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Volumn 37, Issue 4, 2010, Pages 481-491

Chaperoning of a Replicative Polymerase onto a Newly Assembled DNA-Bound Sliding Clamp by the Clamp Loader

Author keywords

DNA

Indexed keywords

DNA POLYMERASE; SINGLE STRANDED DNA;

EID: 76849107748     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2010.01.013     Document Type: Article
Times cited : (34)

References (45)
  • 1
    • 0034696523 scopus 로고    scopus 로고
    • Tracking sliding clamp opening and closing during bacteriophage T4 DNA polymerase holoenzyme assembly
    • Alley S.C., Abel-Santos E., and Benkovic S.J. Tracking sliding clamp opening and closing during bacteriophage T4 DNA polymerase holoenzyme assembly. Biochemistry 39 (2000) 3076-3090
    • (2000) Biochemistry , vol.39 , pp. 3076-3090
    • Alley, S.C.1    Abel-Santos, E.2    Benkovic, S.J.3
  • 2
    • 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., Bertram J.G., Hingorani M.M., Beechem J.M., O'Donnell M.E., Goodman M.F., and Bloom L.B. 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 (2000) 3006-3015
    • (2000) J. Biol. Chem. , vol.275 , pp. 3006-3015
    • Ason, B.1    Bertram, J.G.2    Hingorani, M.M.3    Beechem, J.M.4    O'Donnell, M.E.5    Goodman, M.F.6    Bloom, L.B.7
  • 3
    • 0032544709 scopus 로고    scopus 로고
    • Pre-steady state analysis of the assembly of wild type and mutant circular clamps of Escherichia coli DNA polymerase III onto DNA
    • Bertram J.G., Bloom L.B., Turner J., O'Donnell M.E., Beechem J.M., and Goodman M.F. Pre-steady state analysis of the assembly of wild type and mutant circular clamps of Escherichia coli DNA polymerase III onto DNA. J. Biol. Chem. 273 (1998) 24564-24574
    • (1998) J. Biol. Chem. , vol.273 , pp. 24564-24574
    • Bertram, J.G.1    Bloom, L.B.2    Turner, J.3    O'Donnell, M.E.4    Beechem, J.M.5    Goodman, M.F.6
  • 4
    • 0027280149 scopus 로고
    • The Escherichia coli DNA polymerase III holoenzyme contains both products of the dnaX gene, τ and γ, but only τ is essential
    • Blinkova A., Hervas C., Stukenberg P.T., Onrust R., O'Donnell M.E., and Walker J.R. The Escherichia coli DNA polymerase III holoenzyme contains both products of the dnaX gene, τ and γ, but only τ is essential. J. Bacteriol. 175 (1993) 6018-6027
    • (1993) J. Bacteriol. , vol.175 , pp. 6018-6027
    • Blinkova, A.1    Hervas, C.2    Stukenberg, P.T.3    Onrust, R.4    O'Donnell, M.E.5    Walker, J.R.6
  • 5
    • 63549113890 scopus 로고    scopus 로고
    • Loading clamps for DNA replication and repair
    • Bloom L.B. Loading clamps for DNA replication and repair. DNA Repair (Amst.) 8 (2009) 570-578
    • (2009) DNA Repair (Amst.) , vol.8 , pp. 570-578
    • Bloom, L.B.1
  • 6
    • 0034666303 scopus 로고    scopus 로고
    • The DNA replication machine of a Gram-positive organism
    • Bruck I., and O'Donnell M.E. The DNA replication machine of a Gram-positive organism. J. Biol. Chem. 275 (2000) 28971-28983
    • (2000) J. Biol. Chem. , vol.275 , pp. 28971-28983
    • Bruck, I.1    O'Donnell, M.E.2
  • 7
    • 0037066746 scopus 로고    scopus 로고
    • A three-domain structure for the δ subunit of the DNA polymerase III holoenzyme δ domain III binds δ′ and assembles into the DnaX complex
    • Bullard J.M., Pritchard A.E., Song M.S., Glover B.P., Wieczorek A., Chen J., Janjic N., and McHenry C.S. A three-domain structure for the δ subunit of the DNA polymerase III holoenzyme δ domain III binds δ′ and assembles into the DnaX complex. J. Biol. Chem. 277 (2002) 13246-13256
    • (2002) J. Biol. Chem. , vol.277 , pp. 13246-13256
    • Bullard, J.M.1    Pritchard, A.E.2    Song, M.S.3    Glover, B.P.4    Wieczorek, A.5    Chen, J.6    Janjic, N.7    McHenry, C.S.8
  • 8
    • 0023726103 scopus 로고
