Reference - Detail
| RRC ID | 55053 |
|---|---|
| Author | Wei T, Yang K, Zang J, Mao D. |
| Title | Biochemical characterization of the nuclease StoNurA from the hyperthermophilic archaeon Sulfolobus tokodaii. |
| Journal | An Acad Bras Cienc |
| Abstract |
The DNA nuclease gene ST2109 has been cloned from the hyperthermophilic archaeon Sulfolobus tokodaii and expressed in Escherichia coli. The recombinant protein StoNurA has been purified to homogeneity by affinity chromatography and gel filtration chromatography. Biochemical analyses demonstrated that StoNurA exhibited DNA binding and 5'-3' exonuclease activities towards ssDNA and dsDNA. The temperature and pH optima of StoNurA were determined to be 65 °C and 8.0, respectively. The activity of StoNurA was found to be dependent of Mn2+, and its half-life of heat inactivation at 100 °C was 5 min. Gel filtration chromatography revealed that StoNurA could form dimers in solution. Pull-down assays also showed that StoNurA physically interacted with a DNA helicase (StoHerA). Our data suggest that NurA may play a key functional role in the processing of DNA recombinational repair. |
| Volume | 90(3) |
| Pages | 2731-2740 |
| Published | 2018-1-1 |
| DOI | 10.1590/0001-3765201820160031 |
| PII | S0001-37652018000602731 |
| PMID | 30304218 |
| MeSH | Chromatography, Affinity Chromatography, Gel Cloning, Molecular DNA, Archaeal / genetics* Deoxyribonucleases / genetics Deoxyribonucleases / metabolism* Hydrogen-Ion Concentration Sulfolobus / enzymology* Sulfolobus / genetics Sulfolobus / metabolism Time Factors |
| IF | 0.938 |
| Times Cited | 0 |
| Altmetric score |
オルトメトリクス指標項目
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| The most frequently cited source | X(Twitter) |
| Total number of mentions | 3 |
| Altmetric score changes over past 6months | 0.0 |
| Resource | |
| General Microbes | JCM 10545 |