A ribosomal protein from Thermus thermophilus is homologous to a general shock protein
| Autor: | Anders Liljas, Natalia Davydova, M. B. Garber, O. I. Gryaznova, G.M. Gongadze, Bengt-Harald Jonsson |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Ribosomal Proteins
Molecular Sequence Data Sequence alignment Biology Biochemistry 5S ribosomal RNA Bacterial Proteins Ribosomal protein Escherichia coli Amino Acid Sequence Codon Genetics Base Sequence Sequence Homology Amino Acid Thermus thermophilus RNA Ribosomal 5S Shine-Dalgarno sequence RNA-Binding Proteins General Medicine Ribosomal RNA biology.organism_classification Ribosomal binding site Genes Bacterial 5S rRNA binding Sequence Alignment Bacillus subtilis |
| Zdroj: | Biochimie. 78(11-12) |
| ISSN: | 0300-9084 |
| Popis: | The gene encoding the ribosomal protein from Thermus thermophilus, TL5, which binds to the 5S rRNA, has been cloned and sequenced. The codon usage shows a clear preference for G/C rich codons that is characteristic for many genes in thermophilic bacteria. The deduced amino acid sequence consists of 206 residues. The sequence of TL5 shows a strong similarity to a general shock protein from Bacillus subtilis, named CTC. The protein CTC is homologous in its N-terminal part to the 5S rRNA binding protein, L25, from E coli. An alignment of the TL5, CTC and L25 sequences displays a number of residues that are totally conserved. No clear sequence similarity was found between TL5 and other proteins which are known to bind to 5S rRNA. The evolutionary relationship of a heat shock protein in mesophiles and a ribosomal protein in thermophilic bacteria as well as a possible role of TL5 in the ribosome are discussed. |
| Databáze: | OpenAIRE |
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