A novel DNA helicase with strand-annealing activity from the crenarchaeon Sulfolobus solfataricus
| العنوان: | A novel DNA helicase with strand-annealing activity from the crenarchaeon Sulfolobus solfataricus |
|---|---|
| المؤلفون: | Francesca M. Pisani, Mariarita De Felice, Valentina Aria, Mariarosaria De Falco, Biagio Pucci, Luca Esposito, Mosè Rossi |
| المساهمون: | De Felice, M., Aria, V., Esposito, L., De Falco, M., Pucci, B., Rossi, Mose', Pisani, F. M. |
| المصدر: | Biochemical journal (Lond., 1984) 408 (2007): 87–95. doi:10.1042/BJ20070134 info:cnr-pdr/source/autori:De Felice M.; Aria V.; Esposito L.; De Falco M.; Pucci B.; Rossi M.; Pisani F.M./titolo:A novel DNA helicase with strand annealing activity from the crenarchaeon Sulfolobus solfataricus/doi:10.1042%2FBJ20070134/rivista:Biochemical journal (Lond., 1984)/anno:2007/pagina_da:87/pagina_a:95/intervallo_pagine:87–95/volume:408 |
| بيانات النشر: | Portland Press Ltd., 2007. |
| سنة النشر: | 2007 |
| مصطلحات موضوعية: | DNA recombination, ved/biology.organism_classification_rank.species, DNA helicase, Biochemistry, Catalysis, Substrate Specificity, law.invention, chemistry.chemical_compound, Adenosine Triphosphate, law, Annealing activity, Molecular Biology, biology, ved/biology, Hydrolysis, Circular bacterial chromosome, Sulfolobus solfataricus, DNA Helicases, DNA replication, Helicase, DNA, Cell Biology, Archaea, DNA-pairing activity, chemistry, biology.protein, Recombinant DNA, Primase, Dimerization, genome stability, Research Article, Protein Binding |
| الوصف: | To protect their genetic material cells adopt different mechanisms linked to DNA replication, recombination and repair. Several proteins function at the interface of these DNA transactions. In the present study, we report on the identification of a novel archaeal DNA helicase. BlastP searches of the Sulfolobus solfataricus genome database allowed us to identify an open reading frame (SSO0112, 875 amino acid residues) having sequence similarity with the human RecQ5β. The corresponding protein, termed Hel112 by us, was produced in Escherichia coli in soluble form, purified to homogeneity and characterized. Gel-filtration chromatography and glycerol-gradient sedimentation analyses revealed that Hel112 forms monomers and dimers in solution. Biochemical characterization of the two oligomeric species revealed that only the monomeric form has an ATP-dependent 3′–5′ DNA-helicase activity, whereas, unexpectedly, both the monomeric and dimeric forms possess DNA strand-annealing capability. The Hel112 monomeric form is able to unwind forked and 3′-tailed DNA structures with high efficiency, whereas it is almost inactive on blunt-ended duplexes and bubble-containing molecules. This analysis reveals that S. solfataricus Hel112 shares some enzymatic features with the RecQ-like DNA helicases and suggests potential cellular functions of this protein. |
| وصف الملف: | STAMPA |
| تدمد: | 1470-8728 0264-6021 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e8f8e9aa26d66a81bdb750e9a39ca34Test https://doi.org/10.1042/bj20070134Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....0e8f8e9aa26d66a81bdb750e9a39ca34 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14708728 02646021 |
|---|