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Volumn 7, Issue 10, 2006, Pages 751-761

The replication clamp-loading machine at work in the three domains of life

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DNA POLYMERASE; MULTIPROTEIN COMPLEX;

EID: 33749033347     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm2022     Document Type: Review
Times cited : (155)

References (127)
  • 1
    • 22244478079 scopus 로고    scopus 로고
    • Cellular DNA replicases: Components and dynamics at the replication fork
    • Johnson, A. & O'Donnell, M. Cellular DNA replicases: components and dynamics at the replication fork. Annu. Rev. Biochem.74, 283-315 (2005).
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 283-315
    • Johnson, A.1    O'Donnell, M.2
  • 2
    • 0031663505 scopus 로고    scopus 로고
    • The DNA replication fork in eukaryotic cells
    • Waga, S. & Stillman, B. The DNA replication fork in eukaryotic cells. Annu. Rev. Biochem. 67, 721-751 (1998).
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 721-751
    • Waga, S.1    Stillman, B.2
  • 3
    • 0033777562 scopus 로고    scopus 로고
    • The puzzle of PCNA's many partners
    • Warbrick, E. The puzzle of PCNA's many partners. Bioessays 22, 997-1006 (2000).
    • (2000) Bioessays , vol.22 , pp. 997-1006
    • Warbrick, E.1
  • 4
    • 25444480278 scopus 로고    scopus 로고
    • Open clamp structure in the clamp-loading complex visualized by electron microscopic image analysis
    • Miyata, T. et al. Open clamp structure in the clamp-loading complex visualized by electron microscopic image analysis. Proc. Natl Acad. Sci. USA 102, 13795-13800 (2005). The EM structure of an archaeal RFC-PCNA-DNA complex in the presence of ATPaS shows the clamp in an open state. The open PCNA has a lock-washer conformation and fits onto the AAA+ surface of RFC. Density that probably corresponds to DNA is observed in the centre of PCNA and in the central chamber of RFC. The complex might represent an intermediate in which PCNA is kept open before ATP hydrolysis by RFC.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 13795-13800
    • Miyata, T.1
  • 5
    • 3042588011 scopus 로고    scopus 로고
    • Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex
    • Bowman, G. D., O'Donnell, M. & Kuriyan, J. Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex. Nature 429, 724-730 (2004). The S. cerevisiae RFC-PCNA-ATPγS structure indicates a mechanism for DNA engagement by the AAA+ clamp-loader assembly. The ATPase domains of RFC are arranged in a right-handed spiral that complements the structure of dsDNA modelled inside. The PCNA lies below the RFC spiral in a closed conformation, which indicates that ring closure might precede hydrolysis of ATP.
    • (2004) Nature , vol.429 , pp. 724-730
    • Bowman, G.D.1    O'Donnell, M.2    Kuriyan, J.3
  • 6
    • 0035943342 scopus 로고    scopus 로고
    • Crystal structure of the processivity clamp loader gamma (γ) complex of E. coli DNA polymerase III
    • Jeruzalmi, D., O'Donnell, M. & Kuriyan, J. Crystal structure of the processivity clamp loader gamma (γ) complex of E. coli DNA polymerase III. Cell 106, 429-441 (2001).
    • (2001) Cell , vol.106 , pp. 429-441
    • Jeruzalmi, D.1    O'Donnell, M.2    Kuriyan, J.3
  • 7
    • 0035943399 scopus 로고    scopus 로고
    • Mechanism of processivity clamp opening by the δ subunit wrench of the clamp loader complex of E. coli DNA polymerase III
    • Jeruzalmi, D. et al. Mechanism of processivity clamp opening by the δ subunit wrench of the clamp loader complex of E. coli DNA polymerase III. Cell 106, 417-428 (2001).
    • (2001) Cell , vol.106 , pp. 417-428
    • Jeruzalmi, D.1
  • 8
    • 0035179213 scopus 로고    scopus 로고
    • Intricacies in ATP-dependent clamp loading: Variations across replication systems
    • Trakselis, M. A. & Benkovic, S. J. Intricacies in ATP-dependent clamp loading: variations across replication systems. Structure 9, 999-1004 (2001).
    • (2001) Structure , vol.9 , pp. 999-1004
    • Trakselis, M.A.1    Benkovic, S.J.2
  • 9
    • 0026717535 scopus 로고
    • Three-dimensional structure of the β subunit of E. coli DNA polymerase III holoenzyme: A sliding DNA clamp
    • Kong, X. P., Onrust, R., O'Donnell, M. & Kuriyan, J. Three-dimensional structure of the β subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp. Cell 69, 425-437 (1992).
    • (1992) Cell , vol.69 , pp. 425-437
    • Kong, X.P.1    Onrust, R.2    O'Donnell, M.3    Kuriyan, J.4
  • 10
    • 0034628915 scopus 로고    scopus 로고
    • Crystal structure of the DNA polymerase processivity factor of T4 bacteriophage
    • Moarefi, I., Jeruzalmi, D., Turner, J., O'Donnell, M. & Kuriyan, J. Crystal structure of the DNA polymerase processivity factor of T4 bacteriophage. J. Mol. Biol. 296, 1215-1223 (2000).
    • (2000) J. Mol. Biol. , vol.296 , pp. 1215-1223
    • Moarefi, I.1    Jeruzalmi, D.2    Turner, J.3    O'Donnell, M.4    Kuriyan, J.5
  • 12
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    • Krishna, T. S., Kong, X. P., Gary, S., Burgers, P. M. & Kuriyan, J. Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Cell 79, 1233-1243 (1994).
    • (1994) Cell , vol.79 , pp. 1233-1243
    • Krishna, T.S.1    Kong, X.P.2    Gary, S.3    Burgers, P.M.4    Kuriyan, J.5
  • 13
    • 0035107856 scopus 로고    scopus 로고
    • Crystal structure of an archaeal DNA sliding clamp: Proliferating cell nuclear antigen from Pyrococcus furiosus
    • Matsumiya, S., Ishino, Y. & Morikawa, K. Crystal structure of an archaeal DNA sliding clamp: proliferating cell nuclear antigen from Pyrococcus furiosus. Protein Sci. 10, 17-23 (2001).
    • (2001) Protein Sci. , vol.10 , pp. 17-23
    • Matsumiya, S.1    Ishino, Y.2    Morikawa, K.3
  • 14
    • 0029150469 scopus 로고
    • Characterization of the five replication factor C genes of Saccharomyces cerevisiae
    • Cullmann, G., Fien, K., Kobayashi, R. & Stillman, B. Characterization of the five replication factor C genes of Saccharomyces cerevisiae. Mol. Cell. Biol. 15, 4661-4671 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4661-4671
    • Cullmann, G.1    Fien, K.2    Kobayashi, R.3    Stillman, B.4
  • 17
    • 0025303309 scopus 로고
    • The γ subunit of DNA polymerase III holoenzyme of Escherichia coli is produced by ribosomal frameshifting
    • Flower, A. M. & McHenry, C. S. The γ subunit of DNA polymerase III holoenzyme of Escherichia coli is produced by ribosomal frameshifting. Proc. Natl Acad. Sci. USA 87, 3713-3717 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3713-3717
    • Flower, A.M.1    McHenry, C.S.2
  • 18
    • 0025355475 scopus 로고
    • Translational frameshifting generates the γ subunit of DNA polymerase III holoenzyme
    • Tsuchihashi, Z. & Kornberg, A. Translational frameshifting generates the γ subunit of DNA polymerase III holoenzyme. Proc. Natl Acad. Sci. USA 87, 2516-2520 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2516-2520
    • Tsuchihashi, Z.1    Kornberg, A.2
  • 19
    • 0025354943 scopus 로고
    • Programmed ribosomal frameshifting generates the Escherichia coli DNA polymerase III γ subunit from within the τ subunit reading frame
    • Blinkowa, A. L. & Walker, J. R. Programmed ribosomal frameshifting generates the Escherichia coli DNA polymerase III γ subunit from within the τ subunit reading frame. Nucleic Acids Res. 18, 1725-1729 (1990).
