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Volumn 188, Issue 15, 2006, Pages 5501-5509

The plasmid RK2 replication initiator protein (TrfA) binds to the sliding clamp β subunit of DNA polymerase III: Implication for the toxicity of a peptide derived from the amino-terminal portion of 33-kilodalton TrfA

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; DNA DIRECTED DNA POLYMERASE GAMMA; MUTANT PROTEIN; PROTEIN HDA; PROTEIN TRFA; REPLICATION INITIATOR PROTEIN DNAA; UNCLASSIFIED DRUG;

EID: 33746621720     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00231-06     Document Type: Article
Times cited : (26)

References (42)
  • 1
    • 28844501027 scopus 로고    scopus 로고
    • Overexpression of the Hda DnaA-related protein in Escherichia coli inhibits multiplication, affects membrane permeability, and induces the SOS response
    • Banack, T., N. Clauson, N. Ogbaa, J. Villar, D. Olver, and W. Firshein. 2005. Overexpression of the Hda DnaA-related protein in Escherichia coli inhibits multiplication, affects membrane permeability, and induces the SOS response. J. Bacteriol. 187:8507-8510.
    • (2005) J. Bacteriol. , vol.187 , pp. 8507-8510
    • Banack, T.1    Clauson, N.2    Ogbaa, N.3    Villar, J.4    Olver, D.5    Firshein, W.6
  • 2
    • 0041922662 scopus 로고    scopus 로고
    • Intracellular expression of peptide fusions for demonstration of protein essentiality in bacteria
    • Benson, R. E., E. B. Gottlin, D. J. Christensen, and P. T. Hamilton. 2003. Intracellular expression of peptide fusions for demonstration of protein essentiality in bacteria. Antimicrob. Agents Chemother. 47:2875-2881.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 2875-2881
    • Benson, R.E.1    Gottlin, E.B.2    Christensen, D.J.3    Hamilton, P.T.4
  • 3
    • 0242389787 scopus 로고    scopus 로고
    • Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB to the β-clamp
    • Bunting, K. A., S. M. Roe, and L. H. Pearl. 2003. Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB to the β-clamp. EMBO J. 22:5883-5892.
    • (2003) EMBO J. , vol.22 , pp. 5883-5892
    • Bunting, K.A.1    Roe, S.M.2    Pearl, L.H.3
  • 4
    • 0346654081 scopus 로고    scopus 로고
    • Structural and biochemical analysis of sliding clamp/ligand interactions suggest a competitive between replicative and translesion polymerases
    • Burnouf, D. Y., V. Olieric, J. Wagner, S. Fujii, J. Reinbolt, R. P. Fuchs, and P. Dumas. 2004. Structural and biochemical analysis of sliding clamp/ligand interactions suggest a competitive between replicative and translesion polymerases. J. Mol. Biol. 30:1187-1197.
    • (2004) J. Mol. Biol. , vol.30 , pp. 1187-1197
    • Burnouf, D.Y.1    Olieric, V.2    Wagner, J.3    Fujii, S.4    Reinbolt, J.5    Fuchs, R.P.6    Dumas, P.7
  • 5
    • 0037628613 scopus 로고    scopus 로고
    • Controlled initiation of chromosome replication in Escherichia coli requires functional Hda protein
    • Camara, J. E., K. Skarstad, and E. Crooke. 2003. Controlled initiation of chromosome replication in Escherichia coli requires functional Hda protein. J. Bacteriol. 185:3244-3248.
    • (2003) J. Bacteriol. , vol.185 , pp. 3244-3248
    • Camara, J.E.1    Skarstad, K.2    Crooke, E.3
  • 6
    • 29744460566 scopus 로고    scopus 로고
    • Hda inactivation of DnaA is the predominant mechanism preventing hyperinitiation of Escherichia coli DNA replication
    • Camara, J. E., A. M. Breier, T. Brendler, S. Austin, N. R. Cozzarelli, and E. Crooke. 2005. Hda inactivation of DnaA is the predominant mechanism preventing hyperinitiation of Escherichia coli DNA replication. EMBO Rep. 6:736-741.
