Amino Acid Residue Penultimate to the Amino-terminal Gly Residue Strongly Affects Two Cotranslational Protein Modifications, N-Myristoylation andN-Acetylation*

@article{Utsumi2001AminoAR,
  title={Amino Acid Residue Penultimate to the Amino-terminal Gly Residue Strongly Affects Two Cotranslational Protein Modifications, N-Myristoylation andN-Acetylation*},
  author={Toshihiko Utsumi and M. Sato and Kengo Nakano and D Takemura and H Iwata and Rumi Ishisaka},
  journal={The Journal of Biological Chemistry},
  year={2001},
  volume={276},
  pages={10505 - 10513}
}
To examine the amino-terminal sequence requirements for cotranslational protein N-myristoylation, a series of site-directed mutagenesis of N-terminal region were performed using tumor necrosis factor as a nonmyristoylated model protein. Subsequently, the susceptibility of these mutants to protein N-myristoylation was evaluated by metabolic labeling in an in vitro translation system or in transfected cells. It was found that the amino acid residue at position 3 in an N-myristoylation consensus… 
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Vertical-scanning mutagenesis of amino acids in a model N-myristoylation motif reveals the major amino-terminal sequence requirements for protein N-myristoylation.
TLDR
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.
The consensus motif for N‐myristoylation of plant proteins in a wheat germ cell‐free translation system
TLDR
A wheat germ cell‐free translation system with high protein productivity is applied to examine the N‐myristoylation of various wild‐type and mutant forms of Arabidopsis’thaliana proteins to demonstrate the relationship between efficiency and variability of amino acids at positions’3, 6 and 7 of the motif.
Effects of Myristoylation on the Structure and Stability of Hisactophilin
TLDR
The structure and stability of the protein have only been characterized using the recombinant non-myristoylated protein, and the effects of myristoylation on hisactophilin structure and Stability are focused on.
Protein N-Myristoylation Plays a Critical Role in the Endoplasmic Reticulum Morphological Change Induced by Overexpression of Protein Lunapark, an Integral Membrane Protein of the Endoplasmic Reticulum
TLDR
It was found that protein Lunapark, the human ortholog of yeast protein Lnp1p that has recently been found to be involved in network formation of the endoplasmic reticulum (ER), is an N-myristoylated polytopic integral membrane protein.
N-terminal modifications of cellular proteins: The enzymes involved, their substrate specificities and biological effects
TLDR
The different protein N‐terminal modifications occurring co‐ or post‐translationally with emphasis on the responsible enzymes and their substrate specificities are reviewed.
N‐Terminal protein modifications in an insect cell‐free protein synthesis system and their identification by mass spectrometry
TLDR
The results suggest that N‐terminal modifications occurring in the insect cell‐free protein synthesis system are quite similar to those observed in the mammalianprotein synthesis system.
The N‐terminus of B96Bom, a Bombyx mori G‐protein‐coupled receptor, is N‐myristoylated and translocated across the membrane
TLDR
Results indicate that the N‐myristoylated N‐terminus of B96Bom is translocated across the membrane and exposed to the extracellular surface.
Posttranslational N-Myristoylation Is Required for the Anti-apoptotic Activity of Human tGelsolin, the C-terminal Caspase Cleavage Product of Human Gelsolin*
TLDR
It was found that the C-terminal caspase cleavage product of human gelsolin (tGelsolin) was efficiently N-myristoylated, indicating that posttranslational N- myristoylation of tGelsol does not direct mitochondrial targeting, but this modification is involved in the anti-apoptotic activity of t Gelsolin.
Identification of dually acylated proteins from complementary DNA resources by cell-free and cellular metabolic labeling.
N-terminal protein modifications: Bringing back into play the ribosome.
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