메뉴 건너뛰기




Volumn 289, Issue 9, 2014, Pages 5537-5548

The ATP sites of AAA+ clamp loaders work together as a switch to assemble clamps on DNA

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ACTIVITIES; BINDING AFFINITIES; BIOCHEMICAL ASSAY; CELLULAR ACTIVITIES; CONFORMATIONAL CHANGE; DNA POLYMERASE; OPEN CONFORMATION; PROLIFERATING CELL NUCLEAR ANTIGENS;

EID: 84896895126     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.541466     Document Type: Article
Times cited : (10)

References (53)
  • 2
    • 39449115385 scopus 로고    scopus 로고
    • AAA+ proteins: Diversity in function, similarity in structure
    • DOI 10.1042/BST0360072
    • Snider, J., and Houry, W. A. (2008) AAA+ proteins: diversity in function, similarity in structure. Biochem. Soc. Trans. 36, 72-77 (Pubitemid 351269625)
    • (2008) Biochemical Society Transactions , vol.36 , Issue.1 , pp. 72-77
    • Snider, J.1    Houry, W.A.2
  • 3
    • 0037010120 scopus 로고    scopus 로고
    • AAA+ proteins and substrate recognition, it all depends on their partner in crime
    • DOI 10.1016/S0014-5793(02)03179-4, PII S0014579302031794
    • Dougan, D. A., Mogk, A., Zeth, K., Turgay, K., and Bukau, B. (2002) AAA+ proteins and substrate recognition, it all depends on their partner in crime. FEBS Lett. 529, 6-10 (Pubitemid 35283903)
    • (2002) FEBS Letters , vol.529 , Issue.1 , pp. 6-10
    • Dougan, D.A.1    Mogk, A.2    Zeth, K.3    Turgay, K.4    Bukau, B.5
  • 5
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    • Krishna, T. S., Kong, X. P., Gary, S., Burgers, P. M., and Kuriyan, J. (1994) Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Cell 79, 1233-1243
    • (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
  • 6
    • 0029678248 scopus 로고    scopus 로고
    • Clamp loading, unloading and intrinsic stability of the PCNA, β and gp45 sliding clamps of human, E. coli and T4 replicases
    • Yao, N., Turner, J., Kelman, Z., Stukenberg, P. T., Dean, F., Shechter, D., Pan, Z. Q., Hurwitz, J., and O'Donnell, M. (1996) Clamp loading, unloading and intrinsic stability of the PCNA, β and gp45 sliding clamps of human, E. coli and T4 replicases. Genes Cells 1, 101-113 (Pubitemid 126673110)
    • (1996) Genes to Cells , vol.1 , Issue.1 , pp. 101-113
    • Yao, N.1    Turner, J.2    Kelman, Z.3    Todd, S.P.4    Dean, F.5    Shechter, D.6    Pan, Z.-Q.7    Hurwitz, J.8    O'Donnell, M.9
  • 7
    • 3042588011 scopus 로고    scopus 로고
    • Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex
    • DOI 10.1038/nature02585
    • Bowman, G. D., O'Donnell, M., and Kuriyan, J. (2004) Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex. Nature 429, 724-730 (Pubitemid 38833117)
    • (2004) Nature , vol.429 , Issue.6993 , pp. 724-730
    • Bowman, G.D.1    O'Donnell, M.2    Kuriyan, J.3
  • 9
    • 0001607723 scopus 로고
    • Distantly related sequences in the &alpha- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., Saraste, M., Runswick, M. J., and Gay, N. J. (1982) Distantly related sequences in the &alpha- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1, 945-951
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 10
    • 0032969563 scopus 로고    scopus 로고
    • +: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald, A. F., Aravind, L., Spouge, J. L., and Koonin, E. V. (1999) AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 27-43 (Pubitemid 29095146)
    • (1999) Genome Research , vol.9 , Issue.1 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 11
    • 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., and Burgers, P. M. (2001) 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) J. Biol. Chem. , vol.276 , pp. 34784-34791