    • (2005) EMBO Rep. , vol.6 , pp. 736-741
    • Camara, J.E.1    Breier, A.M.2    Brendler, T.3    Austin, S.4    Cozzarelli, N.R.5    Crooke, E.6
  • 7
    • 0035949599 scopus 로고    scopus 로고
    • A universal protein-protein interaction motif in the eubacterial DNA replication and repair systems
    • Dalrymple, B. P., K. Kongsuwan, G. Wijffels, N. E. Dixon, and P. A. Jennings. 2001. A universal protein-protein interaction motif in the eubacterial DNA replication and repair systems. Proc. Natl. Acad. Sci. USA 98:11627-11632.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11627-11632
    • Dalrymple, B.P.1    Kongsuwan, K.2    Wijffels, G.3    Dixon, N.E.4    Jennings, P.A.5
  • 8
    • 20444420519 scopus 로고    scopus 로고
    • A bipartite polymerase-processivity factor interaction: Only the internal β binding site of the α subunit is required for processive replication by the DNA polymerase III holoenzyme
    • Dohrmann, P. R., and C. S. McHenry. 2005. A bipartite polymerase-processivity factor interaction: only the internal β binding site of the α subunit is required for processive replication by the DNA polymerase III holoenzyme. J. Mol. Biol. 350:228-239.
    • (2005) J. Mol. Biol. , vol.350 , pp. 228-239
    • Dohrmann, P.R.1    McHenry, C.S.2
  • 9
    • 0026055711 scopus 로고
    • Broad-host-range properties of plasmid RK2: Importance of overlapping genes encoding the plasmid replication initiation protein TrfA
    • Fang, F. C., and D. R. Helinski. 1991. Broad-host-range properties of plasmid RK2: importance of overlapping genes encoding the plasmid replication initiation protein TrfA. J. Bacteriol. 173:5861-5868.
    • (1991) J. Bacteriol. , vol.173 , pp. 5861-5868
    • Fang, F.C.1    Helinski, D.R.2
  • 10
    • 0035943399 scopus 로고    scopus 로고
    • Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III
    • Jeruzalmi, D., O. Yurieva, Y. Zhao, M. Young, J. Stewart, M. Hingorani, M. O'Donnell, and J. Kuriyan. 2001. Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III. Cell 106:417-428.
    • (2001) Cell , vol.106 , pp. 417-428
    • Jeruzalmi, D.1    Yurieva, O.2    Zhao, Y.3    Young, M.4    Stewart, J.5    Hingorani, M.6    O'Donnell, M.7    Kuriyan, J.8
  • 11
    • 0032504050 scopus 로고    scopus 로고
    • The initiator function of DnaA protein is negatively regulated by the sliding clamp of the E. coli chromosome replicase
    • Katayama, T., T. Kubota, K. Kurokawa, E. Crooke, and K. Sekimizu. 1998. The initiator function of DnaA protein is negatively regulated by the sliding clamp of the E. coli chromosome replicase. Cell 94:61-71.
    • (1998) Cell , vol.94 , pp. 61-71
    • Katayama, T.1    Kubota, T.2    Kurokawa, K.3    Crooke, E.4    Sekimizu, K.5
  • 12
    • 0032710590 scopus 로고    scopus 로고
    • Inactivation of Escherichia coli DnaA protein by DNA polymerase III and negative regulations for initiation of chromosomal replication
    • Katayama, T., and K. Sekimizu. 1999. Inactivation of Escherichia coli DnaA protein by DNA polymerase III and negative regulations for initiation of chromosomal replication. Biochimie 81:835-840.
    • (1999) Biochimie , vol.81 , pp. 835-840
    • Katayama, T.1    Sekimizu, K.2
  • 13
    • 0035111073 scopus 로고    scopus 로고
    • Multiple pathways regulating DnaA function in Escherichia coli: Distinct roles for DnaA titration by the datA locus and the regulatory inactivation of DnaA
    • Katayama, T., K. Fujimitsu, and T. Ogawa. 2001. Multiple pathways regulating DnaA function in Escherichia coli: distinct roles for DnaA titration by the datA locus and the regulatory inactivation of DnaA. Biochimie 83:13-17.
    • (2001) Biochimie , vol.83 , pp. 13-17
    • Katayama, T.1    Fujimitsu, K.2    Ogawa, T.3
  • 14
    • 0035422651 scopus 로고    scopus 로고
    • Hda, a novel DnaA-related protein, regulates the replication cycle in Escherichia coli
    • Kato, J., and T. Katayama. 2001. Hda, a novel DnaA-related protein, regulates the replication cycle in Escherichia coli. EMBO J. 20:4253-4262.