    • (1990) Nucleic Acids Res. , vol.18 , pp. 1725-1729
    • Blinkowa, A.L.1    Walker, J.R.2
  • 20
    • 0034686075 scopus 로고    scopus 로고
    • Characterization of the unique C terminus of the Escherichia coli τ DnaX protein. Monomeric C-τ binds α and DnaB and can partially replace τ in reconstituted replication forks
    • Dallmann, H. G., Kim, S., Pritchard, A. E., Marians, K. J. & McHenry, C. S. Characterization of the unique C terminus of the Escherichia coli τ DnaX protein. Monomeric C-τ binds α and DnaB and can partially replace τ in reconstituted replication forks. J. Biol. Chem. 275, 15512-15519 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 15512-15519
    • Dallmann, H.G.1    Kim, S.2    Pritchard, A.E.3    Marians, K.J.4    McHenry, C.S.5
  • 21
    • 0035830939 scopus 로고    scopus 로고
    • τ Binds and organizes Escherichia coli replication through distinct domains. Partial proteolysis of terminally tagged τ to determine candidate domains and to assign domain V as the α binding domain
    • Gao, D. & McHenry, C. S. τ binds and organizes Escherichia coli replication through distinct domains. Partial proteolysis of terminally tagged τ to determine candidate domains and to assign domain V as the α binding domain. J. Biol. Chem. 276, 4433-4440 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 4433-4440
    • Gao, D.1    McHenry, C.S.2
  • 22
    • 0030070356 scopus 로고    scopus 로고
    • Coupling of a replicative polymerase and helicase: A τ-DnaB interaction mediates rapid replication fork movement
    • Kim, S., Dallmann, H. G., McHenry, C. S. & Marians, K. J. Coupling of a replicative polymerase and helicase: a τ-DnaB interaction mediates rapid replication fork movement. Cell 84, 643-650 (1996). Shows that the E. coli replicase couples to the helicase through mutual connection to the τ-subunit of the clamp loader. The interaction leads to the dramatically increased speed of helicase-mediated unwinding of DNA.
    • (1996) Cell , vol.84 , pp. 643-650
    • Kim, S.1    Dallmann, H.G.2    McHenry, C.S.3    Marians, K.J.4
  • 23
    • 0030595331 scopus 로고    scopus 로고
    • Replisome assembly reveals the basis for asymmetric function in leading and lagging strand replication
    • Yuzhakov, A., Turner, J. & O'Donnell, M. Replisome assembly reveals the basis for asymmetric function in leading and lagging strand replication. Cell 86, 877-886 (1996).
    • (1996) Cell , vol.86 , pp. 877-886
    • Yuzhakov, A.1    Turner, J.2    O'Donnell, M.3
  • 24
    • 0027298689 scopus 로고
    • DNA polymerase III accessory proteins. II. Characterization of δ and δ′
    • Onrust, R. & O'Donnell, M. DNA polymerase III accessory proteins. II. Characterization of δ and δ′. J. Biol. Chem. 268, 11766-11772 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 11766-11772
    • Onrust, R.1    O'Donnell, M.2
  • 25
    • 0029874442 scopus 로고    scopus 로고
    • In vivo assembly of the τ-complex of the DNA polymerase III holoenzyme expressed from a five-gene artificial operon. Cleavage of the τ-complex to form a mixed γ-τ-complex by the OmpT protease
    • Pritchard, A. E., Dallmann, H. G. & McHenry, C. S. In vivo assembly of the τ-complex of the DNA polymerase III holoenzyme expressed from a five-gene artificial operon. Cleavage of the τ-complex to form a mixed γ-τ-complex by the OmpT protease. J. Biol. Chem. 271, 10291-10298 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 10291-10298
    • Pritchard, A.E.1    Dallmann, H.G.2    McHenry, C.S.3
  • 26
    • 1642521025 scopus 로고    scopus 로고
    • Crystal structure of the χ:π sub-assembly of the Escherichia coli DNA polymerase clamp-loader complex
    • Gulbis, J. M. et al. Crystal structure of the χ:π sub-assembly of the Escherichia coli DNA polymerase clamp-loader complex. Eur. J. Biochem. 271, 439-449 (2004).
    • (2004) Eur. J. Biochem. , vol.271 , pp. 439-449
    • Gulbis, J.M.1
  • 27
    • 0032483511 scopus 로고    scopus 로고
    • The χπ subunits of DNA polymerase III holoenzyme bind to single-stranded DNA-binding protein (SSB) and facilitate replication of an SSB-coated template
    • Glover, B. P. & McHenry, C. S. The χπ subunits of DNA polymerase III holoenzyme bind to single-stranded DNA-binding protein (SSB) and facilitate replication of an SSB-coated template. J. Biol. Chem. 273, 23476-23484 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 23476-23484
    • Glover, B.P.1    McHenry, C.S.2
  • 28
    • 0033534380 scopus 로고    scopus 로고
    • Trading places on DNA - A three-point switch underlies primer handoff from primase to the replicative DNA polymerase
    • Yuzhakov, A., Kelman, Z. & O'Donnell, M. Trading places on DNA - a three-point switch underlies primer handoff from primase to the replicative DNA polymerase. Cell 96, 153-163 (1999).
    • (1999) Cell , vol.96 , pp. 153-163
    • Yuzhakov, A.1    Kelman, Z.2    O'Donnell, M.3
  • 29
    • 27244436298 scopus 로고    scopus 로고
    • The opened processivity clamp slides into view
    • Jeruzalmi, D. The opened processivity clamp slides into view. Proc. Natl Acad. Sci. USA 102, 14939-14940 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 14939-14940
    • Jeruzalmi, D.1
  • 30
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerization domain of N-ethylmaleimide- sensitive fusion protein
    • Lenzen, C. U., Steinmann, D., Whiteheart, S. W. & Weis, W. I. Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein. Cell 94, 525-536 (1998).
    • (1998) Cell , vol.94 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 31
    • 0031715606 scopus 로고    scopus 로고
    • Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP
    • Yu, R. C., Hanson, P. I., Jahn, R. & Brunger, A. T. Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP. Nature Struct. Biol. 5, 803-811 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 803-811
    • Yu, R.C.1    Hanson, P.I.2    Jahn, R.3    Brunger, A.T.4
  • 32
    • 0033081486 scopus 로고    scopus 로고
    • The internal workings of a DNA polymerase clamp-loading machine
    • Turner, J., Hingorani, M. M., Kelman, Z. & O'Donnell, M. The internal workings of a DNA polymerase clamp-loading machine. EMBO J. 18, 771-783 (1999).
