tRNA-like structures. Structure, function and evolutionary significance
| Autor: | Ruud M.W. Mans, Leendert Bosch, Cornelis W. A. Pleij |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
chemistry.chemical_classification
Messenger RNA Base Sequence Genes Viral Chemistry Molecular Sequence Data Biological Evolution Biochemistry Ribosome Amino acid Elongation factor Structure-Activity Relationship RNA Transfer Genes Bacterial Transfer RNA Protein biosynthesis Animals Humans Nucleic Acid Conformation Ternary complex Protein secondary structure |
| Zdroj: | European Journal of Biochemistry. 201:303-324 |
| ISSN: | 1432-1033 0014-2956 |
| Popis: | The structurally and functionally best known RNA molecule is undoubtedly transfer RNA (tRNA). tRNA owes its name to the central role it performs in protein biosynthesis: it mediates the transfer of amino acids to the ribosome. In this process the amino acid is bound to the 3′-CCA end of tRNA by an aminoacyl-tRNA synthetase. The charged tRNA forms additionally a ternary complex with GTP and an elongation factor, like the prokaryotic EF-Tu or the eukaryotic EF-1α. This complex enters the ribosome, where tRNA with its an-ticodon interacts specifically with one of the codon triplets of the messenger RNA (mRNA). Subsequently, the amino acid is covalently bound to the C-terminus of a growing polypeptide chain. This short description of protein biosynthesis reveals that tRNA interacts with many components of this process. To understand these interactions at the molecular level is the main objective of many studies of molecular biologists. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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