    • Schmidt, S.L.1    Gomes, X.V.2    Burgers, P.M.3
  • 13
    • 1942503398 scopus 로고    scopus 로고
    • Distinct roles for ATP binding and hydrolysis at individual subunits of an archaeal clamp loader
    • DOI 10.1038/sj.emboj.7600130
    • Seybert, A., and Wigley, D. B. (2004) Distinct roles for ATP binding and hydrolysis at individual subunits of an archaeal clamp loader. EMBO J. 23, 1360-1371 (Pubitemid 38525007)
    • (2004) EMBO Journal , vol.23 , Issue.6 , pp. 1360-1371
    • Seybert, A.1    Wigley, D.B.2
  • 14
    • 77956538398 scopus 로고    scopus 로고
    • Only one ATP-binding DnaX subunit is required for initiation complex formation by the Escherichia coli DNA polymerase III holoenzyme
    • Wieczorek, A., Downey, C. D., Dallmann, H. G., and McHenry, C. S. (2010) Only one ATP-binding DnaX subunit is required for initiation complex formation by the Escherichia coli DNA polymerase III holoenzyme. J. Biol. Chem. 285, 29049-29053
    • (2010) J. Biol. Chem. , vol.285 , pp. 29049-29053
    • Wieczorek, A.1    Downey, C.D.2    Dallmann, H.G.3    McHenry, C.S.4
  • 15
    • 80052343292 scopus 로고    scopus 로고
    • Polymerase chaperoning and multiple ATPase sites enable the E. Coli DNA polymerase III holoenzyme to rapidly form initiation complexes
    • Downey, C. D., Crooke, E., and McHenry, C. S. (2011) Polymerase chaperoning and multiple ATPase sites enable the E. coli DNA polymerase III holoenzyme to rapidly form initiation complexes. J. Mol. Biol. 412, 340-353
    • (2011) J. Mol. Biol. , vol.412 , pp. 340-353
    • Downey, C.D.1    Crooke, E.2    McHenry, C.S.3
  • 17
    • 34147132697 scopus 로고    scopus 로고
    • A function for the ψ subunit in loading the Escherichia coli DNA polymerase sliding clamp
    • DOI 10.1074/jbc.M610136200
    • Anderson, S. G., Williams, C. R., O'donnell, M., and Bloom, L. B. (2007) A function for the ψ subunit in loading the Escherichia coli DNA polymerase sliding clamp. J. Biol. Chem. 282, 7035-7045 (Pubitemid 47093628)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.10 , pp. 7035-7045
    • Anderson, S.G.1    Williams, C.R.2    O'Donnell, M.3    Bloom, L.B.4
  • 18
    • 70149109582 scopus 로고    scopus 로고
    • Temporal correlation of DNA binding, ATP hydrolysis, and clamp release in the clamp loading reaction catalyzed by the Escherichia coli gamma complex
    • Anderson, S. G., Thompson, J. A., Paschall, C. O., O'Donnell, M., and Bloom, L. B. (2009) Temporal correlation of DNA binding, ATP hydrolysis, and clamp release in the clamp loading reaction catalyzed by the Escherichia coli gamma complex. Biochemistry 48, 8516-8527
    • (2009) Biochemistry , vol.48 , pp. 8516-8527
    • Anderson, S.G.1    Thompson, J.A.2    Paschall, C.O.3    O'Donnell, M.4    Bloom, L.B.5
  • 19
    • 0038353310 scopus 로고    scopus 로고
    • Overproduction and analysis of eukaryotic multiprotein complexes in Escherichia coli using a dual-vector strategy
    • DOI 10.1016/S0003-2697(03)00273-2
    • Finkelstein, J., Antony, E., Hingorani, M. M., and O'Donnell, M. (2003) Overproduction and analysis of eukaryotic multiprotein complexes in Escherichia coli using a dual-vector strategy. Anal. Biochem. 319, 78-87 (Pubitemid 36802145)
    • (2003) Analytical Biochemistry , vol.319 , Issue.1 , pp. 78-87
    • Finkelstein, J.1    Antony, E.2    Hingorani, M.M.3    O'Donnell, M.4
  • 20
    • 33745187598 scopus 로고    scopus 로고
    • Mechanism of proliferating cell nuclear antigen clamp opening by replication factor C
