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Amino Acid Residue Penultimate to the Amino-terminal Gly Residue Strongly Affects Two Cotranslational Protein Modifications, N-Myristoylation andN-Acetylation*
- T. Utsumi, M. Sato, K. Nakano, D. Takemura, H. Iwata, R. Ishisaka
- Biology, ChemistryThe Journal of Biological Chemistry
- 30 March 2001
The amino acid residue penultimate to the N-terminal Gly residue strongly affected two cotranslational protein modifications, N-myristoylation andN-acetylation, and the amino acid requirements at this position for these two modifications were significantly affected by downstream residues.
C‐terminal 15 kDa fragment of cytoskeletal actin is posttranslationally N‐myristoylated upon caspase‐mediated cleavage and targeted to mitochondria
Vertical-scanning mutagenesis of amino acids in a model N-myristoylation motif reveals the major amino-terminal sequence requirements for protein N-myristoylation.
The amino acid requirements found in this study were fully consistent with the N-terminal sequence of 78 N- myristoylated proteins in which N-myristoylation was experimentally verified and strongly indicate that the combination of amino acids at position 3, 6 and 7 is a major determinant for protein N-Myristoylations.