Protein splicing
Protein splicing is an intramolecular reaction of certain proteins in a protein segment, the intein mentioned is cut out of the protein. The resulting N-and C -terminal ends of the protein ( exteins ) are linked, so that again a continuous peptide chain is formed. The splice site of the initial protein is usually a cysteine or serine; these amino acids have nucleophilic side chains. All previously known protein - splicing proceed without external energy sources such as ATP.
Protein splicing heard in contrast to mRNA splicing to the post-translational modifications of proteins.
Inteins
There are four types of inteins: Maxi - intein, mini - intein trans-splicing intein, and alanine - intein. Maximum inteins are N -and C-terminal splicing containing an endonuclease domain. Mini- inteins are also N-and C -terminal splice sites; However, they do not contain endonuclease domain. Trans - splicing inteins are split inteins in N- and C -terminus. Alanine inteins have an alanine instead of cysteine as a splice or serine.
Development of the concept of splicing
The term splicing has been known in connection with the processing of the mRNA. The process of Proteinspleißens was discovered in 1990 by the groups of Anraku and Stevens in Saccharomyces cerevisiae.
Left
- Short rewiev
- Protein splicing mechanism and intein structure
- Post-translational modification