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ATP + H2O
ADP + phosphate
additional information
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ATP + H2O
ADP + phosphate
O28219; O29072
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
O75943, P35251; P35250; P40938; P35249; P40937 -
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ATP + H2O
ADP + phosphate
P35251; P35250; P40938; P35249; P40937
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ATP + H2O
ADP + phosphate
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
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ATP + H2O
ADP + phosphate
Q8TSX5; Q8TUC8; Q8TPU4
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ATP + H2O
ADP + phosphate
Q8TSX5; Q8TUC8; Q8TPU4
the clamp loader complex reconstituted from the three subunits MacRFCS1, MacRFCS2, and MacRFCL stimulates DNA synthesis by a cognate DNA polymerase in the presence of its sliding clamp. Mac-RFCS1 is critical to the clamp loading activity of the Methanosarcina acetivorans clamp loader
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ATP + H2O
ADP + phosphate
Q8TSX5; Q8TUC8; Q8TPU4
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ATP + H2O
ADP + phosphate
Q8TSX5; Q8TUC8; Q8TPU4
the clamp loader complex reconstituted from the three subunits MacRFCS1, MacRFCS2, and MacRFCL stimulates DNA synthesis by a cognate DNA polymerase in the presence of its sliding clamp. Mac-RFCS1 is critical to the clamp loading activity of the Methanosarcina acetivorans clamp loader
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
ATPase activity is activated by primed DNA templates, such as poly(dA)-oligo(dT). The SsoRFC-complex binds poly(dA)-oligo(dT), but not the unprimed homopolymer
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ATP + H2O
ADP + phosphate
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model of the clamp loading process: ATP-bound replication factor C forms a complex with replication factor C. This results in in-plane opening of a single interface of Proliferating-Cell-Nuclear-Antigen (PCNA) and allowing entry of DNA
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
ATPase activity is activated by primed DNA templates, such as poly(dA)-oligo(dT). The SsoRFC-complex binds poly(dA)-oligo(dT), but not the unprimed homopolymer
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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additional information
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the three gamma or tau subunits are the active ATPases, and each binds one molecule of ATP
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additional information
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the three gamma or tau subunits are the active ATPases, and each binds one molecule of ATP
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additional information
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P35251; P35250; P40938; P35249; P40937
loading of human DNA sliding clamp PCNA (proliferating cell nuclear antigen) by the clamp loader complex RFC
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additional information
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loading of human DNA sliding clamp PCNA (proliferating cell nuclear antigen) by the clamp loader complex RFC
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additional information
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DNA loading substrate of CTF18-RFC is proliferating-cell-nuclear-antigen (PCNA)
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additional information
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P35251; P35250; P40938; P35249; P40937
DNA loading substrate of CTF18-RFC is proliferating-cell-nuclear-antigen (PCNA)
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additional information
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DNA loading substrate of CTF18-RFC is proliferating-cell-nuclear-antigen (PCNA)
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additional information
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DNA loading substrate of ELG1-RFC is proliferating-cell-nuclear-antigen (PCNA)
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additional information
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P35251; P35250; P40938; P35249; P40937
DNA loading substrate of ELG1-RFC is proliferating-cell-nuclear-antigen (PCNA)
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additional information
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DNA loading substrate of ELG1-RFC is proliferating-cell-nuclear-antigen (PCNA)
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additional information
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DNA loading substrate of Rad17 is 9-1-1
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additional information
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P35251; P35250; P40938; P35249; P40937
DNA loading substrate of Rad17 is 9-1-1
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additional information
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DNA loading substrate of Rad17 is 9-1-1
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additional information
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schematic model of substrate proliferating-cell-nuclear-antigen (PCNA) loading by RFC: the homotrimeric ring of PCNA has a head-to-tail configuration of subunits. Substrate PCNA is a hub protein That connects DNA replication and peripheral chromosomal reactions. The ring has asymmetric side surfaces known as the N face and C face. PCNA protomer has two repetitive domains, 1 and 2 that are bridged by IDCL, which is located on the C face. In the presence of ATP, RFC attaches to the C face, opens one interface between the subunits, and binds to the 3' primer-template junction. Upon ATP hydrolysis, the structure of RFC changes to dissociate from PCNA and DNA, leaving a closed PCNA ring that is loaded on the duplex DNA with the C face directed to the 3' end of the primer. Poldelta then binds to the 3' primer end using the C face of PCNA as its docking surface and synthesizes lagging-strand DNA processively. After completion of the DNA elongation, FEN1 and DNA ligase 1 are tethered sequentially to ligate the lagging strands. The dynamic status of PCNA on dsDNA is determined by structural analyses, single-molecule imaging, and molecular-dynamics simulations. PCNA moves along dsDNA in a diffusive fashion in both directions. Most of the time, PCNA tracks rotationally the helical pitch of dsDNA by tilting with the DNA axis. This rotational motion of the tilted PCNA on DNA facilitates formation of a large number of electrostatic interactions between DNA backbone and the positively charged residues lining the PCNA inner surface, and it may provide a structure that captures a proper PCNA-binding partner
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additional information
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P35251; P35250; P40938; P35249; P40937
schematic model of substrate proliferating-cell-nuclear-antigen (PCNA) loading by RFC: the homotrimeric ring of PCNA has a head-to-tail configuration of subunits. Substrate PCNA is a hub protein That connects DNA replication and peripheral chromosomal reactions. The ring has asymmetric side surfaces known as the N face and C face. PCNA protomer has two repetitive domains, 1 and 2 that are bridged by IDCL, which is located on the C face. In the presence of ATP, RFC attaches to the C face, opens one interface between the subunits, and binds to the 3' primer-template junction. Upon ATP hydrolysis, the structure of RFC changes to dissociate from PCNA and DNA, leaving a closed PCNA ring that is loaded on the duplex DNA with the C face directed to the 3' end of the primer. Poldelta then binds to the 3' primer end using the C face of PCNA as its docking surface and synthesizes lagging-strand DNA processively. After completion of the DNA elongation, FEN1 and DNA ligase 1 are tethered sequentially to ligate the lagging strands. The dynamic status of PCNA on dsDNA is determined by structural analyses, single-molecule imaging, and molecular-dynamics simulations. PCNA moves along dsDNA in a diffusive fashion in both directions. Most of the time, PCNA tracks rotationally the helical pitch of dsDNA by tilting with the DNA axis. This rotational motion of the tilted PCNA on DNA facilitates formation of a large number of electrostatic interactions between DNA backbone and the positively charged residues lining the PCNA inner surface, and it may provide a structure that captures a proper PCNA-binding partner
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additional information
?