    • (1999) EMBO J. , vol.18 , pp. 771-783
    • Turner, J.1    Hingorani, M.M.2    Kelman, Z.3    O'Donnell, M.4
  • 33
    • 0029019805 scopus 로고
    • Assembly of a chromosomal replication machine: Two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. II. Intermediate complex between the clamp loader and its clamp
    • Naktinis, V., Onrust, R., Fang, L. & O'Donnell, M. Assembly of a chromosomal replication machine: two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. II. Intermediate complex between the clamp loader and its clamp. J. Biol. Chem. 270, 13358-13365 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 13358-13365
    • Naktinis, V.1    Onrust, R.2    Fang, L.3    O'Donnell, M.4
  • 34
    • 0034666136 scopus 로고    scopus 로고
    • Molecular mechanism and energetics of clamp assembly in Escherichia coli. The role of ATP hydrolysis when γ complex loads β on DNA
    • Bertram, J. G. et al. Molecular mechanism and energetics of clamp assembly in Escherichia coli. The role of ATP hydrolysis when γ complex loads β on DNA. J. Biol. Chem. 275, 28413-28420 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 28413-28420
    • Bertram, J.G.1
  • 35
    • 0034723355 scopus 로고    scopus 로고
    • A model for Escherichia coli DNA polymerase III holoenzyme assembly at primer/template ends. DNA triggers a change in binding specificity of the γ complex clamp loader
    • Ason, B. et al. A model for Escherichia coli DNA polymerase III holoenzyme assembly at primer/ template ends. DNA triggers a change in binding specificity of the γ complex clamp loader. J. Biol. Chem. 275, 3006-3015 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 3006-3015
    • Ason, B.1
  • 36
    • 0038193630 scopus 로고    scopus 로고
    • Mechanism of loading the Escherichia coli DNA polymerase III β sliding clamp on DNA. Bona fide primer/templates preferentially trigger the γ complex to hydrolyze ATP and load the clamp
    • Ason, B. et al. Mechanism of loading the Escherichia coli DNA polymerase III β sliding clamp on DNA. Bona fide primer/templates preferentially trigger the γ complex to hydrolyze ATP and load the clamp. J. Biol. Chem. 278, 10033-10040 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 10033-10040
    • Ason, B.1
  • 37
    • 0141959300 scopus 로고    scopus 로고
    • Mechanism of the δ wrench in opening the β sliding clamp
    • Indiani, C. & O'Donnell, M. Mechanism of the δ wrench in opening the β sliding clamp. J. Biol. Chem. 278, 40272-40281 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 40272-40281
    • Indiani, C.1    O'Donnell, M.2
  • 38
    • 10044251053 scopus 로고    scopus 로고
    • Structural analysis of the inactive state of the Escherichia coli DNA polymerase clamp-loader complex
    • Kazmirski, S. L., Podobnik, M., Weitze, T. F., O'Donnell, M. & Kuriyan, J. Structural analysis of the inactive state of the Escherichia coli DNA polymerase clamp-loader complex. Proc. Natl Acad. Sci. USA 101, 16750-16755 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16750-16755
    • Kazmirski, S.L.1    Podobnik, M.2    Weitze, T.F.3    O'Donnell, M.4    Kuriyan, J.5
  • 39
    • 0024435347 scopus 로고
    • ATP interactions of the τ and γ subunits of DNA polymerase III holoenzyme of Escherichia coli
    • Tsuchihashi, Z. & Kornberg, A. ATP interactions of the τ and γ subunits of DNA polymerase III holoenzyme of Escherichia coli. J. Biol. Chem. 264, 17790-17795 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 17790-17795
    • Tsuchihashi, Z.1    Kornberg, A.2
  • 40
    • 0037515607 scopus 로고    scopus 로고
    • Ordered ATP hydrolysis in the γ complex clamp loader AAA+ machine
    • Johnson, A. & O'Donnell, M. Ordered ATP hydrolysis in the γ complex clamp loader AAA+ machine. J. Biol. Chem. 278, 14406-14413 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 14406-14413
    • Johnson, A.1    O'Donnell, M.2
  • 41
    • 1042266661 scopus 로고    scopus 로고
    • Mechanism of loading the Escherichia coli DNA polymerase III sliding clamp: II. Uncoupling the β and DNA binding activities of the γ complex
    • Snyder, A. K., Williams, C. R., Johnson, A., O'Donnell, M. & Bloom, L. B. Mechanism of loading the Escherichia coli DNA polymerase III sliding clamp: II. Uncoupling the β and DNA binding activities of the γ complex. J. Biol. Chem. 279, 4386-4393 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 4386-4393
    • Snyder, A.K.1    Williams, C.R.2    Johnson, A.3    O'Donnell, M.4    Bloom, L.B.5
  • 42
    • 1042301413 scopus 로고    scopus 로고
    • Mechanism of loading the Escherichia coli DNA polymerase III sliding clamp: I. Two distinct activities for individual ATP sites in the γ complex
    • Williams, C. R., Snyder, A. K., Kuzmic, P., O'Donnell, M. & Bloom, L. B. Mechanism of loading the Escherichia coli DNA polymerase III sliding clamp: I. Two distinct activities for individual ATP sites in the γ complex. J. Biol. Chem. 279, 4376-4385 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 4376-4385
    • Williams, C.R.1    Snyder, A.K.2    Kuzmic, P.3    O'Donnell, M.4    Bloom, L.B.5
  • 43
    • 0035967930 scopus 로고    scopus 로고
    • The DNA polymerase III holoenzyme: An asymmetric dimeric replicative complex with leading and lagging strand polymerases
    • Glover, B. P. & McHenry, C. S. The DNA polymerase III holoenzyme: an asymmetric dimeric replicative complex with leading and lagging strand polymerases. Cell 105, 925-934 (2001). This study shows, by using ATPγS, that the two polymerases in the E. coli holoenzyme are functionally distinct. The structurally asymmetric clamp loader to which they are both attached probably imposes the unique properties.
    • (2001) Cell , vol.105 , pp. 925-934
    • Glover, B.P.1    McHenry, C.S.2
  • 44
    • 0141677891 scopus 로고    scopus 로고
    • Chromosomal replicases as asymmetric dimers: Studies of subunit arrangement and functional consequences
    • McHenry, C. S. Chromosomal replicases as asymmetric dimers: studies of subunit arrangement and functional consequences. Mol. Microbiol. 49, 1157-1165 (2003).
    • (2003) Mol. Microbiol. , vol.49 , pp. 1157-1165
    • McHenry, C.S.1
  • 45
    • 0030043101 scopus 로고    scopus 로고
    • τ protects β in the leading-strand polymerase complex at the replication fork
    • Kim, S., Dallmann, H. G., McHenry, C. S. & Marians, K. J. τ protects β in the leading-strand polymerase complex at the replication fork. J. Biol. Chem. 271, 4315-4318 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 4315-4318
    • Kim, S.1    Dallmann, H.G.2    McHenry, C.S.3    Marians, K.J.4
  • 46
    • 0034176307 scopus 로고    scopus 로고
    • The recombination-replication interface
    • von Hippel, P. H. The recombination-replication interface. Trends Biochem. Sci. 25, 155 (2000).
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 155
    • Von Hippel, P.H.1
  • 47
    • 0026560910 scopus 로고
    • Protein-protein interactions at a DNA replication fork: Bacteriophage T4 as a model
    • Nossal, N. G. Protein-protein interactions at a DNA replication fork: bacteriophage T4 as a model. FASEB J. 6, 871-878 (1992).
    • (1992) FASEB J. , vol.6 , pp. 871-878
    • Nossal, N.G.1
  • 49
    • 0032692565 scopus 로고    scopus 로고
    • Building a replisome from interacting pieces: Sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex
    • Shamoo, Y. & Steitz, T. A. Building a replisome from interacting pieces: sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex. Cell 99, 155-166 (1999).