    • Yao, N. Y., Johnson, A., Bowman, G. D., Kuriyan, J., and O'Donnell, M. (2006) Mechanism of proliferating cell nuclear antigen clamp opening by replication factor C. J. Biol. Chem. 281, 17528-17539
    • (2006) J. Biol. Chem. , vol.281 , pp. 17528-17539
    • Yao, N.Y.1    Johnson, A.2    Bowman, G.D.3    Kuriyan, J.4    O'Donnell, M.5
  • 21
    • 33845922103 scopus 로고    scopus 로고
    • The replication factor C clamp loader requires arginine finger sensors to drive DNA binding and proliferating cell nuclear antigen loading
    • DOI 10.1074/jbc.M606090200
    • Johnson, A., Yao, N. Y., Bowman, G. D., Kuriyan, J., and O'Donnell, M. (2006) The replication factor C clamp loader requires arginine finger sensors to drive DNA binding and proliferating cell nuclear antigen loading. J. Biol. Chem. 281, 35531-35543 (Pubitemid 46036588)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.46 , pp. 35531-35543
    • Johnson, A.1    Yao, N.Y.2    Bowman, G.D.3    Kuriyan, J.4    O'Donnell, M.5
  • 22
    • 84863393472 scopus 로고    scopus 로고
    • Replication factor C is a more effective proliferating cell nuclear antigen (PCNA) opener than the checkpoint clamp loader, Rad24-RFC
    • Thompson, J. A., Marzahn, M. R., O'Donnell, M., and Bloom, L. B. (2012) Replication factor C is a more effective proliferating cell nuclear antigen (PCNA) opener than the checkpoint clamp loader, Rad24-RFC. J. Biol. Chem. 287, 2203-2209
    • (2012) J. Biol. Chem. , vol.287 , pp. 2203-2209
    • Thompson, J.A.1    Marzahn, M.R.2    O'Donnell, M.3    Bloom, L.B.4
  • 23
    • 0029001791 scopus 로고
    • A mutational analysis of the yeast proliferating cell nuclear antigen indicates distinct roles in DNA replication and DNA repair
    • Ayyagari, R., Impellizzeri, K. J., Yoder, B. L., Gary, S. L., and Burgers, P. M. (1995) A mutational analysis of the yeast proliferating cell nuclear antigen indicates distinct roles in DNA replication and DNA repair. Mol. Cell. Biol. 15, 4420-4429
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4420-4429
    • Ayyagari, R.1    Impellizzeri, K.J.2    Yoder, B.L.3    Gary, S.L.4    Burgers, P.M.5
  • 24
    • 0004124451 scopus 로고
    • The yeast analog of mammalian cyclin/proliferating-cell nuclear antigen interacts with mammalian DNA polymerase δ
    • Bauer, G. A., and Burgers, P. M. (1988) The yeast analog of mammalian cyclin/proliferating-cell nuclear antigen interacts with mammalian DNA polymerase δ. Proc. Natl. Acad. Sci. U.S.A. 85, 7506-7510
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 7506-7510
    • Bauer, G.A.1    Burgers, P.M.2
  • 25
    • 0347379847 scopus 로고    scopus 로고
    • Replication Factor C Clamp Loader Subunit Arrangement within the Circular Pentamer and Its Attachment Points to Proliferating Cell Nuclear Antigen
    • DOI 10.1074/jbc.M309206200
    • Yao, N., Coryell, L., Zhang, D., Georgescu, R. E., Finkelstein, J., Coman, M. M., Hingorani, M. M., and O'Donnell, M. (2003) Replication factor C clamp loader subunit arrangement within the circular pentamer and its attachment points to proliferating cell nuclear antigen. J. Biol. Chem. 278, 50744-50753 (Pubitemid 37548923)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.50 , pp. 50744-50753
    • Yao, N.1    Coryell, L.2    Zhang, D.3    Georgescu, R.E.4    Finkelstein, J.5    Coman, M.M.6    Hingorani, M.M.7    O'Donnell, M.8
  • 26
    • 84859769400 scopus 로고    scopus 로고
    • Improved solubility of replication factor C (RFC) Walker A mutants
    • Marzahn, M. R., and Bloom, L. B. (2012) Improved solubility of replication factor C (RFC) Walker A mutants. Protein Expr. Purif. 83, 135-144