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schematic model of substrate proliferating-cell-nuclear-antigen (PCNA) loading by RFC: the homotrimeric ring of PCNA has a head-to-tail configuration of subunits. Substrate PCNA is a hub protein That connects DNA replication and peripheral chromosomal reactions. The ring has asymmetric side surfaces known as the N face and C face. PCNA protomer has two repetitive domains, 1 and 2 that are bridged by IDCL, which is located on the C face. In the presence of ATP, RFC attaches to the C face, opens one interface between the subunits, and binds to the 3' primer-template junction. Upon ATP hydrolysis, the structure of RFC changes to dissociate from PCNA and DNA, leaving a closed PCNA ring that is loaded on the duplex DNA with the C face directed to the 3' end of the primer. Poldelta then binds to the 3' primer end using the C face of PCNA as its docking surface and synthesizes lagging-strand DNA processively. After completion of the DNA elongation, FEN1 and DNA ligase 1 are tethered sequentially to ligate the lagging strands. The dynamic status of PCNA on dsDNA is determined by structural analyses, single-molecule imaging, and molecular-dynamics simulations. PCNA moves along dsDNA in a diffusive fashion in both directions. Most of the time, PCNA tracks rotationally the helical pitch of dsDNA by tilting with the DNA axis. This rotational motion of the tilted PCNA on DNA facilitates formation of a large number of electrostatic interactions between DNA backbone and the positively charged residues lining the PCNA inner surface, and it may provide a structure that captures a proper PCNA-binding partner
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additional information
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P35251; P35250; P40938; P35249; P40937
solution dynamics of the substrate human clamp protein in proliferating cell nuclear antigen (PCNA). Computational modeling (molecular dynamic simulations and MM/GBSA binding energy decomposition analyses) is used to identify conserved networks of hydrophobic residues critical for clamp stability and ring-opening dynamics, subunit interface dynamics, substrate structure, detailed overview
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additional information
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solution dynamics of the substrate human clamp protein in proliferating cell nuclear antigen (PCNA). Computational modeling (molecular dynamic simulations and MM/GBSA binding energy decomposition analyses) is used to identify conserved networks of hydrophobic residues critical for clamp stability and ring-opening dynamics, subunit interface dynamics, substrate structure, detailed overview
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additional information
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Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
the ORC motor module displays robust ATPase activity, which is independent of DNA binding, nucleotide-binding site analysis, overview. In the context of the motor module, only the ORC1/4 interface is a functional ATPase. The RecA-fold and lid domains of HsORC1 form a classic ATPase site
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additional information
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the ORC motor module displays robust ATPase activity, which is independent of DNA binding, nucleotide-binding site analysis, overview. In the context of the motor module, only the ORC1/4 interface is a functional ATPase. The RecA-fold and lid domains of HsORC1 form a classic ATPase site
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additional information
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the enzyme stimulates the synthetic activity of Sulfolobus solfataricus B1-type DNA polymerase in reactions containing primed M13mp18 DNA, ATP, and either of the two poliferating cell nuclear antigen-like processivity factors of Sulfolobus solfataricus (039p and 048p)
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additional information
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the enzyme stimulates the synthetic activity of Sulfolobus solfataricus B1-type DNA polymerase in reactions containing primed M13mp18 DNA, ATP, and either of the two poliferating cell nuclear antigen-like processivity factors of Sulfolobus solfataricus (039p and 048p)
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additional information
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the enzyme stimulates the synthetic activity of Sulfolobus solfataricus B1-type DNA polymerase in reactions containing primed M13mp18 DNA, ATP, and either of the two poliferating cell nuclear antigen-like processivity factors of Sulfolobus solfataricus (039p and 048p)
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Adenocarcinoma
Human and mouse homologs of the Schizosaccharomyces pombe rad17+ cell cycle checkpoint control gene.
Ataxia
Ataxia telangiectasia-mutated kinase deficiency exacerbates left ventricular dysfunction and remodeling late after myocardial infarction.
Ataxia
Biallelic expansion of an intronic repeat in RFC1 is a common cause of late-onset ataxia.
Ataxia
Clinical spectrum of the pentanucleotide repeat expansion in the RFC1 gene in ataxia syndromes.
Ataxia
Prevalence of RFC1-mediated spinocerebellar ataxia in a North American ataxia cohort.
Ataxia
Update on Cerebellar Ataxia with Neuropathy and Bilateral Vestibular Areflexia Syndrome (CANVAS).
Ataxia Telangiectasia
Ataxia telangiectasia mutated (ATM) inhibition transforms human mammary gland epithelial cells.
Ataxia Telangiectasia
Ataxia-telangiectasia and Rad3-related and DNA-dependent protein kinase cooperate in G2 checkpoint activation by the DNA strand-breaking nucleoside analogue 2'-C-cyano-2'-deoxy-1-beta-D-arabino-pentofuranosylcytosine.
Ataxia Telangiectasia
Chromatin association of rad17 is required for an ataxia telangiectasia and rad-related kinase-mediated S-phase checkpoint in response to low-dose ultraviolet radiation.
Ataxia Telangiectasia
Deficiency of ataxia telangiectasia mutated kinase modulates cardiac remodeling following myocardial infarction: involvement in fibrosis and apoptosis.
Bilateral Vestibulopathy
Biallelic expansion of an intronic repeat in RFC1 is a common cause of late-onset ataxia.
Bilateral Vestibulopathy
Biallelic RFC1 pentanucleotide repeat expansions in Greek patients with late-onset ataxia.
Bilateral Vestibulopathy
CANVAS: A New Genetic Entity in the Otorhinolaryngologist's Differential Diagnosis.
Bilateral Vestibulopathy
Clinical spectrum of the pentanucleotide repeat expansion in the RFC1 gene in ataxia syndromes.
Bilateral Vestibulopathy
RFC1 AAGGG repeat expansion masquerading as Chronic Idiopathic Axonal Polyneuropathy.
Bilateral Vestibulopathy
RFC1 repeat expansion in Japanese patients with late-onset cerebellar ataxia.
Bloom Syndrome
A novel role for Rad17 in homologous recombination.
Breast Neoplasms
A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins.
Breast Neoplasms
Ataxia telangiectasia mutated (ATM) inhibition transforms human mammary gland epithelial cells.
Breast Neoplasms
Human immunodeficiency virus type 1 Vpr-mediated G2 arrest requires Rad17 and Hus1 and induces nuclear BRCA1 and gamma-H2AX focus formation.
Breast Neoplasms
Regulation of Rad17 protein turnover unveils an impact of Rad17-APC cascade in breast carcinogenesis and treatment.
Breast Neoplasms
Substitution of aspartic acid with glutamic acid at position 67 of the BRCA1 RING domain retains ubiquitin ligase activity and zinc(II) binding with a reduced transition temperature.
Breast Neoplasms
The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by the platinum-based anticancer drugs.
Carcinogenesis
Expression profile and prognostic value of SFN in human ovarian cancer.
Carcinogenesis
LPS promotes HBO1 stability via USP25 to modulate inflammatory gene transcription in THP-1 cells.
Carcinogenesis
Regulation of Rad17 protein turnover unveils an impact of Rad17-APC cascade in breast carcinogenesis and treatment.
Carcinoma
Genetic polymorphism at codon 546 of the human RAD17 contributes to the risk for esophageal squamous cell carcinoma.
Carcinoma
HRad17, a human homologue of the Schizosaccharomyces pombe checkpoint gene rad17, is overexpressed in colon carcinoma.
Carcinoma
Human and mouse homologs of the Schizosaccharomyces pombe rad17+ cell cycle checkpoint control gene.
Carcinoma
The miR-205-5p/BRCA1/RAD17 Axis Promotes Genomic Instability in Head and Neck Squamous Cell Carcinomas.
Carcinoma, Hepatocellular
Exploration of Prognostic Biomarkers among Replication Factor C Family in the Hepatocellular Carcinoma.
