Protein synthesis in Escherichia coli with mischarged tRNA
| Autor: | Gregory Raczniak, Bokkee Min, Dieter Söll, Carla Polycarpo, Suk Namgoong, Hiroyuki Kobayashi, Makoto Kitabatake, Joanne Pelaschier, Benfang Ruan |
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| Rok vydání: | 2003 |
| Předmět: |
Mutant
Aspartate—tRNA ligase Aspartate-tRNA Ligase Mutation Missense Heterologous Tryptophan synthase Genetics and Molecular Biology RNA Transfer Amino Acyl medicine.disease_cause Microbiology RNA Transfer medicine Protein biosynthesis Escherichia coli Tryptophan Synthase Molecular Biology biology Escherichia coli Proteins Tryptophan Peptide Elongation Factors Molecular biology Elongation factor RNA Bacterial Biochemistry Transfer RNA biology.protein Transformation Bacterial |
| Zdroj: | Journal of bacteriology. 185(12) |
| ISSN: | 0021-9193 |
| Popis: | Two types of aspartyl-tRNA synthetase exist: the discriminating enzyme (D-AspRS) forms only Asp-tRNA Asp , while the nondiscriminating one (ND-AspRS) also synthesizes Asp-tRNA Asn , a required intermediate in protein synthesis in many organisms (but not in Escherichia coli ). On the basis of the E. coli trpA34 missense mutant transformed with heterologous ND- aspS genes, we developed a system with which to measure the in vivo formation of Asp-tRNA Asn and its acceptance by elongation factor EF-Tu. While large amounts of Asp-tRNA Asn are detrimental to E. coli , smaller amounts support protein synthesis and allow the formation of up to 38% of the wild-type level of missense-suppressed tryptophan synthetase. |
| Databáze: | OpenAIRE |
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