    • (2012) Protein Expr. Purif. , vol.83 , pp. 135-144
    • Marzahn, M.R.1    Bloom, L.B.2
  • 27
    • 70450265205 scopus 로고    scopus 로고
    • A slow ATP-induced conformational change limits the rate of DNA binding but not the rate of β clamp binding by the Escherichia coli γ complex clamp loader
    • Thompson, J. A., Paschall, C. O., O'Donnell, M., and Bloom, L. B. (2009) A slow ATP-induced conformational change limits the rate of DNA binding but not the rate of β clamp binding by the Escherichia coli γ complex clamp loader. J. Biol. Chem. 284, 32147-32157
    • (2009) J. Biol. Chem. , vol.284 , pp. 32147-32157
    • Thompson, J.A.1    Paschall, C.O.2    O'Donnell, M.3    Bloom, L.B.4
  • 28
    • 35948947822 scopus 로고    scopus 로고
    • AAA+ ATPases: Achieving diversity of function with conserved machinery
    • DOI 10.1111/j.1600-0854.2007.00642.x
    • White, S. R., and Lauring, B. (2007) AAA+ ATPases: achieving diversity of function with conserved machinery. Traffic 8, 1657-1667 (Pubitemid 350066678)
    • (2007) Traffic , vol.8 , Issue.12 , pp. 1657-1667
    • White, S.R.1    Lauring, B.2
  • 31
    • 0026584599 scopus 로고
    • Structure of the recA protein-ADP complex
    • Story, R. M., and Steitz, T. A. (1992) Structure of the recA protein-ADP complex. Nature 355, 374-376
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 32
    • 64649100384 scopus 로고    scopus 로고
    • Mechanism of ATP-driven PCNA clamp loading by S. Cerevisiae RFC
    • Chen, S., Levin, M. K., Sakato, M., Zhou, Y., and Hingorani, M. M. (2009) Mechanism of ATP-driven PCNA clamp loading by S. cerevisiae RFC. J. Mol. Biol. 388, 431-442
    • (2009) J. Mol. Biol. , vol.388 , pp. 431-442
    • Chen, S.1    Levin, M.K.2    Sakato, M.3    Zhou, Y.4    Hingorani, M.M.5
  • 33
    • 84856425218 scopus 로고    scopus 로고
    • ATP binding and hydrolysis-driven rate-determining events in the RFC-catalyzed PCNA clamp loading reaction
    • Sakato, M., Zhou, Y., and Hingorani, M. M. (2012) ATP binding and hydrolysis-driven rate-determining events in the RFC-catalyzed PCNA clamp loading reaction. J. Mol. Biol. 416, 176-191
    • (2012) J. Mol. Biol. , vol.416 , pp. 176-191
    • Sakato, M.1    Zhou, Y.2    Hingorani, M.M.3
  • 34
    • 84875655174 scopus 로고    scopus 로고
    • A novel function for the conserved glutamate residue in the Walker B motif of replication factor C
    • Chiraniya, A., Finkelstein, J., O'Donnell, M., and Bloom, L. B. (2013) A novel function for the conserved glutamate residue in the Walker B motif of replication factor C. Genes 4, 134-151
    • (2013) Genes , vol.4 , pp. 134-151
    • Chiraniya, A.1    Finkelstein, J.2    O'Donnell, M.3    Bloom, L.B.4
  • 35
    • 0035860719 scopus 로고    scopus 로고
    • ATP utilization by yeast replication factor C: I. ATP-mediated interaction with DNA and with proliferating cell nuclear antigen
    • DOI 10.1074/jbc.M011631200
    • Gomes, X. V., and Burgers, P. M. (2001) 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 (Pubitemid 37384476)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.37 , pp. 34768-34775
    • Gomes, X.V.1    Burgers, P.M.J.2
  • 36
    • 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., and Benkovic, S. J. (2006) The structure of a ring-opened proliferating cell nuclear antigen-replication factor C complex revealed by fluorescence energy transfer. Proc. Natl. Acad. Sci. U.S.A. 103, 2546-2551
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 2546-2551
    • Zhuang, Z.1    Yoder, B.L.2    Burgers, P.M.3    Benkovic, S.J.4
  • 37
    • 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
