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Ubiquitin-mediated degradation of proteins occurs through the N-end rule pathway.
In eukaryotes, including humans, the N-end rule pathway is part of the ubiquitin system.
This is called the N-end rule.
ClpS is an N-recognin in the N-end rule pathway.
The N-end rule is a rule related to ubiquitination, discovered by Alexander Varshavsky and co-workers in 1986.
In both prokaryotes and eukaryotes, the exposed N-terminal residue may determine the half-life of the protein according to the N-end rule.
Johanson-Blizzard syndrome is caused by mutations in the UBR1 gene, which encodes one of several ubiquitin ligase enzymes of the N-end rule pathway.
A temperature sensitive degron takes advantage of the N-end rule pathway, in which a destabilizing N-terminal residue dramatically decreases the in vivo half-life of a protein.
However, arginine's being a large, charged amino acid is a disadvantage to the Biofusion assembly technique: these properties of arginine result in the destabilisation of the protein by the N-end rule.
The N-end rule may partially determine the half-life of a protein, and proteins with segments rich in proline, glutamic acid, serine, and threonine (the so-called PEST proteins) have short half-life.
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