The 68 kDa protein of signal recognition particle contains a glycine‐rich region also found in certain RNA‐binding proteins
Joachim Herz, Nicholas Flint, Keith K. Stanley, Rainer Frank, Bernhard Dobberstein
Abstract
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Joachim Herz, Nicholas Flint, Keith K. Stanley, Rainer Frank, Bernhard Dobberstein
Abstract
Open-access reader
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.
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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.
Key concepts: Signal recognition particle, Signal recognition particle receptor, Signal peptide, Endoplasmic reticulum, Signal recognition particle RNA, Protein targeting, Protein Sorting Signals, Biochemistry