    • DOI 10.1074/jbc.273.38.24550
    • Hingorani, M. M., and O'Donnell, M. (1998) 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 (Pubitemid 28454951)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.38 , pp. 24550-24563
    • Hingorani, M.M.1    O'Donnell, M.2
  • 38
    • 0033081486 scopus 로고    scopus 로고
    • The internal workings of a DNA polymerase clamp-loading machine
    • DOI 10.1093/emboj/18.3.771
    • Turner, J., Hingorani, M. M., Kelman, Z., and O'Donnell, M. (1999) The internal workings of a DNA polymerase clamp-loading machine. EMBO J. 18, 771-783 (Pubitemid 29057262)
    • (1999) EMBO Journal , vol.18 , Issue.3 , pp. 771-783
    • Turner, J.1    Hingorani, M.M.2    Kelman, Z.3    O'Donnell, M.4
  • 39
    • 33749033347 scopus 로고    scopus 로고
    • The replication clamp-loading machine at work in the three domains of life
    • DOI 10.1038/nrm2022, PII NRM2022
    • Indiani, C., and O'Donnell, M. (2006) The replication clamp-loading machine at work in the three domains of life. Nat. Rev. Mol. Cell Biol. 7, 751-761 (Pubitemid 44450459)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.10 , pp. 751-761
    • Indiani, C.1    O'Donnell, M.2
  • 40
    • 1542682737 scopus 로고    scopus 로고
    • Archaeal DNA Replication: Eukaryal Proteins in a Bacterial Context
    • DOI 10.1146/annurev.micro.57.030502.090709
    • Grabowski, B., and Kelman, Z. (2003) Archeal DNA replication: eukaryal proteins in a bacterial context. Annu. Rev. Microbiol. 57, 487-516 (Pubitemid 37392953)
    • (2003) Annual Review of Microbiology , vol.57 , pp. 487-516
    • Grabowski, B.1    Kelman, Z.2
  • 41
    • 84858124467 scopus 로고    scopus 로고
    • DNA replication fork proteins
    • Hübscher, U. (2009) DNA replication fork proteins. Methods Mol. Biol. 521, 19-33
    • (2009) Methods Mol. Biol. , vol.521 , pp. 19-33
    • Hübscher, U.1
  • 42
    • 79959431646 scopus 로고    scopus 로고
    • DNA replicases from a bacterial perspective
    • McHenry, C. S. (2011) DNA replicases from a bacterial perspective. Annu. Rev. Biochem. 80, 403-436
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 403-436
    • McHenry, C.S.1
  • 43
    • 0035860728 scopus 로고    scopus 로고
    • ATP utilization by yeast replication factor C. IV. RFC ATP-binding mutants show defects in DNA replication, DNA repair, and checkpoint regulation
    • Schmidt, S. L., Pautz, A. L., and Burgers, P. M. (2001) ATP utilization by yeast replication factor C. IV. RFC ATP-binding mutants show defects in DNA replication, DNA repair, and checkpoint regulation. J. Biol. Chem. 276, 34792-34800
    • (2001) J. Biol. Chem. , vol.276 , pp. 34792-34800
    • Schmidt, S.L.1    Pautz, A.L.2    Burgers, P.M.3
  • 44
    • 0032557559 scopus 로고    scopus 로고
    • Functional interactions among the subunits of replication factor C potentiate and modulate its ATPase activity
    • DOI 10.1074/jbc.273.21.12935
    • Podust, V. N., Tiwari, N., Ott, R., and Fanning, E. (1998) Functional interactions among the subunits of replication factor C potentiate and modulate its ATPase activity. J. Biol. Chem. 273, 12935-12942 (Pubitemid 28246854)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.21 , pp. 12935-12942
    • Podust, V.N.1    Tiwari, N.2    Ott, R.3    Fanning, E.4
  • 45
    • 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., and Burgers, P. M. (2001) 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) J. Biol. Chem. , vol.276 , pp. 34776-34783
    • Gomes, X.V.1    Schmidt, S.L.2    Burgers, P.M.3
  • 46
    • 84859914242 scopus 로고    scopus 로고
