Nascent polypeptide-associated complex protein prevents mistargeting of nascent chains to the endoplasmic reticulum Journal Article

   


Authors: Lauring, B.; Sakai, H.; Kreibich, G.; Wiedmann, M.
Article Title: Nascent polypeptide-associated complex protein prevents mistargeting of nascent chains to the endoplasmic reticulum
Abstract: We show that, after removal of the nascent polypeptide-associated complex (NAC) from ribosome-associated nascent chains, ribosomes synthesizing proteins lacking signal peptides are efficiently targeted to the endoplasmic reticulum (ER) membrane. After this mistargeting, translocation across the ER membrane occurs, albeit less efficiently than for a nascent secretory polypeptide, perhaps because the signal peptide is needed to catalyze the opening of the translocation pore. The mistargeting was prevented by the addition of purified NAC and was shown not to be mediated by the signal recognition particle and its receptor. Instead, it appears to be a consequence of the intrinsic affinity of ribosomes for membrane binding sites, since it can be blocked by competing ribosomes that lack associated nascent polypeptides. We propose that, when bound to a signalless ribosome- associated nascent polypeptide, NAC sterically blocks the site in the ribosome for membrane binding.
Keywords: unclassified drug; nonhuman; animal cell; animal; protein targeting; animalia; endoplasmic reticulum; dog; dogs; signal peptide; protein transport; binding sites; biological transport; ribosomal proteins; ribosome protein; membrane binding; ribosomes; polypeptide; canis familiaris; ribosome; protein sorting signals; signal recognition particle; priority journal; article; support, non-u.s. gov't; support, u.s. gov't, p.h.s.; nascent polypeptide associated complex protein
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 92
Issue: 12
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 1995-06-06
Start Page: 5411
End Page: 5415
Language: English
DOI: 10.1073/pnas.92.12.5411
PUBMED: 7777521
PROVIDER: scopus
PMCID: PMC41704
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029076816&doi=10.1073%2fpnas.92.12.5411&partnerID=40&md5=ce0875f7ec900b79edc7830b9da5c771
Notes: Article -- Correction issued, see Proc Natl Acad Sci U S A 1995 Aug 15;92(17):8088 -- Export Date: 28 August 2018 -- Source: Scopus
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  1. Martin Wiedmann
    44 Wiedmann
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