In: FEBS Letters , 276 (1990), Nr. 1,2. pp. 103-107.
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.
|Journal or Publication Title:||FEBS Letters|
|Date Deposited:||30. Apr 2008 17:28|
|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|