| Structural highlights
Function
[CDC63_SULSO] Involved in regulation of DNA replication. May play essential roles in origin recognition and cell cycle control of replication. Binds to DNA, with a preference for molecules that contain a bubble, a fork, or a tail. Inhibits the binding of the MCM helicase to the origin DNA and inhibits its DNA helicase activity. Also regulates the DNA polymerase and the nuclease activities of PolB1. Inhibits the DNA-binding activity of Cdc6-1 and Cdc6-2.[1] [2] [3] [4] [CDC61_SULSO] Involved in regulation of DNA replication. May play essential roles in origin recognition and cell cycle control of replication. Binds to DNA, with a preference for molecules that contain a bubble, a fork, or a tail. Inhibits the binding of the MCM helicase to the origin DNA and strongly inhibits its DNA helicase activity. Also regulates the DNA polymerase and the nuclease activities of PolB1. Stimulates the DNA-binding activity of Cdc6-3.[5] [6] [7] [8]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The faithful duplication of genetic material depends on essential DNA replication initiation factors. Cellular initiators form higher-order assemblies on replication origins, using adenosine triphosphate (ATP) to locally remodel duplex DNA and facilitate proper loading of synthetic replisomal components. To better understand initiator function, we determined the 3.4 angstrom-resolution structure of an archaeal Cdc6/Orc1 heterodimer bound to origin DNA. The structure demonstrates that, in addition to conventional DNA binding elements, initiators use their AAA+ ATPase domains to recognize origin DNA. Together these interactions establish the polarity of initiator assembly on the origin and induce substantial distortions into origin DNA strands. Biochemical and comparative analyses indicate that AAA+/DNA contacts observed in the structure are dynamic and evolutionarily conserved, suggesting that the complex forms a core component of the basal initiation machinery.
Replication origin recognition and deformation by a heterodimeric archaeal Orc1 complex.,Dueber EL, Corn JE, Bell SD, Berger JM Science. 2007 Aug 31;317(5842):1210-3. PMID:17761879[9]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ De Felice M, Esposito L, Rossi M, Pisani FM. Biochemical characterization of two Cdc6/ORC1-like proteins from the crenarchaeon Sulfolobus solfataricus. Extremophiles. 2006 Feb;10(1):61-70. Epub 2005 Sep 23. PMID:16179962 doi:http://dx.doi.org/10.1007/s00792-005-0473-0
- ↑ Jiang PX, Wang J, Feng Y, He ZG. Divergent functions of multiple eukaryote-like Orc1/Cdc6 proteins on modulating the loading of the MCM helicase onto the origins of the hyperthermophilic archaeon Sulfolobus solfataricus P2. Biochem Biophys Res Commun. 2007 Sep 28;361(3):651-8. Epub 2007 Jul 25. PMID:17673179 doi:http://dx.doi.org/10.1016/j.bbrc.2007.07.073
- ↑ Wang J, Jiang PX, Feng H, Feng Y, He ZG. Three eukaryote-like Orc1/Cdc6 proteins functionally interact and mutually regulate their activities of binding to the replication origin in the hyperthermophilic archaeon Sulfolobus solfataricus P2. Biochem Biophys Res Commun. 2007 Nov 9;363(1):63-70. Epub 2007 Aug 31. PMID:17825793 doi:http://dx.doi.org/10.1016/j.bbrc.2007.08.125
- ↑ Zhang L, Zhang L, Liu Y, Yang S, Gao C, Gong H, Feng Y, He ZG. Archaeal eukaryote-like Orc1/Cdc6 initiators physically interact with DNA polymerase B1 and regulate its functions. Proc Natl Acad Sci U S A. 2009 May 12;106(19):7792-7. doi:, 10.1073/pnas.0813056106. Epub 2009 Apr 29. PMID:19416914 doi:http://dx.doi.org/10.1073/pnas.0813056106
- ↑ De Felice M, Esposito L, Rossi M, Pisani FM. Biochemical characterization of two Cdc6/ORC1-like proteins from the crenarchaeon Sulfolobus solfataricus. Extremophiles. 2006 Feb;10(1):61-70. Epub 2005 Sep 23. PMID:16179962 doi:http://dx.doi.org/10.1007/s00792-005-0473-0
- ↑ Jiang PX, Wang J, Feng Y, He ZG. Divergent functions of multiple eukaryote-like Orc1/Cdc6 proteins on modulating the loading of the MCM helicase onto the origins of the hyperthermophilic archaeon Sulfolobus solfataricus P2. Biochem Biophys Res Commun. 2007 Sep 28;361(3):651-8. Epub 2007 Jul 25. PMID:17673179 doi:http://dx.doi.org/10.1016/j.bbrc.2007.07.073
- ↑ Wang J, Jiang PX, Feng H, Feng Y, He ZG. Three eukaryote-like Orc1/Cdc6 proteins functionally interact and mutually regulate their activities of binding to the replication origin in the hyperthermophilic archaeon Sulfolobus solfataricus P2. Biochem Biophys Res Commun. 2007 Nov 9;363(1):63-70. Epub 2007 Aug 31. PMID:17825793 doi:http://dx.doi.org/10.1016/j.bbrc.2007.08.125
- ↑ Zhang L, Zhang L, Liu Y, Yang S, Gao C, Gong H, Feng Y, He ZG. Archaeal eukaryote-like Orc1/Cdc6 initiators physically interact with DNA polymerase B1 and regulate its functions. Proc Natl Acad Sci U S A. 2009 May 12;106(19):7792-7. doi:, 10.1073/pnas.0813056106. Epub 2009 Apr 29. PMID:19416914 doi:http://dx.doi.org/10.1073/pnas.0813056106
- ↑ Dueber EL, Corn JE, Bell SD, Berger JM. Replication origin recognition and deformation by a heterodimeric archaeal Orc1 complex. Science. 2007 Aug 31;317(5842):1210-3. PMID:17761879 doi:http://dx.doi.org/317/5842/1210
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