ArticleThe Biochemical journal2004
Modular organization of a Cdc6-like protein from the crenarchaeon Sulfolobus solfataricus.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Dimerization of Sir3 via its C-terminal winged helix domain is essential for yeast heterochromatin formation.The EMBO journal · 2013Article
- DnaA protein DNA-binding domain binds to Hda protein to promote inter-AAA+ domain interaction involved in regulatory inactivation of DnaA.The Journal of biological chemistry · 2011Article
- Trypanosome prereplication machinery: a potential new target for an old problem.Enzyme research · 2011Article
- Trypanosome prereplication machinery contains a single functional orc1/cdc6 protein, which is typical of archaea.Eukaryotic cell · 2009Article
- Archaeal eukaryote-like Orc1/Cdc6 initiators physically interact with DNA polymerase B1 and regulate its functions.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Thermoplasma acidophilum Cdc6 protein stimulates MCM helicase activity by regulating its ATPase activity.Nucleic acids research · 2008Article
- The architecture of the DNA replication origin recognition complex in Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Characterization of the Cdc6 Homologues from the Euryarchaeon Thermoplasma acidophilum.The open biochemistry journal · 2008Article
- Biochemical characterization of two Cdc6/ORC1-like proteins from the crenarchaeon Sulfolobus solfataricus.Extremophiles : life under extreme conditions · 2006Article
- Interactions between the archaeal Cdc6 and MCM proteins modulate their biochemical properties.Nucleic acids research · 2005Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the present paper, we report that a Cdc6 (cell-division control)-like factor from the hyperthermophilic crenarchaeon Sulfolobus solfataricus (referred to as SsoCdc6-2) has a modular organization of its biological functions. A reliable model of the SsoCdc6-2 three-dimensional structure was built up, based on the significant sequence identity with the Pyrobaculum aerophylum Cdc6 (PaeCdc6), whose crystallographic structure is known. This allowed us to design two truncated forms of SsoCdc6-2: the DeltaC (residues 1-297, molecular mass 35 kDa) and the DeltaN (residues 298-400, molecular mass 11 kDa) proteins. The DeltaC protein contains the nucleotide-binding Rossmann fold and the Sensor-2 motif (Domains I and II in the PaeCdc6 structure), and retains the ability to bind and hydrolyse ATP. On the other hand, the DeltaN protein contains the C-terminal WH (winged helix)-fold (Domain III), and is able to bind DNA molecules and to inhibit the DNA helicase activity of the SsoMCM (mini-chromosome maintenance) complex, although with lesser efficiency with respect to the full-sized SsoCdc6-2. These results provide direct biochemical evidence that the Cdc6 WH-domain is responsible for DNA-binding and inhibition of MCM DNA helicase activity.
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