    • Mammalian cyclin/PCNA (DNA polymerase δ auxilliary protein) stimulates processive DNA synthesis by yeast DNA polymerase III
    • Burgers P.M.J. Mammalian cyclin/PCNA (DNA polymerase δ auxilliary protein) stimulates processive DNA synthesis by yeast DNA polymerase III. Nucleic Acids Res. 16 (1988) 6297-6307
    • (1988) Nucleic Acids Res. , vol.16 , pp. 6297-6307
    • Burgers, P.M.J.1
  • 10
    • 0019428380 scopus 로고
    • Size classes of products synthesized processively by DNA polymerase III and DNA polymerase III holoenzyme of Escherichia coli
    • Fay P.J., Johanson K.O., McHenry C.S., and Bambara R.A. Size classes of products synthesized processively by DNA polymerase III and DNA polymerase III holoenzyme of Escherichia coli. J. Biol. Chem. 256 (1981) 976-983
    • (1981) J. Biol. Chem. , vol.256 , pp. 976-983
    • Fay, P.J.1    Johanson, K.O.2    McHenry, C.S.3    Bambara, R.A.4
  • 11
    • 0035830834 scopus 로고    scopus 로고
    • τ binds and organizes Escherichia coli replication proteins through distinct domains. Domain IV, located within the unique C terminus of τ, binds the replication fork helicase, DnaB
    • Gao D., and McHenry C.S. τ binds and organizes Escherichia coli replication proteins through distinct domains. Domain IV, located within the unique C terminus of τ, binds the replication fork helicase, DnaB. J. Biol. Chem. 276 (2001) 4441-4446
    • (2001) J. Biol. Chem. , vol.276 , pp. 4441-4446
    • Gao, D.1    McHenry, C.S.2
  • 12
    • 0035830939 scopus 로고    scopus 로고
    • τ binds and organizes Escherichia coli replication proteins 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., and McHenry C.S. τ binds and organizes Escherichia coli replication proteins 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 (2001) 4433-4440
    • (2001) J. Biol. Chem. , vol.276 , pp. 4433-4440
    • Gao, D.1    McHenry, C.S.2
  • 13
    • 0032483511 scopus 로고    scopus 로고
    • The χψ subunits of DNA polymerase III holoenzyme bind to single-stranded DNA-binding protein (SSB) and facilitate replication of a SSB-coated template
    • Glover B.P., and McHenry C.S. The χψ subunits of DNA polymerase III holoenzyme bind to single-stranded DNA-binding protein (SSB) and facilitate replication of a SSB-coated template. J. Biol. Chem. 273 (1998) 23476-23484
    • (1998) J. Biol. Chem. , vol.273 , pp. 23476-23484
    • Glover, B.P.1    McHenry, C.S.2
  • 14
    • 0034603089 scopus 로고    scopus 로고
    • The DnaX-binding subunits δ′ and ψ are bound to γ and not τ in the DNA polymerase III holoenzyme
    • Glover B.P., and McHenry C.S. The DnaX-binding subunits δ′ and ψ are bound to γ and not τ in the DNA polymerase III holoenzyme. J. Biol. Chem. 275 (2000) 3017-3020
    • (2000) J. Biol. Chem. , vol.275 , pp. 3017-3020
    • Glover, B.P.1    McHenry, C.S.2
  • 15
    • 0035967930 scopus 로고    scopus 로고
    • The DNA polymerase III holoenzyme: an asymmetric dimeric replicative complex with leading and lagging strand polymerases
    • Glover B.P., and McHenry C.S. The DNA polymerase III holoenzyme: an asymmetric dimeric replicative complex with leading and lagging strand polymerases. Cell 105 (2001) 925-934
    • (2001) Cell , vol.105 , pp. 925-934
    • Glover, B.P.1    McHenry, C.S.2
  • 16
    • 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., and O'Donnell M.E. ATP binding to the Escherichia coli clamp loader powers opening of the ring-shaped clamp of DNA polymerase III holoenzyme. J. Biol. Chem. 273 (1998) 24550-24563
    • (1998) J. Biol. Chem. , vol.273 , pp. 24550-24563
    • Hingorani, M.M.1    O'Donnell, M.E.2
  • 17
    • 34248647207 scopus 로고    scopus 로고
    • SSB protein limits RecOR binding onto single-stranded DNA
