Open AccessN‐Terminal Methionine Processing
Author(s) -
Wingfield Paul T.
Publication year - 2017
Publication title -
current protocols in protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.409
H-Index - 32
eISSN - 1934-3663
pISSN - 1934-3655
DOI - 10.1002/cpps.29
Subject(s) - methionine , residue (chemistry) , chemistry , biochemistry , radius of gyration , terminal (telecommunication) , stereochemistry , amino acid , computer science , organic chemistry , polymer , telecommunications
Protein synthesis is initiated by methionine in eukaryotes and by formylmethionine in prokaryotes. N‐terminal methionine can be co‐translationally cleaved by the enzyme methionine aminopeptidase (MAP). When recombinant proteins are expressed in bacterial and mammalian expression systems, there is a simple universal rule that predicts whether the initiating methionine will be processed by MAP based on the size of the residue adjacent (penultimate) to the N‐methionine. In general, if the side chains of the penultimate residues have a radius of gyration of 1.29 Å or less, methionine is cleaved. © 2017 by John Wiley & Sons, Inc.