A novel DNA helicase with strand annealing activity from the crenarchaeon Sulfolobus solfataricus (Articolo in rivista)

Type
Label
  • A novel DNA helicase with strand annealing activity from the crenarchaeon Sulfolobus solfataricus (Articolo in rivista) (literal)
Anno
  • 2007-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1042/BJ20070134 (literal)
Alternative label
  • De Felice M.; Aria V.; Esposito L.; De Falco M.; Pucci B.; Rossi M.; Pisani F.M. (2007)
    A novel DNA helicase with strand annealing activity from the crenarchaeon Sulfolobus solfataricus
    in Biochemical journal (Lond., 1984)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • De Felice M.; Aria V.; Esposito L.; De Falco M.; Pucci B.; Rossi M.; Pisani F.M. (literal)
Pagina inizio
  • 87 (literal)
Pagina fine
  • 95 (literal)
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  • Il DOI 10.1042//BJ20070134 riportato nel pdf e nel database bibliografico non è corretto e quindi recuperabile dal Resolver DOI. Quello esatto ha un solo slash: 10.1042/BJ20070134 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 408 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 1 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Biochimica delle Proteine, Consiglio Nazionale delle Ricerche, Via P. Castellino, 111.80131-Napoli, Italy (literal)
Titolo
  • A novel DNA helicase with strand annealing activity from the crenarchaeon Sulfolobus solfataricus (literal)
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 this study, we report on the identification of a novel archaeal DNA helicase. BlastP searches of Sulfolobus solfataricus genome database allowed us to identify an open reading frame (SSO0112, 875 amino acid residues) having sequence similarity with the human RecQ5beta. The corresponding protein, named by us Hel112, was produced in Escherichia coli in soluble form, purified to homogeneity and characterised. Gel filtration chromatography and glycerol gradient sedimentation analyses revealed that Hel112 forms monomers and dimers in solution. Biochemical characterisation 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 form 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. (literal)
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