    • Hobbs M.D., Sakai A., and Cox M.M. SSB protein limits RecOR binding onto single-stranded DNA. J. Biol. Chem. 282 (2007) 11058-11067
    • (2007) J. Biol. Chem. , vol.282 , pp. 11058-11067
    • Hobbs, M.D.1    Sakai, A.2    Cox, M.M.3
  • 18
    • 0035943342 scopus 로고    scopus 로고
    • Crystal structure of the processivity clamp loader gamma complex of E. coli DNA polymerase III
    • Jeruzalmi D., O'Donnell M.E., and Kuriyan J. Crystal structure of the processivity clamp loader gamma complex of E. coli DNA polymerase III. Cell 106 (2001) 429-441
    • (2001) Cell , vol.106 , pp. 429-441
    • Jeruzalmi, D.1    O'Donnell, M.E.2    Kuriyan, J.3
  • 19
    • 0020441919 scopus 로고
    • The β subunit of the DNA polymerase III holoenzyme becomes inaccessible to antibody after formation of an initiation complex with primed DNA
    • Johanson K.O., and McHenry C.S. The β subunit of the DNA polymerase III holoenzyme becomes inaccessible to antibody after formation of an initiation complex with primed DNA. J. Biol. Chem. 257 (1982) 12310-12315
    • (1982) J. Biol. Chem. , vol.257 , pp. 12310-12315
    • Johanson, K.O.1    McHenry, C.S.2
  • 20
    • 0021249446 scopus 로고
    • Adenosine 5′-O-(3-thiotriphosphate) can support the formation of an initiation complex between the DNA polymerase III holoenzyme and primed DNA
    • Johanson K.O., and McHenry C.S. Adenosine 5′-O-(3-thiotriphosphate) can support the formation of an initiation complex between the DNA polymerase III holoenzyme and primed DNA. J. Biol. Chem. 259 (1984) 4589-4595
    • (1984) J. Biol. Chem. , vol.259 , pp. 4589-4595
    • Johanson, K.O.1    McHenry, C.S.2
  • 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
    • Johnson A., Yao N.Y., Bowman G.D., Kuriyan J., and O'Donnell M. The replication factor C clamp loader requires arginine finger sensors to drive DNA binding and proliferating cell nuclear antigen loading. J. Biol. Chem. 281 (2006) 35531-35543
    • (2006) J. Biol. Chem. , vol.281 , pp. 35531-35543
    • Johnson, A.1    Yao, N.Y.2    Bowman, G.D.3    Kuriyan, J.4    O'Donnell, M.5
  • 22
    • 0030064447 scopus 로고    scopus 로고
    • Dual role of the 44/62 protein as a matchmaker protein and DNA polymerase chaperone during assembly of the bacteriophage T4 holoenzyme complex
    • Kaboord B.F., and Benkovic S.J. Dual role of the 44/62 protein as a matchmaker protein and DNA polymerase chaperone during assembly of the bacteriophage T4 holoenzyme complex. Biochemistry 35 (1996) 1084-1092
    • (1996) Biochemistry , vol.35 , pp. 1084-1092
    • Kaboord, B.F.1    Benkovic, S.J.2
  • 23
    • 0032522760 scopus 로고    scopus 로고
    • Devoted to the lagging strand-the χ subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly
    • Kelman Z., Yuzhakov A., Andjelkovic J., and O'Donnell M.E. Devoted to the lagging strand-the χ subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly. EMBO J. 17 (1998) 2436-2449
    • (1998) EMBO J. , vol.17 , pp. 2436-2449
    • Kelman, Z.1    Yuzhakov, A.2    Andjelkovic, J.3    O'Donnell, M.E.4
  • 24
    • 0000178199 scopus 로고    scopus 로고
    • Biotin tagging deletion analysis of domain limits involved in protein-macromolecular interactions: mapping the τ binding domain of the DNA polymerase III α subunit
    • Kim D.R., and McHenry C.S. Biotin tagging deletion analysis of domain limits involved in protein-macromolecular interactions: mapping the τ binding domain of the DNA polymerase III α subunit. J. Biol. Chem. 271 (1996) 20690-20698
    • (1996) J. Biol. Chem. , vol.271 , pp. 20690-20698
    • Kim, D.R.1    McHenry, C.S.2
  • 25
    • 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., and Marians K.J. Coupling of a replicative polymerase and helicase: a τ-DnaB interaction mediates rapid replication fork movement. Cell 84 (1996) 643-650
