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The N-terminus (also known as the amino-terminus, NH2-terminus, N-terminal end or amine-terminus) refers to the start of a protein or polypeptide terminated by an amino acid with a free amine group (-NH2). By convention, peptide sequences are written N-terminus to C-terminus, left to right in LTR languages. This correlates the translation direction to the text direction (because when a protein is translated from messenger RNA, it is created from N-terminus to C-terminus - amino acids are added to the carbonyl end).
Each amino acid has an amine group and a carboxylic group. Amino acids link to one another by peptide bonds which form through a dehydration reaction that joins the carboxyl group of one amino acid to the amine group of the next in a head-to-tail manner to form a polypeptide chain. The chain has two ends - an amine group, the N-terminus, and an unbound carboxyl group, the C-terminus.
When a protein is translated from messenger RNA, it is created from N-terminus to C-terminus. The amino end of an amino acid (on a charged tRNA) during the elongation stage of translation, attaches to the carboxyl end of the growing chain. Since the start codon of the genetic code codes for the amino acid methionine, most protein sequences start with a methionine (or, in bacteria, mitochondria and chloroplasts, the modified version N-formylmethionine, fMet). However, some proteins are modified posttranslationally, for example, by cleavage from a protein precursor, and therefore may have different amino acids at their N-terminus.
N-Terminal targeting signals
The N-terminus is the first part of the protein that exits the ribosome during protein biosynthesis. It often contains signal peptide sequences, "intracellular postal codes" that direct delivery of the protein to the proper organelle. The signal peptide is typically removed at the destination by a signal peptidase. The N-terminal amino acid of a protein is an important determinant of its half-life (likelihood of being degraded). This is called the N-end rule.
The N-terminal signal peptide is recognized by the signal recognition particle (SRP) and results in the targeting of the protein to the secretory pathway. In eukaryotic cells, these proteins are synthesized at the rough endoplasmic reticulum. In prokaryotic cells, the proteins are exported across the cell membrane. In chloroplasts, signal peptides target proteins to the thylakoids.
Mitochondrial targeting peptide
The N-terminal mitochondrial targeting peptide (mtTP) allows for the protein to be imported into the mitochondrion.
Chloroplast targeting peptide
The N-terminal chloroplast targeting peptide (cpTP) allows for the protein to be imported into the chloroplast.
Protein N-termini can be modified co - or posttranslationally. Modifications include the removal of initiator methionine (iMet) by aminopeptidases, attachment of small chemical groups such as acetyl, propionyl and methyl, and the addition of membrane anchors, such as palmitoyl and myristoyl groups
N-terminal acetylation is a form of protein modification that can occur in both prokaryotes and eukaryotes. It has been suggested that N-terminal acetylation can prevent a protein from following a secretory pathway.
The N-terminus can be modified by the addition of a myristoyl anchor. Proteins that are modified this way contain a consensus motif at their N-terminus as a modification signal.
- TopFIND, a scientific database covering proteases, their cleavage site specificity, substrates, inhibitors and protein termini originating from their activity
- Voet, Donald; Voet, Judith G.; Pratt, Charlotte W. (2013). Fundamentals of Biochemistry: Life at the Molecular Level (4th ed.). Hoboken, NJ: Wiley. ISBN 0470547847.
- Varland (April 21, 2015). "N-terminal modiﬁcations of cellular proteins:The enzymes involved, their substrate speciﬁcities and biological effects". Proteomics. 15: 2385–401. doi:10.1002/pmic.201400619. PMC . PMID 25914051.
- Arnesen, Thomas (May 31, 2011). "Towards a Functional Understanding of Protein N-Terminal Acetylation". PLoS Biology. 9: e1001074. doi:10.1371/journal.pbio.1001074.