메뉴 건너뛰기




Volumn 79, Issue 5, 2011, Pages 1325-1338

A phage-encoded inhibitor of Escherichia coli DNA replication targets the DNA polymerase clamp loader

Author keywords

[No Author keywords available]

Indexed keywords

DNA DIRECTED DNA POLYMERASE GAMMA; DNA POLYMERASE III HOLOENZYME; GENE PRODUCT; HOLOENZYME; PROTEIN N4 GP8; REPLISOME; UNCLASSIFIED DRUG;

EID: 79951809315     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2010.07526.x     Document Type: Article
Times cited : (23)

References (41)
  • 1
    • 34147132697 scopus 로고    scopus 로고
    • A function for the psi subunit in loading the Escherichia coli DNA polymerase sliding clamp
    • Anderson, S.G., Williams, C.R., O'Donnell, M., and Bloom, L.B. (2007) A function for the psi subunit in loading the Escherichia coli DNA polymerase sliding clamp. J Biol Chem 282: 7035-7045.
    • (2007) J Biol Chem , vol.282 , pp. 7035-7045
    • Anderson, S.G.1    Williams, C.R.2    O'Donnell, M.3    Bloom, L.B.4
  • 2
    • 33750456998 scopus 로고    scopus 로고
    • Competition of bacteriophage polypeptides with native replicase proteins for binding to the DNA sliding clamp reveals a novel mechanism for DNA replication arrest in Staphylococcus aureus
    • Belley, A., Callejo, M., Arhin, F., Dehbi, M., Fadhil, I., Liu, J., etal. (2006) Competition of bacteriophage polypeptides with native replicase proteins for binding to the DNA sliding clamp reveals a novel mechanism for DNA replication arrest in Staphylococcus aureus. Mol Microbiol 62: 1132-1143.
    • (2006) Mol Microbiol , vol.62 , pp. 1132-1143
    • Belley, A.1    Callejo, M.2    Arhin, F.3    Dehbi, M.4    Fadhil, I.5    Liu, J.6
  • 3
    • 0037066746 scopus 로고    scopus 로고
    • A three-domain structure for the delta subunit of the DNA polymerase III holoenzyme: delta domain III binds delta' and assembles into the DnaX complex
    • Bullard, J.M., Pritchard, A.E., Song, M.-S., Glover, B.P., Wieczorek, A., Chen, J., etal. (2002) A three-domain structure for the delta subunit of the DNA polymerase III holoenzyme: delta domain III binds delta' and assembles into the DnaX complex. J Biol Chem 277: 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
  • 4
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A., and Wanner, B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97: 6640-6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 5
    • 0016204182 scopus 로고
    • Bacterial cell division regulation: characterization of the dnaH locus of Escherichia coli
    • Filip, C.C., Allen, J.S., Gustafson, R.A., Allen, R.G., and Walker, J.R. (1974) Bacterial cell division regulation: characterization of the dnaH locus of Escherichia coli. J Bacteriol 119: 443-449.
    • (1974) J Bacteriol , vol.119 , pp. 443-449
    • Filip, C.C.1    Allen, J.S.2    Gustafson, R.A.3    Allen, R.G.4    Walker, J.R.5
  • 6
    • 0032483511 scopus 로고    scopus 로고
    • The chi-psi 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., and McHenry, C.S. (1998) The chi-psi 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) J Biol Chem , vol.273 , pp. 23476-23484
    • Glover, B.P.1    McHenry, C.S.2
  • 7
    • 0022641001 scopus 로고
    • Host and phage-coded functions required for coliphage N4 DNA replication
    • Guinta, D., Stambouly, J., Falco, S.C., Rist, J.K., and Rothman-Denes, L.B. (1986) Host and phage-coded functions required for coliphage N4 DNA replication. Virology 150: 33-44.
    • (1986) Virology , vol.150 , pp. 33-44
    • Guinta, D.1    Stambouly, J.2    Falco, S.C.3    Rist, J.K.4    Rothman-Denes, L.B.5
  • 8
    • 40549103080 scopus 로고    scopus 로고
    • Introduction of conditional lethal amber mutations in Escherichia coli
    • Herring, C.D. (2008) Introduction of conditional lethal amber mutations in Escherichia coli. Methods Mol Biol 416: 323-334.
    • (2008) Methods Mol Biol , vol.416 , pp. 323-334
    • Herring, C.D.1
  • 9
    • 0016837338 scopus 로고
    • Inactive complex formation between E. coli RNA polymerase and inhibitor protein purified from T7 phage infected cells