    • (1999) Cell , vol.99 , pp. 155-166
    • Shamoo, Y.1    Steitz, T.A.2
  • 50
    • 0024385309 scopus 로고
    • Structural and enzymatic studies of the T4 DNA replication system. I. Physical characterization of the polymerase accessory protein complex
    • Jarvis, T. C., Paul, L. S. & von Hippel, P. H. Structural and enzymatic studies of the T4 DNA replication system. I. Physical characterization of the polymerase accessory protein complex. J. Biol. Chem. 264, 12709-12716 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 12709-12716
    • Jarvis, T.C.1    Paul, L.S.2    Von Hippel, P.H.3
  • 51
    • 4944231970 scopus 로고    scopus 로고
    • On the solution structure of the T4 sliding clamp (gp45)
    • Millar, D., Trakselis, M. A. & Benkovic, S. J. On the solution structure of the T4 sliding clamp (gp45). Biochemistry 43, 12723-12727 (2004). FRET analysis is used to show that the T4 clamp exists in an asymmetric open state in solution.
    • (2004) Biochemistry , vol.43 , pp. 12723-12727
    • Millar, D.1    Trakselis, M.A.2    Benkovic, S.J.3
  • 52
    • 0024406804 scopus 로고
    • Structural and enzymatic studies of the T4 DNA replication system. II. ATPase properties of the polymerase accessory protein complex
    • Jarvis, T. C., Paul, L. S., Hockensmith, J. W. & von Hippel, P. H. Structural and enzymatic studies of the T4 DNA replication system. II. ATPase properties of the polymerase accessory protein complex. J. Biol. Chem. 264, 12717-12729 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 12717-12729
    • Jarvis, T.C.1    Paul, L.S.2    Hockensmith, J.W.3    Von Hippel, P.H.4
  • 53
    • 0030572980 scopus 로고    scopus 로고
    • The kinetic mechanism of formation of the bacteriophage T4 DNA polymerase sliding clamp
    • Young, M. C., Weitzel, S. E. & von Hippel, P. H. The kinetic mechanism of formation of the bacteriophage T4 DNA polymerase sliding clamp. J. Mol. Biol. 264, 440-452 (1996).
    • (1996) J. Mol. Biol. , vol.264 , pp. 440-452
    • Young, M.C.1    Weitzel, S.E.2    Von Hippel, P.H.3
  • 54
    • 0024348537 scopus 로고
    • The 44P subunit of the T4 DNA polymerase accessory protein complex catalyzes ATP hydrolysis
    • Rush, J. et al. The 44P subunit of the T4 DNA polymerase accessory protein complex catalyzes ATP hydrolysis. J. Biol. Chem. 264, 10943-10953 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 10943-10953
    • Rush, J.1
  • 55
    • 0029890834 scopus 로고    scopus 로고
    • Role of adenosine 5′-triphosphate hydrolysis in the assembly of the bacteriophage T4 DNA replication holoenzyme complex
    • Berdis, A. J. & Benkovic, S. J. Role of adenosine 5′-triphosphate hydrolysis in the assembly of the bacteriophage T4 DNA replication holoenzyme complex. Biochemistry 35, 9253-9265 (1996).
    • (1996) Biochemistry , vol.35 , pp. 9253-9265
    • Berdis, A.J.1    Benkovic, S.J.2
  • 56
    • 0034696523 scopus 로고    scopus 로고
    • Tracking sliding clamp opening and closing during bacteriophage T4 DNA polymerase holoenzyme assembly
    • Alley, S. C., Abel-Santos, E. & Benkovic, S. J. Tracking sliding clamp opening and closing during bacteriophage T4 DNA polymerase holoenzyme assembly. Biochemistry 39, 3076-3090 (2000).
    • (2000) Biochemistry , vol.39 , pp. 3076-3090
    • Alley, S.C.1    Abel-Santos, E.2    Benkovic, S.J.3
  • 57
    • 0030573047 scopus 로고    scopus 로고
    • Fluorescence monitoring of T4 polymerase holoenzyme accessory protein interactions during loading of the sliding clamp onto the template-primer junction
    • Latham, G. J., Pietroni, P., Dong, F., Young, M. C. & von Hippel, P. H. Fluorescence monitoring of T4 polymerase holoenzyme accessory protein interactions during loading of the sliding clamp onto the template-primer junction. J. Mol. Biol. 264, 426-439 (1996).
    • (1996) J. Mol. Biol. , vol.264 , pp. 426-439
    • Latham, G.J.1    Pietroni, P.2    Dong, F.3    Young, M.C.4    Von Hippel, P.H.5
  • 58
    • 0029952816 scopus 로고    scopus 로고
    • Protein-protein and protein-DNA interactions at the bacteriophage T4 DNA replication fork. Characterization of a fluorescently labeled DNA polymerase sliding clamp
    • Sexton, D. J., Carver, T. E., Berdis, A. J. & Benkovic, S. J. Protein-protein and protein-DNA interactions at the bacteriophage T4 DNA replication fork. Characterization of a fluorescently labeled DNA polymerase sliding clamp. J. Biol. Chem. 271, 28045-28051 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 28045-28051
    • Sexton, D.J.1    Carver, T.E.2    Berdis, A.J.3    Benkovic, S.J.4
  • 59
    • 0032568497 scopus 로고    scopus 로고
    • Dissecting the order of bacteriophage T4 DNA polymerase holoenzyme assembly
    • Sexton, D. J., Kaboord, B. F., Berdis, A. J., Carver, T. E. & Benkovic, S. J. Dissecting the order of bacteriophage T4 DNA polymerase holoenzyme assembly. Biochemistry 37, 7749-7756 (1998).
    • (1998) Biochemistry , vol.37 , pp. 7749-7756
    • Sexton, D.J.1    Kaboord, B.F.2    Berdis, A.J.3    Carver, T.E.4    Benkovic, S.J.5
  • 60
    • 0035902595 scopus 로고    scopus 로고
    • Creating a dynamic picture of the sliding clamp during T4 DNA polymerase holoenzyme assembly by using fluorescence resonance energy transfer
    • Trakselis, M. A., Alley, S. C., Abel-Santos, E. & Benkovic, S. J. Creating a dynamic picture of the sliding clamp during T4 DNA polymerase holoenzyme assembly by using fluorescence resonance energy transfer. Proc. Natl Acad. Sci. USA 98, 8368-8375 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8368-8375
    • Trakselis, M.A.1    Alley, S.C.2    Abel-Santos, E.3    Benkovic, S.J.4
  • 61
    • 0037436329 scopus 로고    scopus 로고
    • Examination of the role of the clamp-loader and ATP hydrolysis in the formation of the bacteriophage T4 polymerase holoenzyme
    • Trakselis, M. A., Berdis, A. J. & Benkovic, S. J. Examination of the role of the clamp-loader and ATP hydrolysis in the formation of the bacteriophage T4 polymerase holoenzyme. J. Mol. Biol. 326, 435-451 (2003). This study shows that the T4 clamp loader loads the clamp onto DNA through the sequential hydrolysis of two ATP before and two ATP after the addition of DNA. The final holoenzyme complex is formed upon departure of the clamp loader from this complex.
