Back to Search
Start Over
A novel DNA helicase with strand-annealing activity from the crenarchaeon Sulfolobus solfataricus
- Source :
- 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
- Publication Year :
- 2007
- Publisher :
- Portland Press Ltd., 2007.
-
Abstract
- 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.
- Subjects :
- 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
Subjects
Details
- ISSN :
- 14708728 and 02646021
- Volume :
- 408
- Database :
- OpenAIRE
- Journal :
- Biochemical Journal
- Accession number :
- edsair.doi.dedup.....0e8f8e9aa26d66a81bdb750e9a39ca34