Signal peptide
Signal peptide
Signal peptide (pronunciation: /ˈsɪɡnəl ˈpiːptaɪd/), also known as leader peptide or presequence, is a short (3-60 amino acids long) peptide chain that directs the post-translational transport of a protein.
Etymology
The term "signal peptide" was first used in 1975 by Günter Blobel and David D. Sabatini, who proposed the "signal hypothesis" to explain the translocation of proteins across the endoplasmic reticulum membrane.
Function
Signal peptides function as a postal code for proteins, directing them to their correct locations within the cell. They are usually found at the N-terminus of the protein sequence and are cleaved off by a signal peptidase once the protein reaches its destination.
Related terms
- Signal peptidase: An enzyme that cleaves the signal peptide from the protein.
- Endoplasmic reticulum: A cellular organelle where signal peptides direct the proteins.
- Translocation: The process of moving a protein to its correct location within the cell.
- Post-translational modification: Modifications made to a protein after it has been synthesized, including the removal of the signal peptide.
See also
External links
- Medical encyclopedia article on Signal peptide
- Wikipedia's article - Signal peptide
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