Carcinoma, Hepatocellular
Novel candidate biomarkers of origin recognition complex 1, 5 and 6 for survival surveillance in patients with hepatocellular carcinoma.
Carcinoma, Hepatocellular
Nuclear recruitment of A1p145 subunit of replication factor C in the early G1 phase of the cell cycle in Faza 567 hepatoma cell line and hepatocyte primary cultures.
Carcinoma, Non-Small-Cell Lung
Human and mouse homologs of the Schizosaccharomyces pombe rad17+ cell cycle checkpoint control gene.
Carcinoma, Non-Small-Cell Lung
Human Rad17 is phosphorylated upon DNA damage and also overexpressed in primary non-small cell lung cancer tissues.
Carcinoma, Squamous Cell
Human and mouse homologs of the Schizosaccharomyces pombe rad17+ cell cycle checkpoint control gene.
Carcinoma, Squamous Cell
The miR-205-5p/BRCA1/RAD17 Axis Promotes Genomic Instability in Head and Neck Squamous Cell Carcinomas.
Cerebellar Ataxia
Biallelic RFC1 pentanucleotide repeat expansions in Greek patients with late-onset ataxia.
Cerebellar Ataxia
CANVAS: A New Genetic Entity in the Otorhinolaryngologist's Differential Diagnosis.
Cerebellar Ataxia
Clinical spectrum of the pentanucleotide repeat expansion in the RFC1 gene in ataxia syndromes.
Cerebellar Ataxia
RFC1 AAGGG repeat expansion masquerading as Chronic Idiopathic Axonal Polyneuropathy.
Cerebellar Ataxia
RFC1 repeat expansion in Japanese patients with late-onset cerebellar ataxia.
Choriocarcinoma
[Expression of RFC2 and PCNA in different gestational trophoblastic diseases]
Colonic Neoplasms
DNA Replication and Sister Chromatid Cohesion 1 (DSCC1) of the Replication Factor Complex CTF18-RFC is Critical for Colon Cancer Cell Growth.
Colonic Neoplasms
Hrad17 expression in thymoma.
Colonic Neoplasms
Overexpression of Hrad17 gene in non-small cell lung cancers correlated with lymph node metastasis.
Colonic Neoplasms
Overexpression of Krüppel-like factor 4 in the human colon cancer cell line RKO leads to reduced tumorigenecity.
Colorectal Neoplasms
Levels of human replication factor C4, a clamp loader, correlate with tumor progression and predict the prognosis for colorectal cancer.
Colorectal Neoplasms
Mutational and expressional analysis of RFC3, a clamp loader in DNA replication, in gastric and colorectal cancers.
Dwarfism
Mutations in ORC1, encoding the largest subunit of the origin recognition complex, cause microcephalic primordial dwarfism resembling Meier-Gorlin syndrome.
Esophageal Squamous Cell Carcinoma
Genetic polymorphism at codon 546 of the human RAD17 contributes to the risk for esophageal squamous cell carcinoma.
Fanconi Anemia
Cdc5L interacts with ATR and is required for the S-phase cell-cycle checkpoint.
Genetic Diseases, Inborn
Update on Cerebellar Ataxia with Neuropathy and Bilateral Vestibular Areflexia Syndrome (CANVAS).
Gestational Trophoblastic Disease
The second subunit of the replication factor C complex (RFC40) and the regulatory subunit (RIalpha) of protein kinase A form a protein complex promoting cell survival.
Glioblastoma
MicroRNA-744-5p inhibits glioblastoma malignancy by suppressing replication factor C subunit 2.
Glioma
Enhanced radiation-induced cytotoxic effect by 2-ME in glioma cells is mediated by induction of cell cycle arrest and DNA damage via activation of ATM pathways.
Glioma
Forkhead box O1 targeting replication factor C subunit 2 expression promotes glioma temozolomide resistance and survival.
Glioma
Origin recognition complex subunit 1 regulates cell growth and metastasis in glioma by altering activation of ERK and JNK signaling pathway.
Glioma
Targeting multiple pathways in gliomas with stem cell and viral delivered S-TRAIL and Temozolomide.
Head and Neck Neoplasms
Downregulation of RAD17 in head and neck cancer.
Hydatidiform Mole
[Expression of RFC2 and PCNA in different gestational trophoblastic diseases]
Hypersensitivity
hRAD17, a structural homolog of the Schizosaccharomyces pombe RAD17 cell cycle checkpoint gene, stimulates p53 accumulation.
Infections
Efficiency and frequency of translational coupling between the bacteriophage T4 clamp loader genes.
Infections
Pathogenic and apathogenic courses of SIV infection are associated with distinct and characteristic regulatory patterns of G1/S and G2/M cell cycle checkpoints in CD4+ T cells.
Leiomyoma
ORC5L, a new member of the human origin recognition complex, is deleted in uterine leiomyomas and malignant myeloid diseases.
Leukemia
The isolation of a DNA synthesome from human leukemia cells.
Leukemia, Myeloid
Mutation analysis of the origin recognition complex subunit 5 (ORC5L) gene in adult patients with myeloid leukemias exhibiting deletions of chromosome band 7q22.
Leukemia, Myeloid, Acute
Mutation analysis of the origin recognition complex subunit 5 (ORC5L) gene in adult patients with myeloid leukemias exhibiting deletions of chromosome band 7q22.
Lung Neoplasms
Human Rad17 is phosphorylated upon DNA damage and also overexpressed in primary non-small cell lung cancer tissues.
Lung Neoplasms
Identification of RFC5 as a novel potential prognostic biomarker in lung cancer through bioinformatics analysis.
Lung Neoplasms
IQGAP3 interacts with Rad17 to recruit the Mre11-Rad50-Nbs1 complex and contributes to radioresistance in lung cancer.
Lymphoma
ATR-Chk1 signaling pathway and homologous recombinational repair protect cells from 5-fluorouracil cytotoxicity.
Lymphoma
Deleting Ku70 is milder than deleting Ku80 in p53-mutant mice and cells.
Lymphoma
Rad9, Rad17, TopBP1 and claspin play essential roles in heat-induced activation of ATR kinase and heat tolerance.
Lymphoma, B-Cell
WEE1 Inhibition Enhances Anti-Apoptotic Dependency as a Result of Premature Mitotic Entry and DNA Damage.
Lymphoma, Large B-Cell, Diffuse
WEE1 Inhibition Enhances Anti-Apoptotic Dependency as a Result of Premature Mitotic Entry and DNA Damage.
Malaria
Expression and characterization of human malaria parasite Plasmodium falciparum origin recognition complex subunit 1.
Malaria
Functional dissection of the catalytic carboxyl-terminal domain of origin recognition complex subunit 1 (PfORC1) of the human malaria parasite Plasmodium falciparum.
Melanoma
Telomere damage induced by the G-quadruplex ligand RHPS4 has an antitumor effect.
Multiple Endocrine Neoplasia
Adrenergic Differentiation and Ret Expression in Rat Pheochromocytomas.
Myelodysplastic Syndromes
Mutation analysis of the origin recognition complex subunit 5 (ORC5L) gene in adult patients with myeloid leukemias exhibiting deletions of chromosome band 7q22.
