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.
Document type: | Article |
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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 |
DDC-classification: | 570 Life sciences |
Series: | Works by Bernhard Dobberstein |