    • (2001) EMBO J. , vol.20 , pp. 4253-4262
    • Kato, J.1    Katayama, T.2
  • 15
    • 13744252890 scopus 로고    scopus 로고
    • MAFFT version 5: Improvement in accuracy of multiple sequence alignment
    • Katoh, K., K. Kuma, H. Toh, and T. Miyata. 2005. MAFFT version 5: improvement in accuracy of multiple sequence alignment. Nucleic Acids Res. 33:511-518.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 511-518
    • Katoh, K.1    Kuma, K.2    Toh, H.3    Miyata, T.4
  • 16
    • 0034072524 scopus 로고    scopus 로고
    • Identification of a potential membrane targeting region of the replication initiation protein (TrfA) of broad host range plasmid RK2
    • Kim, P. D., T. M. Rosche, and W. Firshein. 2000. Identification of a potential membrane targeting region of the replication initiation protein (TrfA) of broad host range plasmid RK2. Plasmid 43:214-222.
    • (2000) Plasmid , vol.43 , pp. 214-222
    • Kim, P.D.1    Rosche, T.M.2    Firshein, W.3
  • 17
    • 0037334858 scopus 로고    scopus 로고
    • Identification of a novel membrane-associated gene product that suppresses toxicity of a TrfA peptide from plasmid RK2 and its relationship to the DnaA host initiation protein
    • Kim, P. D., T. Banack, D. M. Lerman, J. C. Tracy, J. E. Camara, E. Crooke, D. Oliver, and W. Firshein. 2003. Identification of a novel membrane-associated gene product that suppresses toxicity of a TrfA peptide from plasmid RK2 and its relationship to the DnaA host initiation protein. J. Bacteriol. 185:1817-1824.
    • (2003) J. Bacteriol. , vol.185 , pp. 1817-1824
    • Kim, P.D.1    Banack, T.2    Lerman, D.M.3    Tracy, J.C.4    Camara, J.E.5    Crooke, E.6    Oliver, D.7    Firshein, W.8
  • 18
    • 0032190630 scopus 로고    scopus 로고
    • Negative control of replication inhibition by a novel chromosomal locus exhibiting exceptional affinity for Escherichia coli DnaA protein
    • Kitagawa, R., T. Ozaki, S. Moriya, and T. Ogawa. 1998. Negative control of replication inhibition by a novel chromosomal locus exhibiting exceptional affinity for Escherichia coli DnaA protein. Genes Dev. 12:3032-3304.
    • (1998) Genes Dev. , vol.12 , pp. 3032-3304
    • Kitagawa, R.1    Ozaki, T.2    Moriya, S.3    Ogawa, T.4
  • 19
    • 0025979746 scopus 로고
    • Iteron inhibition of plasmid RK2 replication in vitro: Evidence for intermolecular coupling of replication origins as a mechanism for RK2 replication control
    • Kittel, B. L., and D. R. Helinski. 1991. Iteron inhibition of plasmid RK2 replication in vitro: evidence for intermolecular coupling of replication origins as a mechanism for RK2 replication control. Proc. Natl. Acad. Sci. USA 88:1389-1393.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1389-1393
    • Kittel, B.L.1    Helinski, D.R.2
  • 20
    • 0026717535 scopus 로고
    • Three-dimensional structure of the β subunit of E. coli DNA polymerase III holoenzyme: A sliding DNA clamp
    • Kong, X.-P., R. Onrust, M. O'Donnell, and J. Kuriyan. 1992. Three-dimensional structure of the β subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp. Cell 69:425-437.
    • (1992) Cell , vol.69 , pp. 425-437
    • Kong, X.-P.1    Onrust, R.2    O'Donnell, M.3    Kuriyan, J.4
  • 21
    • 0031467674 scopus 로고    scopus 로고
    • Helicase delivery and activation by DnaA and TrfA proteins during the initiation of replication of the broad host range plasmid RK2
    • Konieczny, I., and D. R. Helinski. 1997. Helicase delivery and activation by DnaA and TrfA proteins during the initiation of replication of the broad host range plasmid RK2. J. Biol. Chem. 272:33312-33318.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33312-33318
    • Konieczny, I.1    Helinski, D.R.2
  • 22
    • 0030792096 scopus 로고    scopus 로고
    • Role of TrfA and DnaA proteins in origin opening during initiation of DNA replication of the broad host range plasmid RK2
    • Konieczny, I., K. S. Doran, D. R. Helinski, and A. Blasina. 1997. Role of TrfA and DnaA proteins in origin opening during initiation of DNA replication of the broad host range plasmid RK2. J. Biol. Chem. 272:20173-20178.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20173-20178
    • Konieczny, I.1    Doran, K.S.2    Helinski, D.R.3    Blasina, A.4
  • 24
    • 2442504231 scopus 로고    scopus 로고
    • Interaction of the sliding clamp β-subunit and Hda, a DnaA related protein
    • Kurz, M., B. Dalrymple, G. Wijffels, and K. Kongsuwan. 2004. Interaction of the sliding clamp β-subunit and Hda, a DnaA related protein. J. Bacteriol. 186:3508-3515.