Neoplasm Metastasis
DNA Replication and Sister Chromatid Cohesion 1 (DSCC1) of the Replication Factor Complex CTF18-RFC is Critical for Colon Cancer Cell Growth.
Neoplasm Metastasis
Origin recognition complex subunit 1 regulates cell growth and metastasis in glioma by altering activation of ERK and JNK signaling pathway.
Neoplasm Metastasis
RFC2, a direct target of miR-744, modulates the cell cycle and promotes the proliferation of CRC cells.
Neoplasm Metastasis
Up-regulated RFC2 predicts unfavorable progression in hepatocellular carcinoma.
Neoplasm Metastasis
Up-Regulation of RFC3 Promotes Triple Negative Breast Cancer Metastasis and is Associated With Poor Prognosis Via EMT.
Neoplasms
Adrenergic Differentiation and Ret Expression in Rat Pheochromocytomas.
Neoplasms
Atrazine Triggers DNA Damage Response and Induces DNA Double-Strand Breaks in MCF-10A Cells.
Neoplasms
Chemogenetic profiling identifies RAD17 as synthetically lethal with checkpoint kinase inhibition.
Neoplasms
Depletion of RAD17 sensitizes pancreatic cancer cells to gemcitabine.
Neoplasms
DNA damage triggers a prolonged p53-dependent G1 arrest and long-term induction of Cip1 in normal human fibroblasts.
Neoplasms
Downregulation of RAD17 in head and neck cancer.
Neoplasms
Functional identification of tumor-suppressor genes through an in vivo RNA interference screen in a mouse lymphoma model.
Neoplasms
Gain of function mutant p53 proteins cooperate with E2F4 to transcriptionally downregulate RAD17 and BRCA1 gene expression.
Neoplasms
Increased radiosensitivity with chronic hypoxia in four human tumor cell lines.
Neoplasms
Levels of human replication factor C4, a clamp loader, correlate with tumor progression and predict the prognosis for colorectal cancer.
Neoplasms
MicroRNA-744-5p inhibits glioblastoma malignancy by suppressing replication factor C subunit 2.
Neoplasms
Multifaceted regulation and functions of replication factor C family in human cancers.
Neoplasms
Mutation analysis of replicative genes encoding the large subunits of DNA polymerase alpha and replication factors A and C in human sporadic colorectal cancers.
Neoplasms
Mutation of the retinoblastoma tumor suppressor gene sensitizes cancers to mitotic inhibitor induced cell death.
Neoplasms
Nitric oxide, a mediator of inflammation, suppresses tumorigenesis.
Neoplasms
P53 and p21 (Waf1/Cip1) mRNA expression associated with DNA damage and repair in acute immune complex alveolitis in mice.
Neoplasms
Pan-cancer analysis of homozygous deletions in primary tumours uncovers rare tumour suppressors.
Neoplasms
Profiling of genes expressed in human monocytes and monocyte-derived dendritic cells using cDNA expression array.
Neoplasms
Reconstitution of complete SV40 DNA replication with purified replication factors.
Neoplasms
Regulation of RelA (p65) function by the large subunit of replication factor C.
Neoplasms
Replication stress and oxidative damage contribute to aberrant constitutive activation of DNA damage signalling in human gliomas.
Neoplasms
RFC2, a direct target of miR-744, modulates the cell cycle and promotes the proliferation of CRC cells.
Neoplasms
ShRNA-mediated silencing of the RFC3 gene suppress ovarian tumor cells proliferation.
Neoplasms
The human homolog of fission yeast Rad17 is implicated in tumor growth.
Neoplasms
The miR-205-5p/BRCA1/RAD17 Axis Promotes Genomic Instability in Head and Neck Squamous Cell Carcinomas.
Neoplasms
Up-regulated RFC2 predicts unfavorable progression in hepatocellular carcinoma.
Neoplasms
WEE1 Inhibition Enhances Anti-Apoptotic Dependency as a Result of Premature Mitotic Entry and DNA Damage.
Ovarian Neoplasms
Differential hRad17 expression by histologic subtype of ovarian cancer.
Pancreatic Neoplasms
Depletion of RAD17 sensitizes pancreatic cancer cells to gemcitabine.
Pheochromocytoma
Adrenergic Differentiation and Ret Expression in Rat Pheochromocytomas.
Progeria
Replication factor C1, the large subunit of replication factor C, is proteolytically truncated in Hutchinson-Gilford progeria syndrome.
Prostatic Neoplasms
BTF3 confers oncogenic activity in prostate cancer through transcriptional upregulation of Replication Factor C.
Prostatic Neoplasms
The Cell Cycle Checkpoint Gene, RAD17 rs1045051, Is Associated with Prostate Cancer Risk.
Pulmonary Disease, Chronic Obstructive
Age-dependent assessment of genes involved in cellular senescence, telomere and mitochondrial pathways in human lung tissue of smokers, COPD and IPF: Associations with SARS-CoV-2 COVID-19 ACE2-TMPRSS2-Furin-DPP4 axis.
Pulmonary Disease, Chronic Obstructive
Age-Dependent Assessment of Genes Involved in Cellular Senescence, Telomere, and Mitochondrial Pathways in Human Lung Tissue of Smokers, COPD, and IPF: Associations With SARS-CoV-2 COVID-19 ACE2-TMPRSS2-Furin-DPP4 Axis.
Retinoblastoma
Malignant transformation of thyroid follicular cells by galectin-3.
Retinoblastoma
Regulation of RelA (p65) function by the large subunit of replication factor C.
Seminoma
Human and mouse RAD17 genes: identification, localization, genomic structure and histological expression pattern in normal testis and seminoma.
Small Cell Lung Carcinoma
Human and mouse homologs of the Schizosaccharomyces pombe rad17+ cell cycle checkpoint control gene.
Squamous Cell Carcinoma of Head and Neck
Downregulation of RAD17 in head and neck cancer.
Squamous Cell Carcinoma of Head and Neck
Gain of function mutant p53 proteins cooperate with E2F4 to transcriptionally downregulate RAD17 and BRCA1 gene expression.
Squamous Cell Carcinoma of Head and Neck
Human and mouse homologs of the Schizosaccharomyces pombe rad17+ cell cycle checkpoint control gene.
Squamous Cell Carcinoma of Head and Neck
The miR-205-5p/BRCA1/RAD17 Axis Promotes Genomic Instability in Head and Neck Squamous Cell Carcinomas.
Stomach Neoplasms
High-Expression HBO1 Predicts Poor Prognosis in Gastric Cancer.
Williams Syndrome
The gene for replication factor C subunit 2 (RFC2) is within the 7q11.23 Williams syndrome deletion.
