The recA gene from the thermophile Thermus aquaticus YT-1: cloning, expression, and characterization
| Autor: | R D Camerini-Otero, E Angov |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Hot Temperature
Molecular Sequence Data Restriction Mapping DNA Single-Stranded Gene Expression Molecular cloning medicine.disease_cause Microbiology chemistry.chemical_compound Escherichia coli medicine Amino Acid Sequence Cloning Molecular Thermus Codon Molecular Biology Peptide sequence DNA Primers Base Sequence Sequence Homology Amino Acid Thermus aquaticus biology Thermophile Nucleic acid sequence biochemical phenomena metabolism and nutrition biology.organism_classification Recombinant Proteins Kinetics Rec A Recombinases chemistry Biochemistry Genes Bacterial Thermodynamics bacteria DNA Research Article Heteroduplex |
| Zdroj: | Journal of Bacteriology. 176:1405-1412 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.176.5.1405-1412.1994 |
| Popis: | We have cloned, expressed, and purified the RecA analog from the thermophilic eubacterium Thermus aquaticus YT-1. Analysis of the deduced amino acid sequence indicates that the T. aquaticus RecA is structurally similar to the Escherichia coli RecA and suggests that RecA-like function has been conserved in thermophilic organisms. Preliminary biochemical analysis indicates that the protein has an ATP-dependent single-stranded DNA binding activity and can pair and carry out strand exchange to form a heteroduplex DNA under reaction conditions previously described for E. coli RecA, but at 55 to 65 degrees C. Further characterization of a thermophilically derived RecA protein should yield important information concerning DNA-protein interactions at high temperatures. In addition, a thermostable RecA protein may have some general applicability in stabilizing DNA-protein interactions in reactions which occur at high temperatures by increasing the specificity (stringency) of annealing reactions. |
| Databáze: | OpenAIRE |
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