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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.
Participation of a cathepsin L-type protease in the activation of caspase-3.
Results suggested that a cathepsin L-type protease activity might participate in the activation mechanism of caspase-3 in the presence of the supernatant of the digitonin-treated ML.
Activation of caspase‐3‐like protease by digitonin‐treated lysosomes
Mechanism of alpha-tocopheryl succinate-induced apoptosis of promyelocytic leukemia cells.
Results indicate that VES-induced apoptosis of HL-60 cells might be caused by activation of the caspase cascade coupled with modulation of mitochondrial membrane function.
Resistance to nitric oxide-mediated apoptosis in HL-60 variant cells is associated with increased activities of Cu,Zn-superoxide dismutase and catalase.
Thyroxine enhancement and the role of reactive oxygen species in tadpole tail apoptosis.
Transmembrane TNF (pro‐TNF) is palmitoylated