Amino Acid Residue Penultimate to the Amino-terminal Gly Residue Strongly Affects Two Cotranslational Protein Modifications, N-Myristoylation andN-Acetylation
| Autor: | Daisuke Takemura, Toshihiko Utsumi, Hiroyuki Iwata, Masahiro Sato, Kengo Nakano, Rumi Ishisaka |
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| Rok vydání: | 2001 |
| Předmět: |
DNA
Complementary Reticulocytes Ovalbumin Amino Acid Motifs Blotting Western Mutant Glycine Transfection Biochemistry chemistry.chemical_compound Protein biosynthesis Animals Humans Amino Acids Molecular Biology Polyacrylamide gel electrophoresis chemistry.chemical_classification COS cells Models Genetic Tumor Necrosis Factor-alpha Acetylation Cell Biology N-Myristoylation Precipitin Tests Amino acid chemistry Protein Biosynthesis COS Cells Mutation Mutagenesis Site-Directed Electrophoresis Polyacrylamide Gel lipids (amino acids peptides and proteins) Rabbits Myristic Acids DNA Plasmids |
| Zdroj: | Journal of Biological Chemistry. 276:10505-10513 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m006134200 |
| Popis: | 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 motif, Met-Gly-X-X-X-Ser-X-X-X, strongly affected the susceptibility of the protein to two different cotranslational protein modifications, N-myristoylation and N-acetylation; 10 amino acids (Ala, Ser, Cys, Thr, Val, Asn, Leu, Ile, Gln, and His) with a radius of gyration smaller than 1.80 A directed N-myristoylation, two negatively charged residues (Asp and Glu) directed N-acetylation, and two amino acids (Gly and Met) directed heterogeneous modification with both N-myristoylation and N-acetylation. The amino acid requirements at this position for the two modifications were dramatically changed when Ser at position 6 in the consensus motif was replaced with Ala. Thus, the amino acid residue penultimate to the N-terminal Gly residue strongly affected two cotranslational protein modifications, N-myristoylation and N-acetylation, and the amino acid requirements at this position for these two modifications were significantly affected by downstream residues. |
| Databáze: | OpenAIRE |
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