The signal sequence of nascent preprolactin interacts with the 54K polypeptide of the signal recognition particle View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1986-04-01

AUTHORS

T. V. Kurzchalia, M. Wiedmann, A. S. Girshovich, E. S. Bochkareva, H. Bielka, T. A. Rapoport

ABSTRACT

Hydrophobic signal sequences direct the translocation of nascent secretory proteins and many membrane proteins across the membrane of the endoplasmic reticulum1,2. Initiation of this process involves the signal recognition particle (SRP)3,4, which consists of six polypeptide chains and a 7S RNA4 and interacts with ribosomes carrying nascent secretory polypeptide chains. In the case of aminoterminal, cleavable signal sequences, in the absence of microsomal membranes it exerts a site-specific translational arrest in vitro3,5,6. The size of the arrested fragment (60–70 amino-acid residues) suggests that elongation stops when the signal sequence has emerged fully from the ribosome. However, a direct interaction between the signal sequence and SRP has not previously been demonstrated and has even been questioned recently7. We now show for the first time a direct interaction between the signal sequence of a secretory protein and a component of SRP, the 54K polypeptide (relative molecular mass (Mr) 54,000). This was achieved by means of a new method of affinity labelling which involves the translational incorporation of an amino acid, carrying a photoreactive group, into nascent polypeptides. More... »

PAGES

634-636

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/320634a0

DOI

http://dx.doi.org/10.1038/320634a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1038743774

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/3010127


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