressor
of yrb1-51 mutants. Ubs1p is a nuclear protein, and its
deletion is synthetic lethal with a yrb1-51 mutation. Interestingly, UBS1 was previously identified as a
multicopy suppressor of cdc34-2 mutants, which are
defective in SCF activity. We suggest that Ubs1p may represent a link
between nucleocytoplasmic transport and ubiquitin ligase activity.
Yeast Ran-binding Protein Yrb1p Is Required for Efficient
Proteolysis of Cell Cycle Regulatory Proteins Pds1p and Sic1p*
,,, and¶
Institute of Microbiology and Genetics,
Georg-August-University, Grisebachstrasse 8, D-37077 Göttingen,
Germany and § Ruprecht-Karls-University Heidelberg,
Biochemie-Zentrum Heidelberg, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany
*
This work was supported by Deutsche Forschungsgemeinschaft
Grants IR36/1-2 and KU1235/1-2 and by funds from the Fonds der Chemischen Industrie and the Volkswagen-Stiftung.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 © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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