Identification, Cloning, and Expression of the Gene for Adenylate Kinase from the Thermoacidophilic Archaebacterium Sulfolobus acidocaldarius
| Autor: | G. Schafer, Thomas Kath, R. Schmid |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
DNA
Bacterial Sulfolobus acidocaldarius Sequence analysis Molecular Sequence Data Biophysics Adenylate kinase Sequence alignment Biology Molecular cloning Biochemistry Escherichia coli Humans heterocyclic compounds Amino Acid Sequence Cloning Molecular Molecular Biology Peptide sequence Base Sequence Sequence Homology Amino Acid Kinase Adenylate Kinase Nucleic acid sequence Sequence Analysis DNA Molecular biology Recombinant Proteins Genes Bacterial |
| Zdroj: | Archives of Biochemistry and Biophysics. 307:405-410 |
| ISSN: | 0003-9861 |
| DOI: | 10.1006/abbi.1993.1607 |
| Popis: | An adenylate kinase gene from a member of the archaebacterial kingdom, the thermoacidophilic archaebacterium (archaeon) Sulfolobus acidocaldarius, has been cloned and sequenced for the first time. Two degenerate oligonucleotide probes, based on the N-terminal amino acid sequence information, led to the amplification of a gene-specific DNA fragment, used to screen subgenomic libraries. Comparing the DNA-derived amino acid sequence of total 194 residues with those of known procaryotic and eucaryotic adenylate kinases revealed only a low degree of similarity, except for a glycine-rich region close to the N-terminus, the so-called P-loop. Using inducible expression systems catalytically active S. acidocaldarius adenylate kinase was produced in large amounts. Although the total length of the protein and the results of alignment procedures suggest a closer relation to eucaryotic than to procaryotic sequences, the archaebacterial enzyme may represent a novel class of adenylate kinases. This is corroborated by the finding that an antiserum against this protein does not cross-react with Escherichia coli nor yeast or rabbit adenylate kinases for example. |
| Databáze: | OpenAIRE |
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