    • (2004) J. Bacteriol. , vol.186 , pp. 3508-3515
    • Kurz, M.1    Dalrymple, B.2    Wijffels, G.3    Kongsuwan, K.4
  • 25
    • 0036171550 scopus 로고    scopus 로고
    • The processivity factor beta controls DNA polymerase IV traffic during spontaneous mutagenesis and translesion synthesis in vivo
    • Lenne-Samuel, N., J. Wagner, H. Etienne, and R. P. Fuchs. 2002. The processivity factor beta controls DNA polymerase IV traffic during spontaneous mutagenesis and translesion synthesis in vivo. EMBO Rep. 3:45-49.
    • (2002) EMBO Rep. , vol.3 , pp. 45-49
    • Lenne-Samuel, N.1    Wagner, J.2    Etienne, H.3    Fuchs, R.P.4
  • 26
    • 0035902496 scopus 로고    scopus 로고
    • Interaction of the beta sliding clamp with MutS, ligase and DNA polymerase I
    • López de Saro, F. J., and M. O'Donnell. 2001. Interaction of the beta sliding clamp with MutS, ligase and DNA polymerase I. Proc. Natl. Acad. Sci. USA 98:8376-8380.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8376-8380
    • De López Saro, F.J.1    O'Donnell, M.2
  • 27
    • 0348134870 scopus 로고    scopus 로고
    • Competitive processivity-clamp usage by DNA polymerases during DNA replication and repair
    • López de Saro, F. J., R. E. Georgescu, M. F. Goodman, and M. O'Donnell. 2003. Competitive processivity-clamp usage by DNA polymerases during DNA replication and repair. EMBO J. 22:6408-6418.
    • (2003) EMBO J. , vol.22 , pp. 6408-6418
    • De López Saro, F.J.1    Georgescu, R.E.2    Goodman, M.F.3    O'Donnell, M.4
  • 28
    • 0028219947 scopus 로고
    • SeqA, a negative modulator of replication initiation in E. coli
    • Lu, M., J. L. Campbell, E. Boye, and N. Kleckner. 1994. SeqA, a negative modulator of replication initiation in E. coli. Cell 77:413-426.
    • (1994) Cell , vol.77 , pp. 413-426
    • Lu, M.1    Campbell, J.L.2    Boye, E.3    Kleckner, N.4
  • 29
    • 0030070111 scopus 로고    scopus 로고
    • A molecular switch in a replication machine defined by an internal competition for protein rings
    • Naktinis, V., J. Turner, and M. O'Donnell. 1996. A molecular switch in a replication machine defined by an internal competition for protein rings. Cell 84:137-145.
    • (1996) Cell , vol.84 , pp. 137-145
    • Naktinis, V.1    Turner, J.2    O'Donnell, M.3
  • 31
    • 0036015656 scopus 로고    scopus 로고
    • The datA locus predominantly contributes to the initiator titration mechanism in the control of replication initiation in Escherichia coli
    • Ogawa, T., Y. Yamada, T. Kuroda, T. Kishi, and S. Moriya. 2002. The datA locus predominantly contributes to the initiator titration mechanism in the control of replication initiation in Escherichia coli. Mol. Microbiol. 44:1367-1375.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1367-1375
    • Ogawa, T.1    Yamada, Y.2    Kuroda, T.3    Kishi, T.4    Moriya, S.5
  • 32
    • 0023665145 scopus 로고
    • Hemimethylation prevents DNA replication E. coli
    • Russell, D. W., and N. D. Zinder. 1987. Hemimethylation prevents DNA replication E. coli. Cell 50:1071-1079.
    • (1987) Cell , vol.50 , pp. 1071-1079
    • Russell, D.W.1    Zinder, N.D.2
  • 33
    • 0028325333 scopus 로고
    • The initiator protein DnaA: Evolution, properties, and function
    • Skarstad, K., and E. Boye. 1994. The initiator protein DnaA: evolution, properties, and function. Biochim. Biophys. Acta 1217:111-120.