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malfunction
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
ORC molecular defects are observed in Meier-Gorlin syndrome mutations
evolution
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most archaeal genomes also encode two RFC homologs, designated the RFC large (RFC-L) and small (RFC-S) subunits, that assemble to form a pentameric complex that contains one RFC-L and four RFC-S subunits
evolution
the clamp loader complex is a member of the AAA+ family of ATPases (adenosine 5'-triphosphatases)
evolution
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
the enzyme complex belongs to the AAA+ ATPase family. The complex is composed of an ORC1/4/5 motor module lobe in an organization reminiscent of the DNA polymerase clamp loader complexes. The structure of HsORC reveals a remarkable similarity between two very different ATPases: the replication initiator ORC-CDC6 ATPase and the replication fork DNA polymerase clamp loader. Both ATPases function at different times during genome replication but load ring-shaped proteins onto double-stranded DNA so that the ring-shaped proteins become topologically linked to the DNA double helix. The ATPase motor module of HsORC is very reminiscent of the DNA polymerase clamp loader complexes such as replication factor C (RFC) in eukaryotes, the bacterial gamma-complex, and the T4 bacteriophage Gene44 clamp loader
evolution
O75943, P35251; P35250; P40938; P35249; P40937 three RFC1 paralogues - RAD17, CTF18 (chromosome transmission fidelity 18), and ELG1 (enhanced level of genome instability 1, in human also called ATAD5, ATPase family, AAA domain containing 5 or FRAG1, FGF receptor activating protein 1) - have been identified in eukaryotes. Furthermore, three proteins that share significant amino acid sequence similarities with PCNA (RAD9, RAD1, and HUS1) are necessary for the checkpoint-response pathway, along with RAD17-RFC
evolution
-
most archaeal genomes also encode two RFC homologs, designated the RFC large (RFC-L) and small (RFC-S) subunits, that assemble to form a pentameric complex that contains one RFC-L and four RFC-S subunits
-
metabolism
O75943, P35251; P35250; P40938; P35249; P40937 Poldelta alone can only incorporate several nucleotides at the primer end, whereas in the presence of proliferating cell nuclear antigen (PCNA), it can produce DNA strands longer than 200-300 nucleotides. The PCNA-RFC-Poldelta system can efficiently fill DNA gaps from short patches to lagging-strand sizes
metabolism
O75943, P35251; P35250; P40938; P35249; P40937 Poldelta alone can only incorporate several nucleotides at the primer end, whereas in the presence of proliferating cell nuclear antigen (PCNA), it can produce DNA strands longer than 200-300 nucleotides. The PCNA-RFC-Poldelta system can efficiently fill DNA gaps from short patches to lagging-strand sizes. Physiological functions and dynamics of proliferating-cell-nuclear-antigen (PCNA), overview
physiological function
-
sliding clamps play central roles in a broad range of DNA replication and repair processes. The clamps form circular molecules that must be opened and resealed around DNA by the clamp loader complex to fulfil their function
physiological function
-
proliferating cell nuclear antigen (PCNA) monomers assemble to form a ring-shaped clamp complex that encircles duplex DNA. PCNA binding to other proteins tethers them to the DNA providing contacts and interactions for many other enzymes essential for DNA metabolic processes. The PCNA clamp does not assemble autonomously but is loaded onto DNA by the replication factor C (RFC) clamp loader complex. RFC recognizes the 3' end of a single-strand/duplex DNA (primer-template) junction and uses the energy of ATP hydrolysis to assemble the PCNA ring around the primer. Primer extension by PolB is completely dependent on the presence of RFC plus either PCNA1 or PCNA2, and the rate of DNA synthesis increases when the PCNA1 or PCNA2 concentration is increased
physiological function
RFC is an ATPase. The RFC complex from Sulfolobus solfataricus physically interacts with DNA polymerase B1 (PolB1) and enhances both the polymerase and 3'-5' exonuclease activities of PolB1 in an ATP-independent manner. Stimulation of the PolB1 activity by RFC is independent of the ability of RFC to bind DNA but is consistent with the ability of RFC to facilitate DNA binding by PolB1 through protein-protein interaction. Sulfolobus RFC may play a role in recruiting DNA polymerase for efficient primer extension, in addition to clamp loading, during DNA replication. RFC is shown to interact with the PCNA1 and PCNA2 subunits through its small subunit RFCS and with PCNA3 through its large subunit RFCL
physiological function
O75943, P35251; P35250; P40938; P35249; P40937 functions of multiple clamp and clamp-loader complexes in eukaryotic DNA replication, detailed overview. Eukaryotes have multiple paralogues of sliding clamp, PCNA and its loader, RFC. Another alternative loader complex, CTF18-RFC, has a role that is distinguishable from the role of the canonical loader, RFC. CTF18-RFC interacts with one of the replicative DNA polymerases, Polepsilon, and loads PCNA onto leading-strand DNA. In the progression of S phase, the alternative PCNA loader maintains appropriate amounts of PCNA on the replicating sister DNAs to ensure that specific enzymes are tethered at specific chromosomal locations
physiological function
O75943, P35251; P35250; P40938; P35249; P40937 functions of multiple clamp and clamp-loader complexes in eukaryotic DNA replication, detailed overview. Eukaryotes have multiple paralogues of sliding clamp, PCNA and its loader, RFC. Another alternative loader complex, ELG1-RFC, has a role that is distinguishable from the role of the canonical loader, RFC. ELG1-RFC unloads PCNA after ligation of lagging-strand DNA. In the progression of S phase, the alternative PCNA loader maintains appropriate amounts of PCNA on the replicating sister DNAs to ensure that specific enzymes are tethered at specific chromosomal locations
physiological function
O75943, P35251; P35250; P40938; P35249; P40937 functions of multiple clamp and clamp-loader complexes in eukaryotic DNA replication, detailed overview. Eukaryotes have multiple paralogues of sliding clamp, PCNA and its loader, RFC. CTF18-RFC interacts with one of the replicative DNA polymerases, Polapsilon, and loads PCNA onto leading-strand DNA, and ELG1-RFC unloads PCNA after ligation of lagging-strand DNA. In the progression of S phase, these alternative PCNA loaders maintain appropriate amounts of PCNA on the replicating sister DNAs to ensure that specific enzymes are tethered at specific chromosomal locations
physiological function
O75943, P35251; P35250; P40938; P35249; P40937 functions of multiple clamp and clamp-loader complexes in eukaryotic DNA replication, detailed overview. Eukaryotes have multiple paralogues of sliding clamp, PCNA and its loader, RFC. The proliferating cell nuclear antigen (PCNA) paralogues, RAD9, HUS1, and RAD1 form the heterotrimeric 9-1-1 ring that is similar to the PCNA homotrimeric ring, and the 9-1-1 clamp complex is loaded onto sites of DNA damage by its specific loader RAD17-RFC. This alternative clamp-loader system transmits DNA-damage signals in genomic DNA to the checkpoint-activation network and the DNA-repair apparatus. Human Rad17 lacks the DNA binding domain compared to human RFC1. It acts as a cell cycle checkpoint protein, RAD17-RFC performs loading of the 9-1-1 clamp onto DNA. 9-1-1 and RAD17-RFC are involved in ATR activation, but are not required for phosphorylation of CHK2, a mediator kinase of the ATM pathway for response to double-strand breaks. Physiological functions of protein 9-1-1
