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Information on EC 3.6.4.B8 - clamp-loader complex
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EC Tree
3.6.4.B8 clamp-loader complexSpecify your search results
Word Map
- 3.6.4.B8
- chromatin
-
slide
-
sliding
-
fork
- helicase
- polymerases
- orc1
-
single-stranded
-
mitosis
- rad9
-
pre-replication
-
pre-rcs
- schizosaccharomyces
- pombe
-
s-phase
-
license
-
minichromosome
-
prereplicative
- rpa
-
encircle
- cdt1
-
ring-shaped
- replisome
- heterochromatin
-
firing
- hydroxyurea
-
unwind
-
telomeres
-
primer-template
-
okazaki
-
translesion
- primase
-
mating-type
-
pcna-binding
-
winged-helix
- rad3-related
-
atr-mediated
- mcm3
-
pcna-dependent
- geminin
-
atr-dependent
-
replicases
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chromatin-bound
- dnax
-
atr-chk1
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lagging-strand
-
template-primer
- fen1
-
topbp1
- claspin
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Synonyms
origin recognition complex, rad17, replication factor c, clamp loader, cell cycle checkpoint protein, ctf18-rfc, clamp loader complex, rfc complex, clamp-loader complex, elg1-rfc, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATP-dependent clamp loader complex
clamp loader complex
MacRFC complex
replication factor C
RFC
RFC complex
SsoRFC-complex
clamp loader complex
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O = ADP + phosphate
multisubunit clamp loader complexes use ATP to open sliding clamp rings and place them around the 3' end of primer-template junctions
ATP + H2O = ADP + phosphate
multisubunit clamp loader complexes use ATP to open sliding clamp rings and place them around the 3' end of primer-template junctions
-
-
ATP + H2O = ADP + phosphate
-
-
-
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
ATP + H2O
ADP + phosphate
-
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
-
-
?
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
-
-
?
additional information
?
-
the three gamma or tau subunits are the active ATPases, and each binds one molecule of ATP
-
-
-
additional information
?
-
-
the three gamma or tau subunits are the active ATPases, and each binds one molecule of ATP
-
-
-
additional information
?
-
P35251; P35250; P40938; P35249; P40937
loading of human DNA sliding clamp PCNA (proliferating cell nuclear antigen) by the clamp loader complex RFC
-
-
-
additional information
?
-
-
loading of human DNA sliding clamp PCNA (proliferating cell nuclear antigen) by the clamp loader complex RFC
-
-
-
additional information
?
-
DNA loading substrate of CTF18-RFC is proliferating-cell-nuclear-antigen (PCNA)
-
-
-
additional information
?
-
P35251; P35250; P40938; P35249; P40937
DNA loading substrate of CTF18-RFC is proliferating-cell-nuclear-antigen (PCNA)
-
-
-
additional information
?
-
-
DNA loading substrate of CTF18-RFC is proliferating-cell-nuclear-antigen (PCNA)
-
-
-
additional information
?
-
DNA loading substrate of ELG1-RFC is proliferating-cell-nuclear-antigen (PCNA)
-
-
-
additional information
?
-
P35251; P35250; P40938; P35249; P40937
DNA loading substrate of ELG1-RFC is proliferating-cell-nuclear-antigen (PCNA)
-
-
-
additional information
?
-
-
DNA loading substrate of ELG1-RFC is proliferating-cell-nuclear-antigen (PCNA)
-
-
-
additional information
?
-
P35251; P35250; P40938; P35249; P40937
DNA loading substrate of Rad17 is 9-1-1
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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)
-
-
?
additional information
?
-
-
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)
-
-
?
additional information
?
-
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)
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
-
-
-
?
additional information
?
-
P35251; P35250; P40938; P35249; P40937
loading of human DNA sliding clamp PCNA (proliferating cell nuclear antigen) by the clamp loader complex RFC
-
-
-
additional information
?