    • (2003) J. Mol. Biol. , vol.326 , pp. 435-451
    • Trakselis, M.A.1    Berdis, A.J.2    Benkovic, S.J.3
  • 62
    • 0031435067 scopus 로고    scopus 로고
    • Structural analyses of gp45 sliding clamp inter actions during assembly of the bacteriophage T4 DNA polymerase holoenzyme. I. Conformational changes within the gp44/62-gp45-ATP complex during clamp loading
    • Pietroni, P., Young, M. C., Latham, G. J. & von Hippel, P. H. Structural analyses of gp45 sliding clamp inter actions during assembly of the bacteriophage T4 DNA polymerase holoenzyme. I. Conformational changes within the gp44/62-gp45-ATP complex during clamp loading. J. Biol. Chem. 272, 31666-31676 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 31666-31676
    • Pietroni, P.1    Young, M.C.2    Latham, G.J.3    Von Hippel, P.H.4
  • 63
    • 0347075718 scopus 로고    scopus 로고
    • Dissociative properties of the proteins within the bacteriophage T4 replisome
    • Trakselis, M. A., Roccasecca, R. M., Yang, J., Valentine, A. M. & Benkovic, S. J. Dissociative properties of the proteins within the bacteriophage T4 replisome. J. Biol. Chem. 278, 49839-49849 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 49839-49849
    • Trakselis, M.A.1    Roccasecca, R.M.2    Yang, J.3    Valentine, A.M.4    Benkovic, S.J.5
  • 64
    • 0025800987 scopus 로고
    • Protein-DNA cross-linking demonstrates stepwise ATP-dependent assembly of T4 DNA polymerase and its accessory proteins on the primer-template
    • Capson, T. L., Benkovic, S. J. & Nossal, N. G. Protein-DNA cross-linking demonstrates stepwise ATP-dependent assembly of T4 DNA polymerase and its accessory proteins on the primer-template. Cell 65, 249-258 (1991).
    • (1991) Cell , vol.65 , pp. 249-258
    • Capson, T.L.1    Benkovic, S.J.2    Nossal, N.G.3
  • 65
    • 0027205336 scopus 로고
    • Laser cross-linking of proteins to nucleic acids. II. Interactions of the bacteriophage T4 DNA replication polymerase accessory proteins complex with DNA
    • Hockensmith, J. W., Kubasek, W. L., Evertsz, E. M., Mesner, L. D. & von Hippel, P. H. Laser cross-linking of proteins to nucleic acids. II. Interactions of the bacteriophage T4 DNA replication polymerase accessory proteins complex with DNA. J. Biol. Chem. 268, 15721-15730 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 15721-15730
    • Hockensmith, J.W.1    Kubasek, W.L.2    Evertsz, E.M.3    Mesner, L.D.4    Von Hippel, P.H.5
  • 66
    • 0035914387 scopus 로고    scopus 로고
    • Building a replisome solution structure by elucidation of protein-protein interactions in the bacteriophage T4 DNA polymerase holoenzyme
    • Alley, S. C. et al. Building a replisome solution structure by elucidation of protein-protein interactions in the bacteriophage T4 DNA polymerase holoenzyme. J. Biol. Chem. 276, 39340-39349 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 39340-39349
    • Alley, S.C.1
  • 67
    • 0030971817 scopus 로고    scopus 로고
    • Mechanism of bacteriophage T4 DNA holoenzyme assembly: The 44/62 protein acts as a molecular motor
    • Berdis, A. J. & Benkovic, S. J. Mechanism of bacteriophage T4 DNA holoenzyme assembly: the 44/62 protein acts as a molecular motor. Biochemistry 36, 2733-2743 (1997).
    • (1997) Biochemistry , vol.36 , pp. 2733-2743
    • Berdis, A.J.1    Benkovic, S.J.2
  • 68
    • 0031451343 scopus 로고    scopus 로고
    • Structural analyses of gp45 sliding clamp interactions during assembly of the bacteriophage T4 DNA polymerase holoenzyme. III. The gp43 DNA polymerase binds to the same face of the sliding clamp as the clamp loader
    • Latham, G. J., Bacheller, D. J., Pietroni, P. & von Hippel, P. H. Structural analyses of gp45 sliding clamp interactions during assembly of the bacteriophage T4 DNA polymerase holoenzyme. III. The gp43 DNA polymerase binds to the same face of the sliding clamp as the clamp loader. J. Biol. Chem. 272, 31685-31692 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 31685-31692
    • Latham, G.J.1    Bacheller, D.J.2    Pietroni, P.3    Von Hippel, P.H.4
  • 69
    • 0031438369 scopus 로고    scopus 로고
    • Structural analyses of gp45 sliding clamp interactions during assembly of the bacteriophage T4 DNA polymerase holoenzyme. II. The gp44/62 clamp loader interacts with a single defined face of the sliding clamp ring
    • Latham, G. J., Bacheller, D. J., Pietroni, P. & von Hippel, P. H. Structural analyses of gp45 sliding clamp interactions during assembly of the bacteriophage T4 DNA polymerase holoenzyme. II. The gp44/62 clamp loader interacts with a single defined face of the sliding clamp ring. J. Biol. Chem. 272, 31677-31684 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 31677-31684
    • Latham, G.J.1    Bacheller, D.J.2    Pietroni, P.3    Von Hippel, P.H.4
  • 70
    • 0027469983 scopus 로고
    • Assembly of a functional replication complex without ATP hydrolysis: A direct interaction of bacteriophage T4 gp45 with T4 DNA polymerase
    • Reddy, M. K., Weitzel, S. E. & von Hippel, P. H. Assembly of a functional replication complex without ATP hydrolysis: a direct interaction of bacteriophage T4 gp45 with T4 DNA polymerase. Proc. Natl Acad. Sci. USA 90, 3211-3215 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3211-3215
    • Reddy, M.K.1    Weitzel, S.E.2    Von Hippel, P.H.3
  • 71
    • 18044384092 scopus 로고    scopus 로고
    • DNA polymerases that propagate the eukaryotic DNA replication fork
    • Garg, P. & Burgers, P. M. DNA polymerases that propagate the eukaryotic DNA replication fork. Crit. Rev. Biochem. Mol. Biol. 40, 115-128 (2005).
    • (2005) Crit. Rev. Biochem. Mol. Biol. , vol.40 , pp. 115-128
    • Garg, P.1    Burgers, P.M.2
  • 73
    • 0031038379 scopus 로고    scopus 로고
    • Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen
    • Mossi, R., Jonsson, Z. O., Allen, B. L., Hardin, S. H. & Hubscher, U. Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen. J. Biol. Chem. 272, 1769-1776 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 1769-1776
    • Mossi, R.1    Jonsson, Z.O.2    Allen, B.L.3    Hardin, S.H.4    Hubscher, U.5
  • 74
    • 0031865131 scopus 로고    scopus 로고
    • Cip1/Waf1, DNA polymerase δ and replication factor C
    • Cip1/Waf1, DNA polymerase δ and replication factor C. Genes Cells 3, 357-369 (1998).
    • (1998) Genes Cells , vol.3 , pp. 357-369
    • Oku, T.1
  • 75
    • 0030892079 scopus 로고    scopus 로고
    • Identification of regions within the four small subunits of human replication factor C required for complex formation and DNA replication
    • Uhlmann, F., Gibbs, E., Cai, J., O'Donnell, M. & Hurwitz, J. Identification of regions within the four small subunits of human replication factor C required for complex formation and DNA replication. J. Biol. Chem. 272, 10065-10071 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 10065-10071
    • Uhlmann, F.1    Gibbs, E.2    Cai, J.3    O'Donnell, M.4    Hurwitz, J.5
  • 76
    • 0027367155 scopus 로고
    • cDNAs encoding the large subunit of human replication factor C
    • Bunz, F., Kobayashi, R. & Stillman, B. cDNAs encoding the large subunit of human replication factor C. Proc. Natl Acad. Sci. USA 90, 11014-11018 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11014-11018
    • Bunz, F.1    Kobayashi, R.2    Stillman, B.3
  • 77
    • 0035860719 scopus 로고    scopus 로고
    • ATP utilization by yeast replication factor C. I. ATP-mediated interaction with DNA and with proliferating cell nuclear antigen
    • Gomes, X. V. & Burgers, P. M. ATP utilization by yeast replication factor C. I. ATP-mediated interaction with DNA and with proliferating cell nuclear antigen. J. Biol. Chem. 276, 34768-34775 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 34768-34775
    • Gomes, X.V.1    Burgers, P.M.2
  • 78
    • 0034640522 scopus 로고    scopus 로고
    • Overproduction in Escherichia coli and characterization of yeast replication factor C lacking the ligase homology domain
    • Gomes, X. V., Gary, S. L. & Burgers, P. M. Overproduction in Escherichia coli and characterization of yeast replication factor C lacking the ligase homology domain. J. Biol. Chem. 275, 14541-14549 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 14541-14549
    • Gomes, X.V.1    Gary, S.L.2    Burgers, P.M.3
  • 79
    • 0033965418 scopus 로고    scopus 로고
    • A novel Rad24 checkpoint protein complex closely related to replication factor C
    • Green, C. M., Erdjument-Bromage, H., Tempst, P. & Lowndes, N. F. A novel Rad24 checkpoint protein complex closely related to replication factor C. Curr. Biol. 10, 39-42 (2000).
