Protein splicing , or protein splicing , is an intramolecular autocatalytic process that occurs in some proteins , in which the inner part of the protein (called ) is cleaved from the precursor protein, followed by ligation of the remaining parts. At the site of splicing in the precursor protein is cysteine or serine , that is, an amino acid with a nucleophilic side group. The currently known splicing reactions do not require exogenous cofactors and energy sources (for example, ATP or GTP ). Prior to the discovery of protein splicing, the word “splicing” meant splicing of pre- mRNA .
History
Protein splicing was discovered by two research groups (Anraku and Stevens) in 1990 . Both groups discovered the Saccharomyces cerevisiae yeast VMA1 protein, a precursor of vacuolar H + ATPase . The amino acid sequence of the N- and C-ends of VMA1 corresponds to the sequence of the vacuolar H + -ATPase of other organisms by 70%, while the central sequence coincides by 30% with the yeast HO.
See also
- Splicing (values)