-
-
loading of human DNA sliding clamp PCNA (proliferating cell nuclear antigen) by the clamp loader complex RFC
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DNA
ATPase activity is activated by primed DNA templates, such as poly(dA)-oligo(dT). ATPase activity of the SsoRFC-complex is substantially stimulated by the primed homopolymer, whereas no effect is detected in the presence of poly(dA)400. The maximal activation (about tenfold) of the ATP-hydrolyzing activity is measured in the presence of poly(dA)4000-oligo(dT)45 at 140 nM
dsDNA
Q8TSX5; Q8TUC8; Q8TPU4
the MacRFC complex (a protein complex of Mac-RFCS1, MacRFCS2, and MacRFCL) possesses very low intrinsic ATPase activity. This activity is stimulated about 12fold by dsDNA
-
proliferating cell nuclear antigen
Q8TSX5; Q8TUC8; Q8TPU4
the MacRFC complex (a protein complex of Mac-RFCS1, MacRFCS2, and MacRFCL) possesses very low intrinsic ATPase activity. This activity is stimulated about 3fold by Methanosarcina acetivorans proliferating cell nuclear antigen
-
singly primed single-stranded DNA
Q8TSX5; Q8TUC8; Q8TPU4
the MacRFC complex (a protein complex of Mac-RFCS1, MacRFCS2, and MacRFCL) possesses very low intrinsic ATPase activity. This activity is stimulated about 58fold by singly primed single-stranded DNA
-
ssDNA
Q8TSX5; Q8TUC8; Q8TPU4
the MacRFC complex (a protein complex of Mac-RFCS1, MacRFCS2, and MacRFCL) possesses very low intrinsic ATPase activity. This activity is stimulated about 33fold by ssDNA
additional information
P35251; P35250; P40938; P35249; P40937
clamp substrate PCNA proteins are assayed for stimulation of the ATPase activity of the RFC clamp loader complex in the presence of DNA
-
additional information
-
clamp substrate PCNA proteins are assayed for stimulation of the ATPase activity of the RFC clamp loader complex in the presence of DNA
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.025
ATP
O28219; O29072
wild-type enzyme, in the presence of DNA and Proliferating-Cell-Nuclear-Antigen (PCNA), pH and temperature not specified in the publication
additional information
ATP
O28219; O29072
Km-values of mutant replication factor C complexes in the presence of DNA and Proliferating-Cell-Nuclear-Antigen (PCNA)
additional information
ATP
-
Km-values of mutant replication factor C complexes in the presence of DNA and Proliferating-Cell-Nuclear-Antigen (PCNA)
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.7
ATP
O28219; O29072
wild-type enzyme, in the presence of DNA and Proliferating-Cell-Nuclear-Antigen (PCNA), pH and temperature not specified in the publication
additional information
ATP
O28219; O29072
turnover numbers of mutant replication factor C complexes in the presence of DNA and Proliferating-Cell-Nuclear-Antigen (PCNA)
additional information
ATP
-
turnover numbers of mutant replication factor C complexes in the presence of DNA and Proliferating-Cell-Nuclear-Antigen (PCNA)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
O28219: Replication factor C small subunit, O29072: Replication factor C large subunit
O28219; O29072
SwissProt
subunits delta, delta', gamma/tau, chi, and psi
UniProt
genes encoding subunits ORC1-6
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
UniProt
Q8TSX5: Replication factor C small subunit, Q8TUC8: Replication factor C subunit, Q8TPU4: Replication factor C large subunit
Q8TSX5; Q8TUC8; Q8TPU4
-
Q8TSX5: subunit MacRFCS1, Q8TUC8: subunit MacRFCS2, Q8TPU4: subunit MacRFCL
Q8TSX5; Q8TUC8; Q8TPU4
-
Q8TSX5: Replication factor C small subunit, Q8TUC8: Replication factor C subunit, Q8TPU4: Replication factor C large subunit
Q8TSX5; Q8TUC8; Q8TPU4
-
Q8TSX5: subunit MacRFCS1, Q8TUC8: subunit MacRFCS2, Q8TPU4: subunit MacRFCL
Q8TSX5; Q8TUC8; Q8TPU4
-
Q9UXF5: Replication factor C small subunit, Q9UXF6: Replication factor C large subunit
SwissProt
Q9UXF5: Replication factor C small subunit, Q9UXF6: Replication factor C large subunit
SwissProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
ORC molecular defects are observed in Meier-Gorlin syndrome mutations
metabolism
physiological function
additional information
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
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
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). RFCS_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
330
0
37741
Swiss-Prot
-
RFCL_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
405
0
46787
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
Q8TSX5; Q8TUC8; Q8TPU4
1 * 67000 (MacRFCL) + 1 * 38000 (MacRFCS2) + 1 * 35000 (MacRFCS1), SDS-PAGE of His6-tagged subunits
37200
-
1 * 58100, subunit RFC-L, + 4 * 37200, subunit RFC-S, SDS-PAGE
37773
4 * 37773 + 1 * 46787, calculated from sequence
38000
46000
4 * 38000 + 1 * 46000, the homo-tetramer of the small subunit is complexed with one large subunit, SDS-PAGE
46787
4 * 37773 + 1 * 46787, calculated from sequence
58100
-
1 * 58100, subunit RFC-L, + 4 * 37200, subunit RFC-S, SDS-PAGE
67000
Q8TSX5; Q8TUC8; Q8TPU4
1 * 67000 (MacRFCL) + 1 * 38000 (MacRFCS2) + 1 * 35000 (MacRFCS1), SDS-PAGE of His6-tagged subunits
38000
Q8TSX5; Q8TUC8; Q8TPU4
1 * 67000 (MacRFCL) + 1 * 38000 (MacRFCS2) + 1 * 35000 (MacRFCS1), SDS-PAGE of His6-tagged subunits
