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J. Biol. Chem., Vol. 275, Issue 43, 33820-33827, October 27, 2000
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From the Department of Cell Biology, Duke University Medical
Center, Durham, North Carolina 27710
Contemporary models for protein translocation in
the mammalian endoplasmic reticulum (ER) identify the termination of
protein synthesis as the signal for ribosome release from the ER
membrane. We have utilized morphometric and biochemical methods to
assess directly the fate of membrane-bound ribosomes following the
termination of protein synthesis. In these studies, tissue culture
cells were treated with cycloheximide to inhibit elongation, with
pactamycin to inhibit initiation, or with puromycin to induce premature
chain termination, and ribosome-membrane interactions were subsequently analyzed. It was found that following the termination of protein synthesis, the majority of ribosomal particles remained
membrane-associated. Analysis of the subunit structure of the
membrane-bound ribosomal particles remaining after termination was
conducted by negative stain electron microscopy and sucrose gradient
sedimentation. By both methods of analysis, the termination of protein
synthesis on membrane-bound ribosomes was accompanied by the
release of small ribosomal subunits from the ER membrane; the majority
of the large subunits remained membrane-bound. On the basis of these results, we propose that large ribosomal subunit release from the ER
membrane is regulated independently of protein translocation.
The Fate of Membrane-bound Ribosomes Following the
Termination of Protein Synthesis*
*
This work was supported by National Institutes of Health
Grant DK47897 (to C. V. N.).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 Cell
Biology, P. O. Box 3709, Duke University Medical Center, Durham, NC 27710. Tel.: 919-684-8948; Fax: 919-684-5481; E-mail:
c.nicchitta@cellbio.duke.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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