    • (2000) Curr. Biol. , vol.10 , pp. 39-42
    • Green, C.M.1    Erdjument-Bromage, H.2    Tempst, P.3    Lowndes, N.F.4
  • 80
  • 81
    • 0041966011 scopus 로고    scopus 로고
    • Elg1 forms an alternative RFC complex important for DNA replication and genome integrity
    • Bellaoui, M. et al. Elg1 forms an alternative RFC complex important for DNA replication and genome integrity. EMBO J. 22, 4304-4313 (2003).
    • (2003) EMBO J. , vol.22 , pp. 4304-4313
    • Bellaoui, M.1
  • 82
    • 0042191693 scopus 로고    scopus 로고
    • ELG1, a yeast gene required for genome stability, forms a complex related to replication factor C
    • Ben-Aroya, S., Koren, A., Liefshitz, B., Steinlauf, R. & Kupiec, M. ELG1, a yeast gene required for genome stability, forms a complex related to replication factor C. Proc. Natl Acad. Sci. USA 100, 9906-9911 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 9906-9911
    • Ben-Aroya, S.1    Koren, A.2    Liefshitz, B.3    Steinlauf, R.4    Kupiec, M.5
  • 83
    • 0141504148 scopus 로고    scopus 로고
    • Elg1 forms an alternative PCNA-interacting RFC complex required to maintain genome stability
    • Kanellis, P., Agyei, R. & Durocher, D. Elg1 forms an alternative PCNA-interacting RFC complex required to maintain genome stability. Curr. Biol. 13, 1583-1595 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 1583-1595
    • Kanellis, P.1    Agyei, R.2    Durocher, D.3
  • 84
    • 4243156107 scopus 로고    scopus 로고
    • Biochemical characterization of DNA damage checkpoint complexes: Clamp loader and clamp complexes with specificity for 5′ recessed DNA
    • Ellison, V. & Stillman, B. Biochemical characterization of DNA damage checkpoint complexes: clamp loader and clamp complexes with specificity for 5′ recessed DNA. PLoS Biol. 1, E33 (2003).
    • (2003) PLoS Biol. , vol.1
    • Ellison, V.1    Stillman, B.2
  • 85
    • 0345564858 scopus 로고    scopus 로고
    • Replication protein A-mediated recruitment and activation of Rad17 complexes
    • Zou, L., Liu, D. & Elledge, S. J. Replication protein A-mediated recruitment and activation of Rad17 complexes. Proc. Natl Acad. Sci. USA 100, 13827-13832 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13827-13832
    • Zou, L.1    Liu, D.2    Elledge, S.J.3
  • 86
    • 3943107573 scopus 로고    scopus 로고
    • Molecular mechanisms of mammalian DNA repair and the DNA damage checkpoints
    • Sancar, A., Lindsey-Boltz, L. A., Unsal-Kacmaz, K. & Linn, S. Molecular mechanisms of mammalian DNA repair and the DNA damage checkpoints. Annu. Rev. Biochem.73, 39-85 (2004).
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 39-85
    • Sancar, A.1    Lindsey-Boltz, L.A.2    Unsal-Kacmaz, K.3    Linn, S.4
  • 87
    • 11144266855 scopus 로고    scopus 로고
    • The PCNA-RFC families of DNA clamps and clamp loaders
    • Majka, J. & Burgers, P. M. The PCNA-RFC families of DNA clamps and clamp loaders. Prog. Nucleic Acid Res. Mol. Biol. 78, 227-260 (2004).
    • (2004) Prog. Nucleic Acid Res. Mol. Biol. , vol.78 , pp. 227-260
    • Majka, J.1    Burgers, P.M.2
  • 88
    • 20744435871 scopus 로고    scopus 로고
    • Replication protein A-directed unloading of PCNA by the Ctf18 cohesion establishment complex
    • Bylund, G. O. & Burgers, P. M. Replication protein A-directed unloading of PCNA by the Ctf18 cohesion establishment complex. Mol. Cell. Biol. 25, 5445-5455 (2005). This study shows that the Ctf18-RFC complex is extremely efficient in removing PCNA from DNA, which indicates that it might recycle clamps.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5445-5455
    • Bylund, G.O.1    Burgers, P.M.2
  • 90
    • 0011065967 scopus 로고    scopus 로고
    • A conserved domain of the large subunit of replication factor C binds PCNA and acts like a dominant negative inhibitor of DNA replication in mammalian cells
    • Fotedar, R. et al. A conserved domain of the large subunit of replication factor C binds PCNA and acts like a dominant negative inhibitor of DNA replication in mammalian cells. EMBO J. 15, 4423-4433 (1996).
