- Previous Names
- P2A, 2A/2B polyprotein cleavage mechanism (1)
Viral 2A sequences modify the activity of the ribosome to promote hydrolysis of the peptidyl(2A)-tRNA(Gly) ester linkage, thereby releasing the polypeptide from the translational complex, in a manner that allows the synthesis of a discrete downstream translation product (2B) to proceed. This process produces a ribosomal 'skip' from one codon to the next without the formation of a peptide bond. The 2A peptide consensus motif (2A, Asp-Val/Ile-Glu-X-Asn-Pro-Gly; 2B, Pro) is associated with cleavage activity between the 2A glycine and the 2B proline. The 2A peptide impairs normal peptide bond formation between the 2A glycine and the 2B proline without affecting the translation of 2B.