physiological function
P35251; P35250; P40938; P35249; P40937
sliding clamp proteins encircle duplex DNA and are involved in processive DNA replication and the DNA damage response. Clamp proteins are ring-shaped oligomers (dimers or trimers) and are loaded onto DNA by an ATP-dependent clamp loader complex that ruptures the interface between two adjacent subunits. The hydrophobic network is shared among clamp proteins and exhibits a key in a keyhole pattern where a bulky aromatic residue from one clamp subunit is anchored into a hydrophobic pocket of the opposing subunit. Bioinformatics and dynamic network analyses show that this oligomeric latch is conserved across DNA sliding clamps from all domains of life and dictates the dynamics of clamp opening and closing
physiological function
sliding clamps are actively loaded onto primed template DNA by ATP-dependent clamp loader complexes. The complex of chi and psi enzyme complex subunits plays an important role in the processivity of Okazaki fragment synthesis
physiological function
the beta-clamp protein and the gamma clamp loader complex are essential components of bacterial DNA replication machinery. The beta-clamp is a ring-shaped homodimer that encircles DNA and increases the efficiency of replication by providing a binding platform for DNA polymerases and other replication-related proteins. The beta-clamp is loaded onto DNA by the five-subunit gamma clamp loader complex in a multi-step ATP-dependent process. The initial steps of this process involve the cooperative binding of the beta-clamp by the five subunits of ATP-bound clamp loader, which induces or traps an open conformation of the clamp. The delta subunit of the Escherichia coli clamp loader, or even its 140 residue N-terminal domain (called mini-delta), alone can shift conformational equilibrium of the beta-clamp towards the open state
physiological function
the clamp loader utilizes ATP binding and hydrolysis to load the sliding clamp onto the DNA at the primer template junction
physiological function
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
the first step in genome replication, the binding of the origin recognition complex (ORC) at origins of DNA replication, triggers a series of highly coordinated steps leading to the assembly of pre-replicative complexes (pre-RCs) in a process that involves CDC6 binding to ORC. ORC and CDC6 then function as an ATP-dependent assembler that first recruits a ring-shaped MCM2-7 hexamer with bound Cdt1 to DNA, and then loads a second MCM2-7 hexamer in a head-to-head orientation, whereby this double hexamer is topologically linked to double-stranded DNA. The enzyme complex loads ring-shaped proteins onto double-stranded DNA so that the ring-shaped proteins become topologically linked to the DNA double helix
physiological function
-
RFC is an ATPase. The RFC complex from Sulfolobus solfataricus physically interacts with DNA polymerase B1 (PolB1) and enhances both the polymerase and 3'-5' exonuclease activities of PolB1 in an ATP-independent manner. Stimulation of the PolB1 activity by RFC is independent of the ability of RFC to bind DNA but is consistent with the ability of RFC to facilitate DNA binding by PolB1 through protein-protein interaction. Sulfolobus RFC may play a role in recruiting DNA polymerase for efficient primer extension, in addition to clamp loading, during DNA replication. RFC is shown to interact with the PCNA1 and PCNA2 subunits through its small subunit RFCS and with PCNA3 through its large subunit RFCL
-
physiological function
-
proliferating cell nuclear antigen (PCNA) monomers assemble to form a ring-shaped clamp complex that encircles duplex DNA. PCNA binding to other proteins tethers them to the DNA providing contacts and interactions for many other enzymes essential for DNA metabolic processes. The PCNA clamp does not assemble autonomously but is loaded onto DNA by the replication factor C (RFC) clamp loader complex. RFC recognizes the 3' end of a single-strand/duplex DNA (primer-template) junction and uses the energy of ATP hydrolysis to assemble the PCNA ring around the primer. Primer extension by PolB is completely dependent on the presence of RFC plus either PCNA1 or PCNA2, and the rate of DNA synthesis increases when the PCNA1 or PCNA2 concentration is increased
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additional information
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
determination and analysis of the structure of human ORC (HsORC motor module) in a functionally active, ATP-hydrolysis ready state, providing insight into ATP-dependent protein loading as well as DNA and CDC6 binding, structure-function relationship, overview. In the context of the motor module, only the ORC1/4 interface is a functional ATPase. Binding of ORC2-ORC3 modulates the ATPase activity of the ORC motor
additional information
-
determination and analysis of the structure of human ORC (HsORC motor module) in a functionally active, ATP-hydrolysis ready state, providing insight into ATP-dependent protein loading as well as DNA and CDC6 binding, structure-function relationship, overview. In the context of the motor module, only the ORC1/4 interface is a functional ATPase. Binding of ORC2-ORC3 modulates the ATPase activity of the ORC motor
additional information
Escherichia coli clamp loader complex is comprised of seven subunits, each of these has critical roles in the function of the clamp loader. Determination and analysis of the solution structure of the complete seven subunit clamp loader complex using small angle X-ray scattering, model of the dynamic nature of the clamp loader complex, overview
additional information
-
Escherichia coli clamp loader complex is comprised of seven subunits, each of these has critical roles in the function of the clamp loader. Determination and analysis of the solution structure of the complete seven subunit clamp loader complex using small angle X-ray scattering, model of the dynamic nature of the clamp loader complex, overview
additional information
mechanism of primary PCNA and 9-1-1 loading and unloading by RFC and homologues, secondary PCNA loading by CTF18-RFC, unloading by ELG1-RFC, detailed overview. DNA-sequence-specific PCNA loading occurs via interaction of RFC with a sequence-specific DNA-binding protein
additional information
P35251; P35250; P40938; P35249; P40937
mechanism of primary PCNA and 9-1-1 loading and unloading by RFC and homologues, secondary PCNA loading by CTF18-RFC, unloading by ELG1-RFC, detailed overview. DNA-sequence-specific PCNA loading occurs via interaction of RFC with a sequence-specific DNA-binding protein
additional information
-
mechanism of primary PCNA and 9-1-1 loading and unloading by RFC and homologues, secondary PCNA loading by CTF18-RFC, unloading by ELG1-RFC, detailed overview. DNA-sequence-specific PCNA loading occurs via interaction of RFC with a sequence-specific DNA-binding protein
additional information
mechanism of primary PCNA loading and unloading by RFC and of 9-1-1 by Rad17, secondary PCNA loading by CTF18-RFC, unloading by ELG1-RFC, detailed overview. DNA-sequence-specific PCNA loading occurs via interaction of RFC with a sequence-specific DNA-binding protein
additional information
P35251; P35250; P40938; P35249; P40937
mechanism of primary PCNA loading and unloading by RFC and of 9-1-1 by Rad17, secondary PCNA loading by CTF18-RFC, unloading by ELG1-RFC, detailed overview. DNA-sequence-specific PCNA loading occurs via interaction of RFC with a sequence-specific DNA-binding protein
additional information