    • (1996) EMBO J. , vol.15 , pp. 4423-4433
    • Fotedar, R.1
  • 91
    • 0025889702 scopus 로고
    • Saccharomyces cerevisiae replication factor C. II. Formation and activity of complexes with the proliferating cell nuclear antigen and with DNA polymerases δ and ε
    • Burgers, P. M. Saccharomyces cerevisiae replication factor C. II. Formation and activity of complexes with the proliferating cell nuclear antigen and with DNA polymerases δ and ε. J. Biol. Chem. 266, 22698-22706 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 22698-22706
    • Burgers, P.M.1
  • 92
    • 0032544708 scopus 로고    scopus 로고
    • ATP binding to the Escherichia coli clamp loader powers opening of the ring-shaped clamp of DNA polymerase III holoenzyme
    • Hingorani, M. M. & O'Donnell, M. ATP binding to the Escherichia coli clamp loader powers opening of the ring-shaped clamp of DNA polymerase III holoenzyme. J. Biol. Chem. 273, 24550-24563 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 24550-24563
    • Hingorani, M.M.1    O'Donnell, M.2
  • 93
    • 0025293914 scopus 로고
    • Mechanism of elongation of primed DNA by DNA polymerase δ, proliferating cell nuclear antigen, and activator 1
    • Lee, S. H. & Hurwitz, J. Mechanism of elongation of primed DNA by DNA polymerase δ, proliferating cell nuclear antigen, and activator 1. Proc. Natl Acad. Sci. USA 87, 5672-5676 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5672-5676
    • Lee, S.H.1    Hurwitz, J.2
  • 94
    • 0026089096 scopus 로고
    • Replication factors required for SV40 DNA replication in vitro. I. DNA structure-specific recognition of a primer-template junction by eukaryotic DNA polymerases and their accessory proteins
    • Tsurimoto, T. & Stillman, B. Replication factors required for SV40 DNA replication in vitro. I. DNA structure-specific recognition of a primer-template junction by eukaryotic DNA polymerases and their accessory proteins. J. Biol. Chem. 266, 1950-1960 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 1950-1960
    • Tsurimoto, T.1    Stillman, B.2
  • 95
    • 0035860694 scopus 로고    scopus 로고
    • ATP utilization by yeast replication factor C. II. Multiple stepwise ATP binding events are required to load proliferating cell nuclear antigen onto primed DNA
    • Gomes, X. V., Schmidt, S. L. & Burgers, P. M. ATP utilization by yeast replication factor C. II. Multiple stepwise ATP binding events are required to load proliferating cell nuclear antigen onto primed DNA. J. Biol. Chem. 276, 34776-34783 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 34776-34783
    • Gomes, X.V.1    Schmidt, S.L.2    Burgers, P.M.3
  • 96
    • 0035860818 scopus 로고    scopus 로고
    • ATP utilization by yeast replication factor C. III. The ATP-binding domains of Rfc2, Rfc3, and Rfc4 are essential for DNA recognition and clamp loading
    • Schmidt, S. L., Gomes, X. V. & Burgers, P. M. ATP utilization by yeast replication factor C. III. The ATP-binding domains of Rfc2, Rfc3, and Rfc4 are essential for DNA recognition and clamp loading. J. Biol. Chem. 276, 34784-34791 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 34784-34791
    • Schmidt, S.L.1    Gomes, X.V.2    Burgers, P.M.3
  • 97
    • 25444469141 scopus 로고    scopus 로고
    • Out-of-plane motions in open sliding clamps: Molecular dynamics simulations of eukaryotic and archaeal proliferating cell nuclear antigen
    • Kazmirski, S. L., Zhao, Y., Bowman, G. D., O'Donnell, M. & Kuriyan, J. Out-of-plane motions in open sliding clamps: molecular dynamics simulations of eukaryotic and archaeal proliferating cell nuclear antigen. Proc. Natl Acad. Sci. USA 102, 13801-13806 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 13801-13806
    • Kazmirski, S.L.1    Zhao, Y.2    Bowman, G.D.3    O'Donnell, M.4    Kuriyan, J.5
  • 98
    • 33644531259 scopus 로고    scopus 로고
    • The structure of a ring-opened proliferating cell nuclear antigen-replication factor C complex revealed by fluorescence energy transfer
    • Zhuang, Z., Yoder, B. L., Burgers, P. M. & Benkovic, S. J. The structure of a ring-opened proliferating cell nuclear antigen-replication factor C complex revealed by fluorescence energy transfer. Proc. Natl Acad. Sci. USA 3, 2546-2551 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.3 , pp. 2546-2551
    • Zhuang, Z.1    Yoder, B.L.2    Burgers, P.M.3    Benkovic, S.J.4
  • 99
  • 100
    • 0029062984 scopus 로고
    • Mammalian DNA polymerase auxiliary proteins: Analysis of replication factor C-catalyzed proliferating cell nuclear antigen loading onto circular double-stranded DNA
    • Podust, L. M., Podust, V. N., Sogo, J. M. & Hubscher, U. Mammalian DNA polymerase auxiliary proteins: analysis of replication factor C-catalyzed proliferating cell nuclear antigen loading onto circular double-stranded DNA. Mol. Cell. Biol. 15, 3072-3081 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3072-3081
    • Podust, L.M.1    Podust, V.N.2    Sogo, J.M.3    Hubscher, U.4
  • 101
    • 0001271789 scopus 로고
    • Phylogenetic structure of the prokaryotic domain: The primary kingdoms
    • Woese, C. R. & Fox, G. E. Phylogenetic structure of the prokaryotic domain: the primary kingdoms. Proc. Natl Acad. Sci. USA 74, 5088-5090 (1977).
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 5088-5090
    • Woese, C.R.1    Fox, G.E.2
  • 102
    • 0031587820 scopus 로고    scopus 로고
    • Archaeal genomics: An overview
    • Olsen, G. J. & Woese, C. R. Archaeal genomics: an overview. Cell 89, 991-994 (1997).
    • (1997) Cell , vol.89 , pp. 991-994
    • Olsen, G.J.1    Woese, C.R.2
  • 103
    • 0031587829 scopus 로고    scopus 로고
    • Archaea and the origin(s) of DNA replication proteins
    • Edgell, D. R. & Doolittle, W. F. Archaea and the origin(s) of DNA replication proteins. Cell 89, 995-998 (1997).
    • (1997) Cell , vol.89 , pp. 995-998
    • Edgell, D.R.1    Doolittle, W.F.2
  • 104
    • 0033199713 scopus 로고    scopus 로고
    • Did DNA replication evolve twice independently?
    • Leipe, D. D., Aravind, L. & Koonin, E. V. Did DNA replication evolve twice independently? Nucleic Acids Res. 27, 3389-3401 (1999).
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3389-3401
    • Leipe, D.D.1    Aravind, L.2    Koonin, E.V.3
  • 105
    • 0742321956 scopus 로고    scopus 로고
    • Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair
    • Chapados, B. R. et al. Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair. Cell 116, 39-50 (2004).
    • (2004) Cell , vol.116 , pp. 39-50
    • Chapados, B.R.1
  • 106
    • 0032745320 scopus 로고    scopus 로고
    • Functional interactions of a homolog of proliferating cell nuclear antigen with DNA polymerases in archaea
    • Cann, I. K. et al. Functional interactions of a homolog of proliferating cell nuclear antigen with DNA polymerases in archaea. J. Bacteriol. 181, 6591-6599 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 6591-6599
    • Cann, I.K.1
  • 107
    • 0037251411 scopus 로고    scopus 로고
    • A heterotrimeric PCNA in the hyperthermophilic archaeon Sulfolobus solfataricus
    • Dionne, I., Nookala, R. K., Jackson, S. P., Doherty, A. J. & Bell, S. D. A heterotrimeric PCNA in the hyperthermophilic archaeon Sulfolobus solfataricus. Mol. Cell 11, 275-282 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 275-282
    • Dionne, I.1    Nookala, R.K.2    Jackson, S.P.3    Doherty, A.J.4    Bell, S.D.5
  • 108
    • 0032814005 scopus 로고    scopus 로고
    • Archaeal DNA replication: Identifying the pieces to solve a puzzle
    • Cann, I. K. & Ishino, Y. Archaeal DNA replication: identifying the pieces to solve a puzzle. Genetics 152, 1249-1267 (1999).
    • (1999) Genetics , vol.152 , pp. 1249-1267
    • Cann, I.K.1    Ishino, Y.2
  • 109
    • 0035093865 scopus 로고    scopus 로고
    • Biochemical analysis of replication factor C from the hyperthermophilic archaeon Pyrococcus furiosus
    • Cann, I. K. et al. Biochemical analysis of replication factor C from the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 183, 2614-2623 (2001).
    • (2001) J. Bacteriol. , vol.183 , pp. 2614-2623
    • Cann, I.K.1
  • 110
    • 0034604383 scopus 로고    scopus 로고
    • Biochemical characterization of a clamp-loader complex homologous to eukaryotic replication factor C from the hyperthermophilic archaeon Sulfolobus solfataricus
    • 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).
    • (2000) J. Mol. Biol. , vol.301 , pp. 61-73
    • Pisani, F.M.1    De Felice, M.2    Carpentieri, F.3    Rossi, M.4
  • 111
    • 0037109208 scopus 로고    scopus 로고
    • Biochemical characterisation of the clamp/clamp loader proteins from the euryarchaeon Archaeoglobus fulgidus
    • Seybert, A., Scott, D. J., Scaife, S., Singleton, M. R. & Wigley, D. B. Biochemical characterisation of the clamp/clamp loader proteins from the euryarchaeon Archaeoglobus fulgidus. Nucleic Acids Res. 30, 4329-4338 (2002).
