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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.
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.
Effect of Polysaccharide Conjugation or Transglutaminase Treatment on the Allergenicity and Functional Properties of Soy Protein
Monitoring of polyclonal antibody titers by an indirect enzyme-linked immunosorbent assay and immunoblotting of rabbit sera, monoclonal antibody, and human allergic sera showed that soy protein−galactomannan conjugation was more effective in reducing the allergenicity of the soy protein than transglutaminase treatments and/or chymotrypsin.
A part of the transmembrane domain of pro-TNF can function as a cleavable signal sequence that generates a biologically active secretory form of TNF.
The in vitro translation/translocation assay involving a canine pancreatic microsomal membrane system including a mutant, Delta-75-47, -32-1, revealed that the N-terminal half of the transmembrane domain of pro-TNF consisting of 14 residues functioned as a cleavable signal sequence; it generated a cleaved form of TNF having a molecular mass similar to that of mature TNF.
Activation of macrophages by sulfated glycopeptides in ovomucin, yolk membrane, and chalazae in chicken eggs.
- H. Tanizaki, H. Tanaka, H. Iwata, A. Kato
- Biology, ChemistryBioscience, biotechnology, and biochemistry
- 23 November 1997
In vitro culture assay with macrophages showed that the protease digests of ovomucin, yolk membrane, and chalazae induced morphologic alteration and increased H2O2 generation and IL-1 production in lower concentration (100 micrograms/ml).
Met-Gly-Cys motif from G-protein alpha subunit cannot direct palmitoylation when fused to heterologous protein.
- T. Utsumi, E. Tou, D. Takemura, R. Ishisaka, M. Yabuki, H. Iwata
- Biology, ChemistryArchives of biochemistry and biophysics
- 15 January 1998
Heterologous fusion proteins containing the first 10 amino acids of Gi1 alpha and Gs alpha using tumor necrosis factor as a model protein determined their ability to incorporate palmitate using in vitro and in vivo expression systems and indicated the Met-Gly-Cys motif found in G-protein alpha subunits itself is not sufficient to direct palmitoylation even if Gly-2 is myristoylated after removal of initiating Met.