    • Hesselbach, B.A., and Nakada, D. (1975) Inactive complex formation between E. coli RNA polymerase and inhibitor protein purified from T7 phage infected cells. Nature 258: 354-357.
    • (1975) Nature , vol.258 , pp. 354-357
    • Hesselbach, B.A.1    Nakada, D.2
  • 10
    • 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. (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.
    • (1998) J Biol Chem , vol.273 , pp. 24550-24563
    • Hingorani, M.M.1    O'Donnell, M.2
  • 11
    • 0347004717 scopus 로고    scopus 로고
    • Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling
    • Ignatova, Z., and Gierasch, L.M. (2004) Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling. Proc Natl Acad Sci USA 101: 523-528.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 523-528
    • Ignatova, Z.1    Gierasch, L.M.2
  • 12
    • 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., Yurieva, O., Zhao, Y., Young, M., Stewart, J., Hingorani, M., etal. (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
  • 13
    • 0026717535 scopus 로고
    • Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp
    • Kong, X.-P., Onrust, R., O'Donnell, M., and Kuriyan, J. (1992) Three-dimensional structure of the beta 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
  • 14
    • 0023187031 scopus 로고
    • Escherichia coli DnaX product, the tau subunit of DNA polymerase III, is a multifunctional protein with single-stranded DNA-dependent ATPase activity
    • Lee, S.-H., and Walker, J.R. (1987) Escherichia coli DnaX product, the tau subunit of DNA polymerase III, is a multifunctional protein with single-stranded DNA-dependent ATPase activity. Proc Natl Acad Sci USA 84: 2713-2717.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 2713-2717
    • Lee, S.-H.1    Walker, J.R.2
  • 15
    • 0034602163 scopus 로고    scopus 로고
    • The delta subunit of DNA polymerase III holoenzyme serves as a sliding clamp unloader in Escherichia coli
    • Leu, F.P., Hingorani, M.M., Turner, J., and O'Donnell, M. (2000) The delta subunit of DNA polymerase III holoenzyme serves as a sliding clamp unloader in Escherichia coli. J Biol Chem 275: 34609-34618.
    • (2000) J Biol Chem , vol.275 , pp. 34609-34618
    • Leu, F.P.1    Hingorani, M.M.2    Turner, J.3    O'Donnell, M.4
  • 16
    • 0023812678 scopus 로고
    • Purification and characterization of bacteriophage N4-induced DNA polymerase
    • Lindberg, G.K., Rist, J.K., Kunkel, T.A., Sugino, A., and Rothman-Denes, L.B. (1988) Purification and characterization of bacteriophage N4-induced DNA polymerase. J Biol Chem 263: 11319-11326.
    • (1988) J Biol Chem , vol.263 , pp. 11319-11326
    • Lindberg, G.K.1    Rist, J.K.2    Kunkel, T.A.3    Sugino, A.4    Rothman-Denes, L.B.5
  • 17
  • 18
    • 0023957528 scopus 로고
    • Cloning and generation of a genetic map of bacteriophage N4 DNA
    • Malone, C., Spellman, S., Hyman, D., and Rothman-Denes, L.B. (1988) Cloning and generation of a genetic map of bacteriophage N4 DNA. Virology 162: 328-336.
    • (1988) Virology , vol.162 , pp. 328-336
    • Malone, C.1    Spellman, S.2    Hyman, D.3    Rothman-Denes, L.B.4
  • 19
    • 0003842951 scopus 로고
    • A Short Course in Bacterial Genetics: A Laboratory Manual and Handbook for Escherichia coli and Related Bacteria
    • Plainview, NY: Cold Spring Harbor Laboratory Press.
    • Miller, J.H. (1992) A Short Course in Bacterial Genetics: A Laboratory Manual and Handbook for Escherichia coli and Related Bacteria. Plainview, NY: Cold Spring Harbor Laboratory Press.
    • (1992)
    • Miller, J.H.1
  • 20
    • 0033022148 scopus 로고    scopus 로고
    • Inhibition of Escherichia coli RNA polymerase by bacteriophage T7 gene 2 protein
    • Nechaev, S., and Severinov, K. (1999) Inhibition of Escherichia coli RNA polymerase by bacteriophage T7 gene 2 protein. J Mol Biol 289: 815-826.
    • (1999) J Mol Biol , vol.289 , pp. 815-826
    • Nechaev, S.1    Severinov, K.2
  • 21
    • 0033994310 scopus 로고    scopus 로고
    • The interaction of bacteriophage P2 protein with Escherichia coli DnaB helicase