    • (1996) Cell , vol.84 , pp. 643-650
    • Kim, S.1    Dallmann, H.G.2    McHenry, C.S.3    Marians, K.J.4
  • 26
    • 0029839057 scopus 로고    scopus 로고
    • τ couples the leading- and lagging-strand polymerases at the Escherichia coli DNA replication fork
    • Kim S., Dallmann H.G., McHenry C.S., and Marians K.J. τ couples the leading- and lagging-strand polymerases at the Escherichia coli DNA replication fork. J. Biol. Chem. 271 (1996) 21406-21412
    • (1996) J. Biol. Chem. , vol.271 , pp. 21406-21412
    • Kim, S.1    Dallmann, H.G.2    McHenry, C.S.3    Marians, K.J.4
  • 27
    • 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., and Marians K.J. τ protects β in the leading-strand polymerase complex at the replication fork. J. Biol. Chem. 271 (1996) 4315-4318
    • (1996) J. Biol. Chem. , vol.271 , pp. 4315-4318
    • Kim, S.1    Dallmann, H.G.2    McHenry, C.S.3    Marians, K.J.4
  • 28
    • 0022878685 scopus 로고
    • The β subunit of the Escherichia coli DNA polymerase III holoenzyme interacts functionally with the catalytic core in the absence of other subunits
    • LaDuca R.J., Crute J.J., McHenry C.S., and Bambara R.A. The β subunit of the Escherichia coli DNA polymerase III holoenzyme interacts functionally with the catalytic core in the absence of other subunits. J. Biol. Chem. 261 (1986) 7550-7557
    • (1986) J. Biol. Chem. , vol.261 , pp. 7550-7557
    • LaDuca, R.J.1    Crute, J.J.2    McHenry, C.S.3    Bambara, R.A.4
  • 29
    • 0034652208 scopus 로고    scopus 로고
    • Nonlinearity in genetic decoding: homologous DNA replicase genes use alternatives of transcriptional slippage or translational frameshifting
    • Larsen B., Wills N.M., Nelson C., Atkins J.F., and Gesteland R.F. Nonlinearity in genetic decoding: homologous DNA replicase genes use alternatives of transcriptional slippage or translational frameshifting. Proc. Natl. Acad. Sci. USA 97 (2000) 1683-1688
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1683-1688
    • Larsen, B.1    Wills, N.M.2    Nelson, C.3    Atkins, J.F.4    Gesteland, R.F.5
  • 30
    • 0037292424 scopus 로고    scopus 로고
    • Mechanism of the E. coli τ processivity switch during lagging-strand synthesis
    • Leu F.P., Georgescu R., and O'Donnell M.E. Mechanism of the E. coli τ processivity switch during lagging-strand synthesis. Mol. Cell 11 (2003) 315-327
    • (2003) Mol. Cell , vol.11 , pp. 315-327
    • Leu, F.P.1    Georgescu, R.2    O'Donnell, M.E.3
  • 31
    • 0028246888 scopus 로고
    • Escherichia coli single-stranded DNA-binding protein: multiple DNA-binding modes and cooperativities
    • Lohman T.M., and Ferrari M. Escherichia coli single-stranded DNA-binding protein: multiple DNA-binding modes and cooperativities. Annu. Rev. Biochem. 63 (1994) 527-570
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 527-570
    • Lohman, T.M.1    Ferrari, M.2
  • 32
    • 11144266855 scopus 로고    scopus 로고
    • The PCNA-RFC families of DNA clamps and clamp loaders
    • Majka J., and Burgers P.M. The PCNA-RFC families of DNA clamps and clamp loaders. Prog. Nucleic Acid Res. Mol. Biol. 78 (2004) 227-260
    • (2004) Prog. Nucleic Acid Res. Mol. Biol. , vol.78 , pp. 227-260
    • Majka, J.1    Burgers, P.M.2
  • 33
    • 0020478712 scopus 로고
    • Purfication and characterization of DNA polymerase III′: identification of τ as a subunit of the DNA polymerase III holoenzyme
    • McHenry C.S. Purfication and characterization of DNA polymerase III′: identification of τ as a subunit of the DNA polymerase III holoenzyme. J. Biol. Chem. 257 (1982) 2657-2663
    • (1982) J. Biol. Chem. , vol.257 , pp. 2657-2663
    • McHenry, C.S.1
  • 34
    • 0018786252 scopus 로고
    • DNA polymerase III of Escherichia coli: purification and identification of subunits
