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J. Biol. Chem., Vol. 277, Issue 38, 34760-34765, September 20, 2002
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From the Department of Biochemistry, Molecular Biology, and Cell
Biology, Northwestern University, Evanston, Illinois 60208-3500
The proteasome can actively unfold proteins by
sequentially unraveling their substrates from the attachment point of
the degradation signal. To investigate the steric constraints imposed
on substrate proteins during their degradation by the proteasome, we
constructed a model protein in which specific parts of the polypeptide
chain were covalently connected through disulfide bridges. The
cross-linked model proteins were fully degraded by the proteasome, but
two or more cross-links retarded the degradation slightly. These
results suggest that the pore of the proteasome allows the concurrent passage of at least three stretches of a polypeptide chain. A degradation channel that can tolerate some steric bulk may reconcile the two opposing needs for degradation that is compartmentalized to
avoid aberrant proteolysis yet able to handle a range of substrates of
various sizes.
Concurrent Translocation of Multiple Polypeptide Chains through
the Proteasomal Degradation Channel*
*
This work as supported by CAREER award MCB-9875857 from the
National Science Foundation.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: Dept. of Biochemistry,
Molecular Biology, and Cell Biology, Northwestern University, 2153 Sheridan Rd., Evanston, IL 60208-3500. Tel.: 847-467-3570; Fax:
847-467-6489; E-mail: matouschek@northwestern.edu.
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