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analyses show that orc1 allele newly identified is female sterile and possesses a unique feature of phenotypes that are distinct in different modes of DNA replication
Orc1 functioned in silencing before duplication and Orc1 and Sir2 may have an ancient history of cooperating to generate chromatin structures, with Sir2 deacetylating histones and Orc1 binding to these deacetylated nucleosomes
The opposing effects of ORC1 (represor) and CDC6 (gene activator) in controlling the level of Cyclin E ensures genome stability and a mechanism for linking directly DNA replication and cell division commitment.
The authors have discovered that human cell lines in culture proliferate with intact chromosomal origins of replication after disruption of both alleles of ORC2 or of the ATPase subunit, ORC1.
Orc1 acts as a nucleating center for origin recognition complex assembly and then pre-replication complex assembly by binding to mitotic chromosomes, followed by gradual removal from chromatin during the G1 phase.
ORC1 harbors a G-rich RNA/ssDNA-binding domain, which may be involved in the preferential binding to G-quadruplex-formable RNA/DNA by ORC. Structure modeling predicts the structural similarity between the G-rich RNA/ssDNA-binding domain of ORC1 and part of mammalian DNA methyltransferase 1.
ORC1 associated with transcription start sites of coding or noncoding RNAs. Transcription levels at the ORC1 sites directly correlated with replication timing.
results identify the BAH domain as a novel methyl-lysine-binding module, thereby establishing the first direct link between histone methylation and the metazoan DNA replication machinery, and defining a pivotal aetiological role for the canonical H4K20me2 mark, via ORC1, in primordial dwarfism
Orc1 harbors a PACT centrosome-targeting domain and a separate domain that differentially inhibits the protein kinase activities of Cyclin E-CDK2 and Cyclin A-CDK2
Data show that purified Epstein-Barr nuclear antigen 1 EBNA1 recruits purified Human Orc1 and Cdc6 onto replication origin oriP.
A lethal phenotype was seen in four individuals with compound heterozygous ORC1 mutations
As cells moved through the cell cycle, the local-ization of ORC1 shifted, suggesting changes in thelocalization of ORC-bound origin sequences.
Mutations in ORC1, encoding a subunit of the origin recognition complex, cause microcephalic primordial dwarfism resembling Meier-Gorlin syndrome. These mutations disrupt ORC1 functions including pre-replicative complex formation and origin activation.
Data show that Orc1 specifically binds hypo-phosphorylated Rb and that this interaction is competitive with the binding of Rb to E2F1.
in human cancer cells, RBX1 silencing causes the accumulation of DNA replication licensing proteins CDT1 and ORC1, leading to DNA double-strand breaks, DDR, G(2) arrest, and, eventually, aneuploidy
a component of the origin recognition complex (ORC) that functions in DNA replication
ORC2 physically interacts with ORC1 on non-chromatin nuclear structures
Data suggest that hOrc1p is targeted for destruction by an SCF-Skp2 complex during S phase.
ORC1 regulates the status of the ORC complex in human nuclei by tethering ORCs 2-5 to nuclear structures
the ORC1 cycle in human cells is highly linked with cell cycle progression, allowing the initiation of replication to be coordinated with the cell cycle and preventing origins from refiring
The precise nucleotide of binding for ORC1 was identified near the start sites for leading-strand DNA synthesis.
HP1 has a role in the recruitment but not in the stable association of Orc1p with heterochromatin
ORC1 in mice is essential for mitotic cell divisions but dispensable for endoreduplication.
mouse Orc1, Orc2, and Orc3 each exist in two alternative-splicing variants and naturally occurring Orc1B lacks a functional domain that is essential for nuclear translocation and proteasome-dependent degradation
The origin recognition complex (ORC) is a highly conserved six subunits protein complex essential for the initiation of the DNA replication in eukaryotic cells. Studies in yeast demonstrated that ORC binds specifically to origins of replication and serves as a platform for the assembly of additional initiation factors such as Cdc6 and Mcm proteins. The protein encoded by this gene is the largest subunit of the ORC complex. While other ORC subunits are stable throughout the cell cycle, the levels of this protein vary during the cell cycle, which has been shown to be controlled by ubiquitin-mediated proteolysis after initiation of DNA replication. This protein is found to be selectively phosphorylated during mitosis. It is also reported to interact with MYST histone acetyltransferase 2 (MyST2/HBO1), a protein involved in control of transcription silencing. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
, origin recognition complex 1
, origin recognition complex subunit 1
, origin recognition complex, subunit 1 homolog
, replication control protein 1
, origin recognition complex protein 1
, origin recognition complex, subunit 1-like