NDLI: A general mechanism for regulation of access to the translocon: Competition for a membrane attachment site on ribosomes

Content Provider	PubMed Central
Author	Möller, Ines Jung, Martin Beatrix, Birgitta Levy, Robert Kreibich, Gert Zimmermann, Richard Wiedmann, Martin Lauring, Brett
Copyright Year	1998
Abstract	For proteins to enter the secretory pathway, the membrane attachment site (M-site) on ribosomes must bind cotranslationally to the Sec61 complex present in the endoplasmic reticulum membrane. The signal recognition particle (SRP) and its receptor (SR) are required for targeting, and the nascent polypeptide associated complex (NAC) prevents inappropriate targeting of nonsecretory nascent chains. In the absence of NAC, any ribosome, regardless of the polypeptide being synthesized, binds to the endoplasmic reticulum membrane, and even nonsecretory proteins are translocated across the endoplasmic reticulum membrane. By occupying the M-site, NAC prevents all ribosome binding unless a signal peptide and SRP are present. The mechanism by which SRP overcomes the NAC block is unknown. We show that signal peptide-bound SRP occupies the M-site and therefore keeps it free of NAC. To expose the M-site and permit ribosome binding, SR can pull SRP away from the M-site without prior release of SRP from the signal peptide.
Starting Page	13425
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	23
Volume Number	95
Language	English
Publisher	The National Academy of Sciences
Publisher Date	1998-11-10
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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A general mechanism for regulation of access to the translocon: competition for a membrane attachment site on ribosomes.

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