The α and β subunit of the nascent polypeptide-associated complex have distinct functions Journal Article

  


Authors: Beatrix, B.; Sakai, H.; Wiedmann, M.
Article Title: The α and β subunit of the nascent polypeptide-associated complex have distinct functions
Abstract: 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 α- and βNAC, 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, βNAC alone directly binds to the ribosome and is sufficient to prevent ribosome binding to the endoplasmic reticulum membrane.
Keywords: immunohistochemistry; signal transduction; protein expression; unclassified drug; nonhuman; animal cell; mouse; animals; mice; complex formation; protein protein interaction; protein targeting; cell protein; cell line; protein binding; animalia; endoplasmic reticulum; amino acid sequence; molecular sequence data; dogs; nucleic acids; recombinant proteins; trans-activators; protein folding; chromatography, gel; polypeptide; molecular chaperones; signal recognition particle; priority journal; article; protein nac
Journal Title: Journal of Biological Chemistry
Volume: 275
Issue: 48
ISSN: 0021-9258
Publisher: American Society for Biochemistry and Molecular Biology  
Date Published: 2000-12-01
Start Page: 37838
End Page: 37845
Language: English
DOI: 10.1074/jbc.M006368200
PUBMED: 10982809
PROVIDER: scopus
DOI/URL:

http://www.scopus.com/inward/record.url?eid=2-s2.0-0034528831&partnerID=40&md5=ee951bbca77cf904e0bade8b88415a6a
Notes: Export Date: 18 November 2015 -- Source: Scopus
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MSK Authors
  1. Martin Wiedmann
    44 Wiedmann
  2. Birgitta M Beatrix
    4 Beatrix
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