    • Clamp loader ATPases and the evolution of DNA replication machinery
    • Kelch, B. A., Makino, D. L., O'Donnell, M., and Kuriyan, J. (2012) Clamp loader ATPases and the evolution of DNA replication machinery. BMC Biol. 10, 34
    • (2012) BMC Biol. , vol.10 , pp. 34
    • Kelch, B.A.1    Makino, D.L.2    O'Donnell, M.3    Kuriyan, J.4
  • 47
    • 0030986962 scopus 로고    scopus 로고
    • Deletion analysis of the large subunit p140 in human replication factor C reveals regions required for complex formation and replication activities
    • DOI 10.1074/jbc.272.15.10058
    • Uhlmann, F., Cai, J., Gibbs, E., O'Donnell, M., and Hurwitz, J. (1997) Deletion analysis of the large subunit p140 in human replication factor C reveals regions required for complex formation and replication activities. J. Biol. Chem. 272, 10058-10064 (Pubitemid 27171680)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.15 , pp. 10058-10064
    • Uhlmann, F.1    Cai, J.2    Gibbs, E.3    O'Donnell, M.4    Hurwitz, J.5
  • 48
    • 0033610922 scopus 로고    scopus 로고
    • Replication factor C disengages from proliferating cell nuclear antigen (PCNA) upon sliding clamp formation, and PCNA itself tethers dna polymerase delta to DNA
    • DOI 10.1074/jbc.273.48.31992
    • Podust, V. N., Tiwari, N., Stephan, S., and Fanning, E. (1998) Replication factor C disengages from proliferating cell nuclear antigen (PCNA) upon sliding clamp formation, and PCNA itself tethers DNA polymerase delta to DNA. J. Biol. Chem. 273, 31992-31999 (Pubitemid 29177139)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.48 , pp. 31992-31999
    • Podust, V.N.1    Tiwari, N.2    Stephan, S.3    Fanning, E.4
  • 49
    • 0034640522 scopus 로고    scopus 로고
    • Overproduction in Escherichia coli and characterization of yeast replication factor C lacking the ligase homology domain
    • DOI 10.1074/jbc.275.19.14541
    • Gomes, X. V., Gary, S. L., and Burgers, P. M. (2000) Overproduction in Escherichia coli and characterization of yeast replication factor C lacking the ligase homology domain. J. Biol. Chem. 275, 14541-14549 (Pubitemid 30339743)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.19 , pp. 14541-14549
    • Gomes, X.V.1    Gary, S.L.2    Burgers, P.M.J.3
  • 50
    • 84856447919 scopus 로고    scopus 로고
    • A central swivel point in the RFC clamp loader controls PCNA opening and loading on DNA
    • Sakato, M., O'Donnell, M., and Hingorani, M. M. (2012) A central swivel point in the RFC clamp loader controls PCNA opening and loading on DNA. J. Mol. Biol. 416, 163-175
    • (2012) J. Mol. Biol. , vol.416 , pp. 163-175
    • Sakato, M.1    O'Donnell, M.2    Hingorani, M.M.3
  • 51
    • 84455163347 scopus 로고    scopus 로고
    • How a DNA polymerase clamp loader opens a sliding clamp
    • Kelch, B. A., Makino, D. L., O'Donnell, M., and Kuriyan, J. (2011) How a DNA polymerase clamp loader opens a sliding clamp. Science 334, 1675-1680
    • (2011) Science , vol.334 , pp. 1675-1680
    • Kelch, B.A.1    Makino, D.L.2    O'Donnell, M.3    Kuriyan, J.4
  • 52
    • 77952796820 scopus 로고    scopus 로고
    • Recognition of the ring-opened state of proliferating cell nuclear antigen by replication factor C promotes eukaryotic clamp-loading
    • Tainer, J. A., McCammon, J. A., and Ivanov, I. (2010) Recognition of the ring-opened state of proliferating cell nuclear antigen by replication factor C promotes eukaryotic clamp-loading. J. Am. Chem. Soc. 132, 7372-7378
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 7372-7378
    • Tainer, J.A.1    McCammon, J.A.2    Ivanov, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.