    • McHenry C.S., and Crow W. DNA polymerase III of Escherichia coli: purification and identification of subunits. J. Biol. Chem. 254 (1979) 1748-1753
    • (1979) J. Biol. Chem. , vol.254 , pp. 1748-1753
    • McHenry, C.S.1    Crow, W.2
  • 35
    • 0033593355 scopus 로고    scopus 로고
    • Identification of the acidic residues in the active site of DNA polymerase III
    • Pritchard A.E., and McHenry C.S. Identification of the acidic residues in the active site of DNA polymerase III. J. Mol. Biol. 285 (1999) 1067-1080
    • (1999) J. Mol. Biol. , vol.285 , pp. 1067-1080
    • Pritchard, A.E.1    McHenry, C.S.2
  • 36
    • 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., and 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 (1996) 10291-10298
    • (1996) J. Biol. Chem. , vol.271 , pp. 10291-10298
    • Pritchard, A.E.1    Dallmann, H.G.2    McHenry, C.S.3
  • 37
    • 34248664689 scopus 로고    scopus 로고
    • Dynamic structural rearrangements between DNA binding modes of E. coli SSB protein
    • Roy R., Kozlov A.G., Lohman T.M., and Ha T. Dynamic structural rearrangements between DNA binding modes of E. coli SSB protein. J. Mol. Biol. 369 (2007) 1244-1257
    • (2007) J. Mol. Biol. , vol.369 , pp. 1244-1257
    • Roy, R.1    Kozlov, A.G.2    Lohman, T.M.3    Ha, T.4
  • 38
    • 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.J. 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 (2001) 34784-34791
    • (2001) J. Biol. Chem. , vol.276 , pp. 34784-34791
    • Schmidt, S.L.1    Gomes, X.V.2    Burgers, P.M.J.3
  • 41
    • 0035860749 scopus 로고    scopus 로고
    • The δ and δ′ subunits of the DNA polymerase III holoenzyme are essential for initiation complex formation and processive elongation
    • Song M.S., Pham P.T., Olson M., Carter J.R., Franden M.A., Schaaper R.M., and McHenry C.S. The δ and δ′ subunits of the DNA polymerase III holoenzyme are essential for initiation complex formation and processive elongation. J. Biol. Chem. 276 (2001) 35165-35175
    • (2001) J. Biol. Chem. , vol.276 , pp. 35165-35175
    • Song, M.S.1    Pham, P.T.2    Olson, M.3    Carter, J.R.4    Franden, M.A.5    Schaaper, R.M.6    McHenry, C.S.7
  • 42
    • 0025988893 scopus 로고
    • Constitution of the twin polymerase of DNA polymerase III holoenzyme
    • Studwell-Vaughan P.S., and O'Donnell M.E. Constitution of the twin polymerase of DNA polymerase III holoenzyme. J. Biol. Chem. 266 (1991) 19833-19841
    • (1991) J. Biol. Chem. , vol.266 , pp. 19833-19841
    • Studwell-Vaughan, P.S.1    O'Donnell, M.E.2
  • 43
    • 0029788209 scopus 로고    scopus 로고
    • The interaction between helicase and primase sets the replication fork clock
    • Tougu K., and Marians K.J. The interaction between helicase and primase sets the replication fork clock. J. Biol. Chem. 271 (1996) 21398-21405
    • (1996) J. Biol. Chem. , vol.271 , pp. 21398-21405
    • Tougu, K.1    Marians, K.J.2
  • 44
    • 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.E., and 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 (2003) 4376-4385
    • (2003) J. Biol. Chem. , vol.279 , pp. 4376-4385
    • Williams, C.R.1    Snyder, A.K.2    Kuzmic, P.3    O'Donnell, M.E.4    Bloom, L.B.5
  • 45
    • 0043163774 scopus 로고    scopus 로고
    • DNA polymerase III χ subunit ties single-stranded DNA binding protein to the bacterial replication machinery
    • Witte G., Urbanke C., and Curth U. DNA polymerase III χ subunit ties single-stranded DNA binding protein to the bacterial replication machinery. Nucleic Acids Res. 31 (2003) 4434-4440
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4434-4440
    • Witte, G.1    Urbanke, C.2    Curth, U.3


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