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The 68 kDa protein of signal recognition particle contains a glycine-richregion also found in certain RNA-binding proteins

Herz, Joachim and Flint, Nicholas and Stanley, Keith and Frank, Rainer and Dobberstein, Bernhard

In: FEBS Letters , 276 (1990), Nr. 1,2. pp. 103-107.

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Abstract

Signal recognition particle (SRP) interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the endoplasmic reticulum. Membrane targeting is mediated by the 68 and the 72 kDa proteins of SRP. We have cloned and sequenced cDNA encoding the 68 kDa protein of canine signal recognition particle (SRP68). SRP68 is a basic protein comprised of 622 amino acid residues. Close to the amino terminus there is a glycine-rich region which SRP68 has in common with some RNA-binding proteins. SRP68 shares no detectable similarity to any of the proteins in data libraries.

Item Type: Article
Journal or Publication Title: FEBS Letters
Volume: 276
Number: 1,2
Date Deposited: 30. Apr 2008 17:28
Date: 1990
Page Range: pp. 103-107
Faculties / Institutes: Service facilities > Center for Molecular Biology Heidelberg
Subjects: 570 Life sciences
Uncontrolled Keywords: Signal recognition particle , Translocation , Ribonucleoprotein particle , Glycine-rich
Schriftenreihe ID: Works by Bernhard Dobberstein
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