Protein splicing--the lengths some proteins will go to.
We review the recently discovered phenomenon of protein splicing which is the excision of an internal protein sequence at the protein level rather than at the RNA level. The means by which examples of protein splicing have been identified are described, and the similarities of the internally spliced protein products (or inteins) are discussed. Comparisons are made between inteins and group I RNA introns. We describe the evidence supporting excision of intiens by a post-translational autocatalytic reaction of a full length polypeptide precursor, rather than by RNA splicing. An examination is made of some of the proposed mechanism schemes and the supporting them presented.
Davis
E O
EO
Laboratory for Leprosy and Mycobacterial Research, National Institute for Medical Research, Mill Hill, London, England.
Jenner
P J
PJ
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017124:Conserved Sequence / Q000235:genetics; D004720:Endonucleases / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D007438:Introns; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016296:Mutagenesis; D017510:Protein Folding; D011499:Protein Processing, Post-Translational; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D005656:Fungal Proteins; D004720:Endonucleases; D010450:Endopeptidases