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J. Biol. Chem., Vol. 276, Issue 4, 2340-2346, January 26, 2001
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From the The Sec61p complex forms the core element of the
protein translocation complex (translocon) in the rough endoplasmic
reticulum (rough ER) membrane. Translating or nontranslating ribosomes
bind with high affinity to ER membranes that have been stripped of ribosomes or to liposomes containing purified Sec61p. Here we present
evidence that the
In Vitro Binding of Ribosomes to the
Subunit of
the Sec61p Protein Translocation Complex*
,¶
Department of Cell Biology, New York
University School of Medicine, New York, New York 10016 and
§ Cellular Biochemistry and Biophysics Program, Memorial
Sloan-Kettering Cancer Center, New York, New York 10021
subunit of the complex (Sec61) makes contact
with nontranslating ribosomes. A fusion protein containing the Sec61
cytoplasmic domain (Sec61c) prevents the binding
of ribosomes to stripped ER-derived membranes and also binds to
ribosomes directly with an affinity close to the affinity of ribosomes
for stripped ER-derived membranes. The ribosome binding activity of Sec61c, like that of native ER membranes, is sensitive
to high salt concentrations and is not based on an unspecific
charge-dependent interaction of the relatively basic
Sec61c domain with ribosomal RNA. Like stripped ER
membranes, the Sec61c sequence binds to large ribosomal
subunits in preference over small subunits. Previous studies have shown
that Sec61 is inessential for ribosome binding and protein
translocation, but translocation is impaired by the absence of
Sec61, and it has been proposed that Sec61 assists in the
insertion of nascent proteins into the translocation pore. Our results
suggest a physical interaction of the ribosome itself with Sec61;
this may normally occur alongside interactions between the ribosome and
other elements of Sec61p, or it may represent one stage in a temporal
sequence of binding.
*
This work was supported in part by a grant from the American
Cancer Society and by the National Institutes of Health Medical Scientist Training Program.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 © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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