    • (1994) Biochim. Biophys. Acta , vol.1217 , pp. 111-120
    • Skarstad, K.1    Boye, E.2
  • 34
    • 0021690245 scopus 로고
    • Nucleotide sequence of the trfA gene of broad host range plasmid RK2
    • Smith, C. A., and C. M. Thomas. 1984. Nucleotide sequence of the trfA gene of broad host range plasmid RK2. J. Mol. Biol. 175:251-262.
    • (1984) J. Mol. Biol. , vol.175 , pp. 251-262
    • Smith, C.A.1    Thomas, C.M.2
  • 35
    • 0025809742 scopus 로고
    • Mechanism of the sliding β-clamp of DNA polymerase III holoenzyme
    • Stukenberg, P. T., P. S. Studwell-Vaughan, and M. O'Donnell. 1991. Mechanism of the sliding β-clamp of DNA polymerase III holoenzyme. J. Biol. Chem. 266:11328-11334.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11328-11334
    • Stukenberg, P.T.1    Studwell-Vaughan, P.S.2    O'Donnell, M.3
  • 36
    • 3042815929 scopus 로고    scopus 로고
    • Molecular mechanism of DNA replication-coupled inactivation of the initiator protein in Escherichia coli: Interaction of DnaA with the sliding clamp-loaded DNA and the sliding clamp-Hda complex
    • Su'etsugu, M., M. Takata, T. Kubota, Y. Matsuda, and T. Katayama. 2004. Molecular mechanism of DNA replication-coupled inactivation of the initiator protein in Escherichia coli: interaction of DnaA with the sliding clamp-loaded DNA and the sliding clamp-Hda complex. Genes Cells 9:509-522.
    • (2004) Genes Cells , vol.9 , pp. 509-522
    • Su'Etsugu, M.1    Takata, M.2    Kubota, T.3    Matsuda, Y.4    Katayama, T.5
  • 37
    • 4944228029 scopus 로고    scopus 로고
    • The Escherichia coli dnaN159 mutant displays altered DNA polymerase usage and chronic SOS induction
    • Sutton, M. D. 2004. The Escherichia coli dnaN159 mutant displays altered DNA polymerase usage and chronic SOS induction. J. Bacteriol. 286:6738-6748.
    • (2004) J. Bacteriol. , vol.286 , pp. 6738-6748
    • Sutton, M.D.1
  • 38
    • 0037117539 scopus 로고    scopus 로고
    • Posttranslational modification of the umuD-encoded subunit of Escherichia coli DNA polymerase V regulates its interactions with the β processivity clamp
    • Sutton, M. D., I. Narumi, and G. C. Walker. 2002. Posttranslational modification of the umuD-encoded subunit of Escherichia coli DNA polymerase V regulates its interactions with the β processivity clamp. Proc. Natl. Acad. Sci. USA 99:5307-5312.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5307-5312
    • Sutton, M.D.1    Narumi, I.2    Walker, G.C.3
  • 39
    • 0033081486 scopus 로고    scopus 로고
    • The internal workings of a DNA polymerase clamp-loading machine
    • Turner, J., M. M. Hingorani, Z. Kelman, and M. O'Donnell. 1999. The internal workings of a DNA polymerase clamp-loading machine. EMBO J. 18:771-783.
    • (1999) EMBO J. , vol.18 , pp. 771-783
    • Turner, J.1    Hingorani, M.M.2    Kelman, Z.3    O'Donnell, M.4
  • 40
    • 0034574554 scopus 로고    scopus 로고
    • The β clamp targets DNA polymerase IV to DNA and strongly increases its processivity
    • Wagner, J., S. Fujii, P. Gruz, T. Nohmi, and R. P. P. Fuchs. 2000. The β clamp targets DNA polymerase IV to DNA and strongly increases its processivity. EMBO Rep. 1:484-488.
    • (2000) EMBO Rep. , vol.1 , pp. 484-488
    • Wagner, J.1    Fujii, S.2    Gruz, P.3    Nohmi, T.4    Fuchs, R.P.P.5
  • 42
    • 0037523309 scopus 로고    scopus 로고
    • The diverse spectrum of sliding clamp interacting proteins
    • Vivona, J. B., and Z. Kelman. 2003. The diverse spectrum of sliding clamp interacting proteins. FEBS Lett. 546:167-172.
    • (2003) FEBS Lett. , vol.546 , pp. 167-172
    • Vivona, J.B.1    Kelman, Z.2


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