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Assembly of the 68- and 72-kD Proteins of Signal Recognition Particle with 7S RNA

Lütcke, Henrich and Prehn, Siegfried and Ashford, Anthony J. and Remus, Michael and Frank, Rainer and Dobberstein, Bernhard

In: The Journal of Cell Biology, 121 (1993), Nr. 5. pp. 977-985.

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Abstract

Signal recognition particle (SRP), the cytoplasmic ribonucleoprotein particle that mediates the targeting of proteins to the ER, consists of a 7S RNA and six different proteins. The 68- (SRP68) and 72-(SRP72) kD proteins of SRP are bound to the 7S RNA of SRP as a heterodimeric complex (SRP68/72). Here we describe the primary structure of SRP72 and the assembly of SRP68, SRP72 and 7S RNA into a ribonucleoprotein particle. The amino acid sequence deduced from the cDNA of SRP72 reveals a basic protein of 671 amino acids which shares no sequence similarity with any protein in the sequence data libraries. Assembly of SRP72 into a ribonucleoprotein particle required the presence of 7S RNA and SRP68. In contrast, SRP68 alone specifically bound to 7S RNA. SRP68 contacts the 7S RNA via its NH2-terminal half while COOH-terminal portions of SRP68 and SRP72 are in contact with each other in SRP. SRP68 thus serves as a link between 7S RNA and SRP72. As a large NH2-terminal domain of SRP72 is exposed on SRP it may be a site of contact to other molecules involved in the SRP cycle between the ribosome and the ER membrane.

Item Type: Article
Journal or Publication Title: The Journal of Cell Biology
Volume: 121
Number: 5
Date Deposited: 22. Jul 2008 14:52
Date: 1993
Page Range: pp. 977-985
Faculties / Institutes: Service facilities > Center for Molecular Biology Heidelberg
Subjects: 570 Life sciences
Schriftenreihe ID: Works by Bernhard Dobberstein
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