-
mechanism of primary PCNA loading and unloading by RFC and of 9-1-1 by Rad17, secondary PCNA loading by CTF18-RFC, unloading by ELG1-RFC, detailed overview. DNA-sequence-specific PCNA loading occurs via interaction of RFC with a sequence-specific DNA-binding protein
additional information
structure of Escherichia coli clamp loader complex CLC in complex with primed template DNA (PDB ID 3GLI). The chi and psi subunits serve to link the clamp loader complex and ssDNA binding protein SSB, with chi binding to SSB. Through its interaction with the CLC and SSB, the chi-psi complex plays an important role in the processivity of Okazaki fragment synthesis. Folds of chi and psi are similar to mononucleotide and dinucleotide binding proteins, respectively
additional information
-
structure of Escherichia coli clamp loader complex CLC in complex with primed template DNA (PDB ID 3GLI). The chi and psi subunits serve to link the clamp loader complex and ssDNA binding protein SSB, with chi binding to SSB. Through its interaction with the CLC and SSB, the chi-psi complex plays an important role in the processivity of Okazaki fragment synthesis. Folds of chi and psi are similar to mononucleotide and dinucleotide binding proteins, respectively
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hexamer
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
the enzyme complex is organized as a double-layered shallow corkscrew, with the AAA+ and AAA+-like domains forming one layer, and the winged-helix domains (WHDs) forming a top layer. CDC6 fits easily between ORC1 and ORC2, completing the ring and the DNA-binding channel, forming an additional ATP hydrolysis site. The overall architecture of the HsORC motor module resembles a cashew nut. Each ORC subunit is comprised of three domains: the RecA-fold, the alpha-helical lid and the alpha-helical winged-helix domain (WHD), although the WHD domain is truncated in ORC5. The RecA-fold domain and the lid together constitute the well-known AAA+ domain. The three RecA domains form a semicircle with ATP nucleotides wedged between them in a classic AAA+ oligomerization arrangement. In the context of the motor module, only the ORC1/4 interface is a functional ATPase. SUbunit HsCDC6 binds to the core of HsORC as a second step in the assembly of the pre-RC. It is also an AAA+ ATPase with 29% sequence identity to ORC1, and completes the ring structure
heptamer
determination and analysis of the solution structure of the complete seven subunit clamp loader complex using small angle X-ray scattering, modeling, detailed overview. The Escherichia coli core clamp loader contains the five core (delta', delta, and three truncated gamma or tau) subunits, and additionally the psi and chi subunits. The delta subunit is responsible for clamp binding and opening. The d' subunit acts as a stator and stabilizes the interaction of d subunit with the sliding clamp. The tau and gamma subunits are the active ATPases, and both gamma and tau are products of the dnaX gene. The tau and gamma clamp loading function is interchangeable and the major difference is in the length of the two proteins: gamma is a shorter version of s subunits that is created by a translational frame shift. Each DnaX subunit (either tau or gamma) binds one molecule of ATP, and the clamp loader binds and hydrolyses three ATP molecules for each loading cycle. The Escherichia coli clamp loader complex contains two other subunits psi and chi. These two subunits form a tight 1:1 elongated heterodimeric complex. The psi subunit interacts with the C-terminal region of gamma subunit. These two subunits are essential for bridging the interaction between the clamp loader and single strand DNA binding protein (SSB) in Escherichia coli. The psi subunit plays a role in stabilizing the conformational changes induced by ATP binding, the chi subunit directly interacts with the C-terminus of SSB (8 amino acid residues), and the interaction of SSB with chi subunit is increased thousand of folds when SSB is bound to DNA. The chipsi complex also plays a role in increasing the affinity of tau and gamma for delta/delta' to a physiologically relevant range
heptamer
the Escherichia coli clamp loader complex CLC comprises seven subunits: delta, tau_n, gamma(3-n), delta', psi, and chi. The delta and delta' subunits (encoded by holA and holB) together with three copies of gamma and/or tau (encoded by dnaX) form a heteropentamer. The chi and psi subunits (encoded by holC and holD) are not required for clamp-loading activity, but serve to bridge the CLC with single-stranded DNA (ssDNA)-binding protein (SSB). The gamma subunit is a truncated (residues 1-431) form of tau (residues 1-643) resulting from a programmed frameshift during translation of dnaX mRNA. Enzyme pentameric and heptameric complex structures with bound DNA or SSB and without, overview. The pentameric deltagamma3delta' complex in the apo, ADP-, or ATP-gammaS-bound states are nearly identical
heteropentamer
-
heteropentamer
4 * 37773 + 1 * 46787, calculated from sequence
heteropentamer
4 * 38000 + 1 * 46000, the homo-tetramer of the small subunit is complexed with one large subunit, SDS-PAGE
heteropentamer
-
4 * 37773 + 1 * 46787, calculated from sequence
-
heteropentamer
-
4 * 38000 + 1 * 46000, the homo-tetramer of the small subunit is complexed with one large subunit, SDS-PAGE
-
oligomer
O28219; O29072
communication between subunits in the RFC holoenzyme is investigated. The small subunit alone forms a hexameric ring that is six-fold symmetric in the absence of ATP. This symmetry is broken when the nucleotide is bound to the complex. The large conformational change observed may relate to the opening of PCNA rings that is required for them to be loaded onto DNA substrates
oligomer
Q8TSX5; Q8TUC8; Q8TPU4
Methanosarcina acetivorans clamp loader comprises two different small subunits (RFCS1 and RFCS2) and a large subunit (RFCL). RFCS1, RFCS2, and RFCL form a stable complex with a stoichiometric ratio of 3:1:1
oligomer
-
Methanosarcina acetivorans clamp loader comprises two different small subunits (RFCS1 and RFCS2) and a large subunit (RFCL). RFCS1, RFCS2, and RFCL form a stable complex with a stoichiometric ratio of 3:1:1
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pentamer
P35251; P35250; P40938; P35249; P40937
5 RFC subunits 1-5
pentamer
-
1 * 58100, subunit RFC-L, + 4 * 37200, subunit RFC-S, SDS-PAGE
pentamer
-
1 * 58100, subunit RFC-L, + 4 * 37200, subunit RFC-S, SDS-PAGE
-
trimer
Q8TSX5; Q8TUC8; Q8TPU4
1 * 67000 (MacRFCL) + 1 * 38000 (MacRFCS2) + 1 * 35000 (MacRFCS1), SDS-PAGE of His6-tagged subunits
trimer
-
1 * 67000 (MacRFCL) + 1 * 38000 (MacRFCS2) + 1 * 35000 (MacRFCS1), SDS-PAGE of His6-tagged subunits
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additional information
clamp loader complex organization of tau domains, the truncated version gamma comprises domains I-III, overview
additional information
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clamp loader complex organization of tau domains, the truncated version gamma comprises domains I-III, overview
additional information
NMR resonance assignments for the N-terminal domain of the delta subunit of the gamma clamp loader complex. Nearly complete backbone and side-chain 1H, 13C and 15N NMR resonance assignments of mini-delta will facilitate NMR studies of the mechanisms of beta-clamp opening and its loading on DNA by the clamp loader
additional information
-
NMR resonance assignments for the N-terminal domain of the delta subunit of the gamma clamp loader complex. Nearly complete backbone and side-chain 1H, 13C and 15N NMR resonance assignments of mini-delta will facilitate NMR studies of the mechanisms of beta-clamp opening and its loading on DNA by the clamp loader