38000
4 * 38000 + 1 * 46000, the homo-tetramer of the small subunit is complexed with one large subunit, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heptamer
heteropentamer
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
oligomer
pentamer
trimer
additional information
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
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 * 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
-
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
-
additional information
clamp loader complex organization of tau domains, the truncated version gamma comprises domains I-III, overview
additional information
-
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of replication factor C domains 1 and 2 at 2.1 A, crystal structure of replication factor C ADPNP complex at 3.5 A and at 4.0 A, hanging drop vapour diffusion method
O28219; O29072
analysis of crystal structure of mini-delta taken from a structure of the mini-delta:beta-clamp I272A/L273A complex (PDB ID 1JQL) and of the X-ray crystal structures of the gamma clamp loader complex
determination and analysis of the solution structure of the complete seven subunit clamp loader complex using small angle X-ray scattering (SAXS), modeling, detailed overview. The C-terminal regions of the gamma subunits (residues 374-431) are truncated in the crystal structures because of the flexibility of this region
purified recombinant ORC in active form, X-ray diffraction structure determination and analysis at 3.39 A resolution, molecular replacement using the Drosophila melanogaster DmORC4, DmORC5-AAA+ domain and DmORC1-WHD of the DmORC complex as template
Q13415; Q13416; Q9UBD5; O43929; O43913; Q9Y5N6
electron microscopic structure of an archaeal RFC(proliferating cell nuclear antigen)DNA complex at 12 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
R84A/R90A/T120A/K149A
site-directed mutagenesis, quadruple mutant of RFCS small subunit
R84A/R90A/T120A/K149A
-
site-directed mutagenesis, quadruple mutant of RFCS small subunit
-
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
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant clamp loader complex subunits delta, gamma, delta', chi, and psi
recombinant His-tagged mini-delta from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, cleavage of the His tag by thrombin, dialysis, and gel filtration
recombinant replication factor C subunits RFC2, 3, 4, and 5 with mutated truncated subunit RFC1
P35251; P35250; P40938; P35249; P40937
the two SsoRFC polypeptides are coexpressed in Escherichia coli and purified as a complex. The small subunit is individually expressed in Escherichia coli and purified
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of RFCS1Ma and RFCS2Ma as N-terminal His6-tagged proteins
Q8TSX5; Q8TUC8; Q8TPU4
gene holA gene encodes the N-terminal domain (residues 1-140) of the Escherichia coli gamma clamp loader, recombinant His-tagged mini-delta is obtained by expression in Escherichia coli strain BL21(DE3)
recombinant expression of clamp loader complex subunits delta, gamma, delta', chi, and psi
recombinant expression of replication factor C subunits 2, 3, 4, and 5 with mutated truncated subunit RFC1
P35251; P35250; P40938; P35249; P40937
recombinant expression of small subunit RFCS, and full-length enzyme RFCSL in Escherichia coli strain Rosetta(DE3)/pLysS
the two SsoRFC polypeptides are coexpressed in Escherichia coli and purified as a complex. The small subunit is individually expressed in Escherichia coli and purified
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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)
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)
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)
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
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
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)
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
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
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
Tocilj, A.; On, K.F.; Yuan, Z.; Sun, J.; Elkayam, E.; Li, H.; Stillman, B.; Joshua-Tor, L.
Structure of the active form of human origin recognition complex and its ATPase motor module
eLife
6
e20818
2017
Homo sapiens (Q13415 AND Q13416 AND Q9UBD5 AND O43929 AND O43913 AND Q9Y5N6), Homo sapiens
Perumal, S.K.; Xu, X.; Yan, C.; Ivanov, I.; Benkovic, S.J.
Recognition of a key anchor residue by a conserved hydrophobic pocket ensures subunit interface integrity in DNA clamps
J. Mol. Biol.
431
2493-2510
2019
Homo sapiens (P35251 AND P35250 AND P40938 AND P35249 AND P40937), Homo sapiens
Oakley, A.J.
A structural view of bacterial DNA replication
Protein Sci.
28
990-1004
2019
Escherichia coli (P28630 AND P28631 AND P06710 AND P28905 AND P28632), Escherichia coli
Tondnevis, F.; Gillilan, R.E.; Bloom, L.B.; McKenna, R.
Solution study of the Escherichia coli DNA polymerase III clamp loader reveals the location of the dynamic psichi heterodimer
Struct. Dyn.
2
54701
2015
Escherichia coli (P28630 AND P28631 AND P06710 AND P28905 AND P28632), Escherichia coli
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