    • Odegrip, R., Schoen, S., Haggård-Ljungquist, E., Park, K., and Chattoraj, D. (2000) The interaction of bacteriophage P2 protein with Escherichia coli DnaB helicase. J Virol 74: 4057-4063.
    • (2000) J Virol , vol.74 , pp. 4057-4063
    • Odegrip, R.1    Schoen, S.2    Haggård-Ljungquist, E.3    Park, K.4    Chattoraj, D.5
  • 22
    • 33744950932 scopus 로고    scopus 로고
    • Replisome architecture and dynamics in Escherichia coli
    • O'Donnell, M. (2006) Replisome architecture and dynamics in Escherichia coli. J Biol Chem 281: 10653-10656.
    • (2006) J Biol Chem , vol.281 , pp. 10653-10656
    • O'Donnell, M.1
  • 23
    • 0027298689 scopus 로고
    • DNA polymerase III accessory proteins. II. Characterization of delta and delta
    • Onrust, R., and O'Donnell, M. (1993) DNA polymerase III accessory proteins. II. Characterization of delta and delta. J Biol Chem 268: 11766-11772.
    • (1993) J Biol Chem , vol.268 , pp. 11766-11772
    • Onrust, R.1    O'Donnell, M.2
  • 24
    • 0029058292 scopus 로고
    • Assembly of a chromosomal replication machine: two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. I. Organization of the clamp loader
    • Onrust, R., Finkelstein, J., Naktinis, V., Turner, J., Fang, L., and O'Donnell, M. (1995) Assembly of a chromosomal replication machine: two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. I. Organization of the clamp loader. J Biol Chem 270: 13348-13357.
    • (1995) J Biol Chem , vol.270 , pp. 13348-13357
    • Onrust, R.1    Finkelstein, J.2    Naktinis, V.3    Turner, J.4    Fang, L.5    O'Donnell, M.6
  • 25
    • 0016434157 scopus 로고
    • Host DNA degradation after infection of Escherichia coli with bacteriophage T4: dependence of the alternate pathway of degradation which occurs in the absence of both T4 endonuclease II and nuclear disruption on T4 endonuclease IV
    • Parson, K.A., and Snustad, D.P. (1975) Host DNA degradation after infection of Escherichia coli with bacteriophage T4: dependence of the alternate pathway of degradation which occurs in the absence of both T4 endonuclease II and nuclear disruption on T4 endonuclease IV. J Virol 15: 221-224.
    • (1975) J Virol , vol.15 , pp. 221-224
    • Parson, K.A.1    Snustad, D.P.2
  • 26
    • 0016148847 scopus 로고
    • Novel transcribing activities in N4-infected Escherichia coli
    • Rothman-Denes, L.B., and Schito, G.C. (1974) Novel transcribing activities in N4-infected Escherichia coli. Virology 60: 65-72.
    • (1974) Virology , vol.60 , pp. 65-72
    • Rothman-Denes, L.B.1    Schito, G.C.2
  • 27
    • 0015418650 scopus 로고
    • Selective shutoff of catabolite-sensitive host syntheses by coliphage N4
    • Rothman-Denes, L.B., Haselkorn, R., and Schito, G.C. (1972) Selective shutoff of catabolite-sensitive host syntheses by coliphage N4. Virology 50: 95-102.
    • (1972) Virology , vol.50 , pp. 95-102
    • Rothman-Denes, L.B.1    Haselkorn, R.2    Schito, G.C.3
  • 28
    • 79951810463 scopus 로고
    • Fate of the host chromosome during N4 coliphage replication
    • Satta, G., Pesce, A., and Schito, G.C. (1969) Fate of the host chromosome during N4 coliphage replication. G Microbiol 17: 131-139.
    • (1969) G Microbiol , vol.17 , pp. 131-139
    • Satta, G.1    Pesce, A.2    Schito, G.C.3
  • 29
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa
    • Schagger, H., and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa. Anal Biochem 166: 368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 30
    • 0015845848 scopus 로고
    • The genetics and physiology of coliphage N4
    • Schito, G.C. (1973) The genetics and physiology of coliphage N4. Virology 55: 254-265.
    • (1973) Virology , vol.55 , pp. 254-265
    • Schito, G.C.1
  • 31
    • 0015944563 scopus 로고
    • Development of coliphage N4: ultrastructural studies
    • Schito, G.C. (1974) Development of coliphage N4: ultrastructural studies. J Virol 13: 186-196.
    • (1974) J Virol , vol.13 , pp. 186-196
    • Schito, G.C.1
  • 32
    • 79951810287 scopus 로고