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D125A
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
site-directed mutagenesis of subunit ORC5 at the ATP-binding site
D159A
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
site-directed mutagenesis of subunit ORC4 at the ATP-binding site. The mutation of the ORC4 Walker-B motif has little effect on ATPase activity
D620A
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
site-directed mutagenesis of subunit ORC1 at the ATP-binding site. Disrupting the ORC1 Walker-B motif effectively abolishes ATPase activity
D620A/D159A
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
site-directed mutagenesis of subunits ORC1 and ORC4 at the ATP-binding site. The double mutation of the Walker-B motif of both ORC1 and ORC4 abolishes activity
R261Q
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
site-directed mutagenesis of subunit ORC3 at the ATP-binding site
R69V
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
site-directed mutagenesis of subunit ORC4 at the ATP-binding site
R720Q
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
site-directed mutagenesis of subunit ORC1 at the ATP-binding site. The mutation abolishes ATPase activity of the motor module, and this mutation exists in a single heterozygous individual with a wild-type allele
R98Q
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
site-directed mutagenesis of subunit ORC3 at the ATP-binding site
Y174C
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
site-directed mutagenesis of subunit ORC4 at the ATP-binding site. The ORC4-Y174C mutation in the ORC4 tether, which disrupts its hydrogen bond to an ORC1 Walker-B side chain (ORC1-E621), renders the motor module hyperactive for ATPase activity. The ORC4 MGS mutant Y174C has reduced activity (at about 50% of wild-type) in the context of ORC1-5. The hyperactivity of this mutant observed in the context of the motor module alone suggests that binding of ORC2-ORC3 modulates the ATPase activity of the ORC motor
R84A/R90A/T120A/K149A
site-directed mutagenesis, quadruple mutant of RFCS small subunit
R84A/R90A/T120A/K149A
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site-directed mutagenesis, quadruple mutant of RFCS small subunit
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additional information
O28219; O29072
mutation of the proposed arginine finger in the small subunits results in a complex that can still bind ATP but has impaired clamp-loading activity
additional information
-
mutation of the proposed arginine finger in the small subunits results in a complex that can still bind ATP but has impaired clamp-loading activity
additional information
P35251; P35250; P40938; P35249; P40937
deletion of its N-terminal DNA binding domain does not affect the activity of the wild-type RFC complex, leading to generate a truncated RFC1DELTA555 construct, that is easier to purify in the RFC pentamer
additional information
-
deletion of its N-terminal DNA binding domain does not affect the activity of the wild-type RFC complex, leading to generate a truncated RFC1DELTA555 construct, that is easier to purify in the RFC pentamer
additional information
Q8TSX5; Q8TUC8; Q8TPU4
site-directed mutagenesis in the Walker A and SRC motifs is performed to examine the contribution of each subunit to the function of the Methanosarcina acetivorans clamp loader. Mutations in the large subunit MacRFCL and the small subunit MacRFCS2 do not impair clamp loading activity. Any mutant clamp loader harboring a mutation in MacRFCS1 is devoid of the clamp loading property
additional information
-
site-directed mutagenesis in the Walker A and SRC motifs is performed to examine the contribution of each subunit to the function of the Methanosarcina acetivorans clamp loader. Mutations in the large subunit MacRFCL and the small subunit MacRFCS2 do not impair clamp loading activity. Any mutant clamp loader harboring a mutation in MacRFCS1 is devoid of the clamp loading property
additional information
-
site-directed mutagenesis in the Walker A and SRC motifs is performed to examine the contribution of each subunit to the function of the Methanosarcina acetivorans clamp loader. Mutations in the large subunit MacRFCL and the small subunit MacRFCS2 do not impair clamp loading activity. Any mutant clamp loader harboring a mutation in MacRFCS1 is devoid of the clamp loading property
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Seybert, A.; Singleton, M.R.; Cook, N.; Hall, D.R.; Wigley, D.B.
Communication between subunits within an archaeal clamp-loader complex
EMBO J.
25
2209-2218
2006
Archaeoglobus fulgidus (O28219 and O29072), Archaeoglobus fulgidus
brenda
Chen, Y.H.; Lin, Y.; Yoshinaga, A.; Chhotani, B.; Lorenzini, J.L.; Crofts, A.A.; Mei, S.; Mackie, R.I.; Ishino, Y.; Cann, I.K.
Molecular analyses of a three-subunit euryarchaeal clamp loader complex from Methanosarcina acetivorans
J. Bacteriol.
191
6539-6549
2009
Methanosarcina acetivorans (Q8TSX5 and Q8TUC8 and Q8TPU4), Methanosarcina acetivorans, Methanosarcina acetivorans DSM 2834 (Q8TSX5 and Q8TUC8 and Q8TPU4)
brenda
Chen, Y.H.; Kocherginskaya, S.A.; Lin, Y.; Sriratana, B.; Lagunas, A.M.; Robbins, J.B.; Mackie, R.I.; Cann, I.K.
Biochemical and mutational analyses of a unique clamp loader complex in the archaeon Methanosarcina acetivorans
J. Biol. Chem.
280
41852-41863
2005
Methanosarcina acetivorans (Q8TSX5 and Q8TUC8 and Q8TPU4), Methanosarcina acetivorans, Methanosarcina acetivorans DSM 2834 (Q8TSX5 and Q8TUC8 and Q8TPU4)
brenda
Pisani, F.M.; De Felice, M.; Carpentieri, F.; Rossi, M.
Biochemical characterization of a clamp-loader complex homologous to eukaryotic replication factor C from the hyperthermophilic archaeon Sulfolobus solfataricus
J. Mol. Biol.
301
61-73
2000
Saccharolobus solfataricus (Q9UXF5 and Q9UXF6), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q9UXF5 and Q9UXF6)
brenda
Dionne, I.; Brown, N.J.; Woodgate, R.; Bell, S.D.
On the mechanism of loading the PCNA sliding clamp by RFC
Mol. Microbiol.
68
216-222
2008
Saccharolobus solfataricus
brenda
Miyata, T.; Suzuki, H.; Oyama, T.; Mayanagi, K.; Ishino, Y.; Morikawa, K.
Open clamp structure in the clamp-loading complex visualized by electron microscopic image analysis
Proc. Natl. Acad. Sci. USA
102
13795-13800
2005
Pyrococcus furiosus
brenda
Xing, X.; Zhang, L.; Guo, L.; She, Q.; Huang, L.
Sulfolobus replication factor C stimulates the activity of DNA polymerase B1
J. Bacteriol.
196
2367-2375
2014
Saccharolobus solfataricus (Q9UXF5), Saccharolobus solfataricus (Q9UXF6), Saccharolobus solfataricus P2 (Q9UXF5), Saccharolobus solfataricus P2 (Q9UXF6)
brenda
Pan, M.; Santangelo, T.J.; Cubonova, L.; Li, Z.; Metangmo, H.; Ladner, J.; Hurwitz, J.; Reeve, J.N.; Kelman, Z.
Thermococcus kodakarensis has two functional PCNA homologs but only one is required for viability
Extremophiles
17
453-461
2013
Thermococcus kodakarensis, Thermococcus kodakarensis KW128
brenda
Ohashi, E.; Tsurimoto, T.
Functions of multiple clamp and clamp-loader complexes in eukaryotic DNA replication
Adv. Exp. Med. Biol.
1042
135-162
2017
Homo sapiens (O75943), Homo sapiens (P35251 AND P35250 AND P40938 AND P35249 AND P40937), Homo sapiens
brenda
Alyami, E.M.; Rizzo, A.A.; Beuning, P.J.; Korzhnev, D.M.
NMR resonance assignments for the N-terminal domain of the delta subunit of the E. coli gamma clamp loader complex
Biomol. NMR Assign.
11
169-173
2017
Escherichia coli (P28630 AND P28631 AND P06710 AND P28905 AND P28632), Escherichia coli
brenda
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