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J. Biol. Chem., Vol. 275, Issue 48, 37838-37845, December 1, 2000
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From the Nascent polypeptide-associated complex (NAC) is
probably the first cytosolic protein to contact nascent polypeptide
chains emerging from ribosomes. In this way NAC prevents inappropriate interactions with other factors. Eventually other factors involved in
targeting and folding, like the Signal Recognition Particle or
cytosolic chaperones, must gain access to the nascent chain. All NAC
preparations to date consist of two copurifying polypeptides. Here we
rigorously show that these two polypeptides, termed
The
and 
Subunit of the Nascent Polypeptide-associated
Complex Have Distinct Functions*
,¶
Cellular Biochemistry and Biophysics Program, Memorial
Sloan-Kettering Cancer Center, New York, New York 10021 and the
§ Department of Pharmacology, School of Dentistry, Nagasaki University,
1-7-1 Sakamoto, Nagasaki 852, Japan
- and 
NAC,
form a very stable complex in vivo and in vitro
and that a functional complex can be reconstituted from the individual subunits. A dissection of the contributions of the individual subunits
to NACs function revealed that both subunits are in direct contact with
nascent polypeptide chains on the ribosome and that both contribute to
the prevention of inappropriate interactions. However, NAC alone
directly binds to the ribosome and is sufficient to prevent ribosome
binding to the endoplasmic reticulum membrane.
*
This work was supported by a Fellowship from the Deutsche
Forschungsgemeinschaft (to B. B.), by The Sloan-Kettering Institute (to M. W.), and by Grant GM50920-01 from the National Institutes of
Health (to M. W.).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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