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4329-4338
    • Seybert, A.1    Scott, D.J.2    Scaife, S.3    Singleton, M.R.4    Wigley, D.B.5
  • 112
    • 0034629109 scopus 로고    scopus 로고
    • A unique organization of the protein subunits of the DNA polymerase clamp loader in the archaeon Methanobacterium thermoautotrophicum δH
    • Kelman, Z. & Hurwitz, J. A unique organization of the protein subunits of the DNA polymerase clamp loader in the archaeon Methanobacterium thermoautotrophicum δH. J. Biol. Chem. 275, 7327-7336 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 7327-7336
    • Kelman, Z.1    Hurwitz, J.2
  • 113
    • 0036734527 scopus 로고    scopus 로고
    • Physical interaction between proliferating cell nuclear antigen and replication factor C from Pyrococcus furiosus
    • Matsumiya, S., Ishino, S., Ishino, Y. & Morikawa, K. Physical interaction between proliferating cell nuclear antigen and replication factor C from Pyrococcus furiosus. Genes Cells 7, 911-922 (2002).
    • (2002) Genes Cells , vol.7 , pp. 911-922
    • Matsumiya, S.1    Ishino, S.2    Ishino, Y.3    Morikawa, K.4
  • 114
    • 0034840471 scopus 로고    scopus 로고
    • Atomic structure of the clamp loader small subunit from Pyrococcus furiosus
    • Oyama, T., Ishino, Y., Cann, I. K., Ishino, S. & Morikawa, K. Atomic structure of the clamp loader small subunit from Pyrococcus furiosus. Mol. Cell 8, 455-463 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 455-463
    • Oyama, T.1    Ishino, Y.2    Cann, I.K.3    Ishino, S.4    Morikawa, K.5
  • 115
    • 33646778502 scopus 로고    scopus 로고
    • Communication between subunits within an archaeal clamp-loader complex
    • 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). The crystal structure of the hexameric complex formed by the RFC-s from A. fulgidus shows a conformational change that is associated with nucleotide binding. Mutational analysis shows distinct regulatory roles during clamp loading that distinguish the large and the small subunits in the RFC complex.
    • (2006) EMBO J. , vol.25 , pp. 2209-2218
    • Seybert, A.1    Singleton, M.R.2    Cook, N.3    Hall, D.R.4    Wigley, D.B.5
  • 116
    • 0035783136 scopus 로고    scopus 로고
    • Three-dimensional electron microscopy of the clamp loader small subunit from Pyrococcus furiosus
    • Mayanagi, K., Miyata, T., Oyama, T., Ishino, Y. & Morikawa, K. Three-dimensional electron microscopy of the clamp loader small subunit from Pyrococcus furiosus. J. Struct. Biol. 134, 35-45 (2001).
    • (2001) J. Struct. Biol. , vol.134 , pp. 35-45
    • Mayanagi, K.1    Miyata, T.2    Oyama, T.3    Ishino, Y.4    Morikawa, K.5
  • 117
    • 0037334909 scopus 로고    scopus 로고
    • Nucleotide-induced conformational changes in an isolated Escherichia coli DNA polymerase III clamp loader subunit
    • Podobnik, M., Weitze, T. F., O'Donnell, M. & Kuriyan, J. Nucleotide-induced conformational changes in an isolated Escherichia coli DNA polymerase III clamp loader subunit. Structure 11, 253-263 (2003).
    • (2003) Structure , vol.11 , pp. 253-263
    • Podobnik, M.1    Weitze, T.F.2    O'Donnell, M.3    Kuriyan, J.4
  • 118
    • 1942503398 scopus 로고    scopus 로고
    • Distinct roles for ATP binding and hydrolysis at individual subunits of an archaeal clamp loader
    • Seybert, A. & Wigley, D. B. Distinct roles for ATP binding and hydrolysis at individual subunits of an archaeal clamp loader. EMBO J. 23, 1360-1371 (2004).
    • (2004) EMBO J. , vol.23 , pp. 1360-1371
    • Seybert, A.1    Wigley, D.B.2
  • 119
    • 3042642152 scopus 로고    scopus 로고
    • The clamp-loading complex for processive DNA replication
    • Miyata, T. et al. The clamp-loading complex for processive DNA replication. Nature Struct. Mol. Biol. 11, 632-636 (2004).
    • (2004) Nature Struct. Mol. Biol. , vol.11 , pp. 632-636
    • Miyata, T.1
  • 120
    • 0346654081 scopus 로고    scopus 로고
    • Structural and biochemical analysis of sliding clamp-ligand interactions suggest a competition between replicative and translesion DNA polymerases
    • Burnouf, D. Y. et al. Structural and biochemical analysis of sliding clamp-ligand interactions suggest a competition between replicative and translesion DNA polymerases. J. Mol. Biol. 335, 1187-1197 (2004).
    • (2004) J. Mol. Biol. , vol.335 , pp. 1187-1197
    • Burnouf, D.Y.1
  • 121
    • 24944543952 scopus 로고    scopus 로고
    • A sliding-clamp toolbelt binds high- and low-fidelity DNA polymerases simultaneously
    • Indiani, C., McInerney, P., Georgescu, R., Goodman, M. F. & O'Donnell, M. A sliding-clamp toolbelt binds high- and low-fidelity DNA polymerases simultaneously. Mol. Cell 19, 805-815 (2005).
    • (2005) Mol. Cell , vol.19 , pp. 805-815
    • Indiani, C.1    McInerney, P.2    Georgescu, R.3    Goodman, M.F.4    O'Donnell, M.5
  • 123
    • 33745041480 scopus 로고    scopus 로고
    • Evolutionary relationships and structural mechanisms of AAA+ proteins
    • Erzberger, J. P. & Berger, J. M. Evolutionary relationships and structural mechanisms of AAA+ proteins. Annu. Rev. Biophys. Biomol. Struct. 35, 93-114 (2006). This review describes critical features of the AAA+ domain, provides classifications of the AAA+ modules and discusses the versatility and adaptability of the hexameric AAA+ assembly.
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 93-114
    • Erzberger, J.P.1    Berger, J.M.2
  • 124
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald, A. F., Aravind, L., Spouge, J. L. & Koonin, E. V. AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 27-43 (1999).
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 125
    • 23344439328 scopus 로고    scopus 로고
    • Evolutionary clues to eukaryotic DNA clamp-loading mechanisms: Analysis of the functional constraints imposed on replication factor C AAA+ ATPases
    • Neuwald, A. F. Evolutionary clues to eukaryotic DNA clamp-loading mechanisms: analysis of the functional constraints imposed on replication factor C AAA+ ATPases. Nucleic Acids Res. 33, 3614-3628 (2005).
    • (2005) Nucleic Acids Res. , vol.33 , pp. 3614-3628
    • Neuwald, A.F.1
  • 126
    • 0030666224 scopus 로고    scopus 로고
    • Crystal structure of the δ′ subunit of the clamp-loader complex of E. coli DNA polymerase III
    • Guenther, B., Onrust, R., Sali, A., O'Donnell, M. & Kuriyan, J. Crystal structure of the δ′ subunit of the clamp-loader complex of E. coli DNA polymerase III. Cell 91, 335-345 (1997).
    • (1997) Cell , vol.91 , pp. 335-345
    • Guenther, B.1    Onrust, R.2    Sali, A.3    O'Donnell, M.4    Kuriyan, J.5
  • 127
    • 0031231083 scopus 로고    scopus 로고
    • Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras
    • Ahmadian, M. R., Stege, P., Scheffzek, K. & Wittinghofer, A. Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras. Nature Struct. Biol. 4, 686-689 (1997).
    • (1997) Nature Struct. Biol. , vol.4 , pp. 686-689
    • Ahmadian, M.R.1    Stege, P.2    Scheffzek, K.3    Wittinghofer, A.4


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