An archaeal protein homologous to mammalian SRP54 and bacterial Ffh recognizes a highly conserved region of SRP RNA
| Autor: | Tadanori Aimi, Tsutomu Morinaga, Takuzi Itoh, Hideki Maeshima, Emi Okuno |
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| Rok vydání: | 2001 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Archaeal Proteins 5.8S ribosomal RNA Molecular Sequence Data Biophysics RNA-binding protein Biology Biochemistry 54 kDa protein of signal recognition particle Methionine Structural Biology Genetics Animals Humans Signal recognition particle RNA Amino Acid Sequence Binding site Cloning Molecular Molecular Biology Conserved Sequence Mammals Binding Sites Base Sequence Sequence Homology Amino Acid Escherichia coli Proteins RNA Nuclease protection assay Cell Biology Non-coding RNA Molecular biology RNA binding protein Pyrococcus furiosus RNA editing 7S RNA Signal Recognition Particle |
| Zdroj: | FEBS letters. 507(3) |
| ISSN: | 0014-5793 |
| Popis: | The gene encoding the 54 kDa protein of signal recognition particle (SRP54) in the hyperthermophilic archaeon Pyrococcus furiosus has been cloned and sequenced. Recombinant P. furiosus SRP54 (pf-SRP54) and the N-terminal G-domain and C-terminal M-domain (pf-SRP54M) of pf-SRP54 with an amino-terminal addition of six histidine residues were expressed in Escherichia coli and subjected to binding experiments for SRP RNA, non-conserved 213-nucleotide RNA (helices 1, 2, 3, 4 and 5) and conserved 107-nucleotide RNA (helices 6 and 8) from SRP RNA. The RNA binding properties of the purified protein were determined by filter binding assays. The histidine-tagged pf-SRP54M bound specifically to the conserved 107-nucleotide RNA in the absence of pf-SRP19, unlike the eukaryotic homologue, with an apparent binding constant (K) of 18 nM. |
| Databáze: | OpenAIRE |
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