    • Sintesi macromolecolari in cellule infettate con il colifago N4. Estratto da atti del XV Congresso Nazionale di Micrologia, Societa' Italiana di Microbiologia.
    • Schito, G.C., Satta, G., Pesce, A., and Romanzi, C.A. (1969) Sintesi macromolecolari in cellule infettate con il colifago N4. Estratto da atti del XV Congresso Nazionale di Micrologia, Societa' Italiana di Microbiologia.
    • (1969)
    • Schito, G.C.1    Satta, G.2    Pesce, A.3    Romanzi, C.A.4
  • 33
    • 0035844990 scopus 로고    scopus 로고
    • Cell toxicity caused by products of the p(L) operon of bacteriophage lambda
    • Sergueev, K., Yu, D., Austin, S., and Court, D. (2001) Cell toxicity caused by products of the p(L) operon of bacteriophage lambda. Gene 272: 227-235.
    • (2001) Gene , vol.272 , pp. 227-235
    • Sergueev, K.1    Yu, D.2    Austin, S.3    Court, D.4
  • 34
    • 0036438807 scopus 로고    scopus 로고
    • E. coli cell-cycle regulation by bacteriophage lambda
    • Sergueev, K., Court, D., Reaves, L., and Austin, S. (2002) E. coli cell-cycle regulation by bacteriophage lambda. J Mol Biol 324: 297-307.
    • (2002) J Mol Biol , vol.324 , pp. 297-307
    • Sergueev, K.1    Court, D.2    Reaves, L.3    Austin, S.4
  • 35
    • 65549110769 scopus 로고    scopus 로고
    • The mechanism of ATP-dependent primer-template recognition by a clamp loader complex
    • Simonetta, K.R., Kazmirski, S.L., Goedken, E.R., Cantor, A.J., Kelch, B.A., McNally, R., etal. (2009) The mechanism of ATP-dependent primer-template recognition by a clamp loader complex. Cell 137: 659-671.
    • (2009) Cell , vol.137 , pp. 659-671
    • Simonetta, K.R.1    Kazmirski, S.L.2    Goedken, E.R.3    Cantor, A.J.4    Kelch, B.A.5    McNally, R.6
  • 36
    • 69849085776 scopus 로고    scopus 로고
    • Roles of genes 38, 39 and 40 in shutoff of host biosynthesis during infection of Bacillus subtilis by bacteriophage SPO1
    • Stewart, C.R., Yip, T.K.S., Myles, B., and Laughlin, L. (2009) Roles of genes 38, 39 and 40 in shutoff of host biosynthesis during infection of Bacillus subtilis by bacteriophage SPO1. Virology 392: 271-274.
    • (2009) Virology , vol.392 , pp. 271-274
    • Stewart, C.R.1    Yip, T.K.S.2    Myles, B.3    Laughlin, L.4
  • 37
    • 0025809742 scopus 로고
    • Mechanism of the sliding beta-clamp of DNA polymerase III holoenzyme
    • Stukenberg, P.T., Studwell-Vaughan, P.S., and O'Donnell, M. (1991) Mechanism of the sliding beta-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
  • 38
    • 0043163774 scopus 로고    scopus 로고
    • DNA polymerase III chi subunit ties single-stranded DNA binding protein to the bacterial replication machinery
    • Witte, G., Urbanke, C., and Curth, U. (2003) DNA polymerase III chi subunit ties single-stranded DNA binding protein to the bacterial replication machinery. Nucleic Acids Res 31: 4434-4440.
    • (2003) Nucleic Acids Res , vol.31 , pp. 4434-4440
    • Witte, G.1    Urbanke, C.2    Curth, U.3
  • 39
    • 67649173541 scopus 로고    scopus 로고
    • Genome sequences of two novel phages infecting marine roseobacters
    • Zhao, Y., Wang, K., Jiao, N., and Chen, F. (2009) Genome sequences of two novel phages infecting marine roseobacters. Environ Microbiol 11: 2055-2064.
    • (2009) Environ Microbiol , vol.11 , pp. 2055-2064
    • Zhao, Y.1    Wang, K.2    Jiao, N.3    Chen, F.4
  • 40
    • 0018935420 scopus 로고
    • Physical map of coliphage N4 DNA
    • Zivin, R., Malone, C., and Rothman-Denes, L.B. (1980) Physical map of coliphage N4 DNA. Virology 104: 205-218.
    • (1980) Virology , vol.104 , pp. 205-218
    • Zivin, R.1    Malone, C.2    Rothman-Denes, L.B.3
  • 41
    • 0019839124 scopus 로고
    • Transcriptional map of bacteriophage N4. Location and polarity of N4 RNAs
    • Zivin, R., Zehring, W., and Rothman-Denes, L.B. (1981) Transcriptional map of bacteriophage N4. Location and polarity of N4 RNAs. J Mol Biol 152: 335-356.
    • (1981) J Mol Biol , vol.152 , pp. 335-356
    • Zivin, R.1    Zehring, W.2    Rothman-Denes, L.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.