메뉴 건너뛰기




Volumn 107, Issue 38, 2010, Pages 16548-16553

Viral terminal protein directs early organization of phage DNA replication at the bacterial nucleoid

Author keywords

Bacillus subtilis; Bacterial cytoskeleton; Dna polymerase; DNA binding; Phage 29

Indexed keywords

BACTERIOPHAGE DNA; DNA POLYMERASE; TERMINAL PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN; DNA DIRECTED DNA POLYMERASE; DNA TERMINAL PROTEIN, ENTEROBACTERIA PHAGE PRD1; HYBRID PROTEIN; TERMINAL PROTEIN, BACILLUS PHAGE PHI29; VIRUS DNA;

EID: 78049233242     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1010530107     Document Type: Article
Times cited : (34)

References (33)
  • 1
    • 0025815855 scopus 로고
    • Protein-priming of DNA replication
    • Salas M (1991) Protein-priming of DNA replication. Annu Rev Biochem 60:39-71.
    • (1991) Annu Rev Biochem , vol.60 , pp. 39-71
    • Salas, M.1
  • 2
    • 0033287841 scopus 로고    scopus 로고
    • Mechanisms of initiation of linear DNA replication in prokaryotes
    • Salas M (1999) Mechanisms of initiation of linear DNA replication in prokaryotes. Genet Eng (N Y) 21:159-171.
    • (1999) Genet Eng (N Y) , vol.21 , pp. 159-171
    • Salas, M.1
  • 4
    • 11144224991 scopus 로고    scopus 로고
    • ed Higgins NP (American Society for Microbiology Press, Washington, DC)
    • Chaconas G, Chen CW (2005) The Bacterial Chromosome, ed Higgins NP (American Society for Microbiology Press, Washington, DC), pp 525-539.
    • (2005) The Bacterial Chromosome , pp. 525-539
    • Chaconas, G.1    Chen, C.W.2
  • 5
    • 21644462488 scopus 로고    scopus 로고
    • Constituents of SH1, a novel lipid-containing virus infecting the halophilic euryarchaeon Haloarcula hispanica
    • Bamford DH, et al. (2005) Constituents of SH1, a novel lipid-containing virus infecting the halophilic euryarchaeon Haloarcula hispanica. J Virol 79:9097-9107.
    • (2005) J Virol , vol.79 , pp. 9097-9107
    • Bamford, D.H.1
  • 6
    • 33744929889 scopus 로고    scopus 로고
    • His1 and His2 are distantly related, spindle-shaped haloviruses belonging to the novel virus group, Salterprovirus
    • DOI 10.1016/j.virol.2006.02.005, PII S0042682206000870
    • Bath C, Cukalac T, Porter K, Dyall-Smith ML (2006) His1 and His2 are distantly related, spindle-shaped haloviruses belonging to the novel virus group, Salterprovirus. Virology 350:228-239. (Pubitemid 43850590)
    • (2006) Virology , vol.350 , Issue.1 , pp. 228-239
    • Bath, C.1    Cukalac, T.2    Porter, K.3    Dyall-Smith, M.L.4
  • 7
    • 34249726708 scopus 로고    scopus 로고
    • Genome of the Acidianus bottle-shaped virus and insights into the replication and packaging mechanisms
    • DOI 10.1016/j.virol.2007.03.005, PII S0042682207001481
    • Peng X, Basta T, Häring M, Garrett RA, Prangishvili D (2007) Genome of the Acidianus bottle-shaped virus and insights into the replication and packaging mechanisms. Virology 364:237-243. (Pubitemid 46829289)
    • (2007) Virology , vol.364 , Issue.1 , pp. 237-243
    • Peng, X.1    Basta, T.2    Haring, M.3    Garrett, R.A.4    Prangishvili, D.5
  • 8
    • 0023525929 scopus 로고
    • + ions on φ29 DNA-protein p3 replication: Formation of a complex between the terminal protein and the DNA polymerase
    • + ions on φ29 DNA-protein p3 replication: Formation of a complex between the terminal protein and the DNA polymerase. J Virol 61:3983-3991.
    • (1987) J Virol , vol.61 , pp. 3983-3991
    • Blanco, L.1
  • 9
    • 0031626930 scopus 로고    scopus 로고
    • Transcription activation and repression by interaction of a regulator with the α subunit of RNA polymerase: The model of phage φ29 protein p4
    • Rojo F, Mencía M, Monsalve M, Salas M (1998) Transcription activation and repression by interaction of a regulator with the α subunit of RNA polymerase: The model of phage φ29 protein p4. Prog Nucleic Acid Res Mol Biol 60:29-46.
    • (1998) Prog Nucleic Acid Res Mol Biol , vol.60 , pp. 29-46
    • Rojo, F.1    Mencía, M.2    Monsalve, M.3    Salas, M.4
  • 10
    • 33845619142 scopus 로고    scopus 로고
    • The bacterial actin-like cytoskeleton
    • Carballido-López R (2006) The bacterial actin-like cytoskeleton. Microbiol Mol Biol Rev 70:888-909.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 888-909
    • Carballido-López, R.1
  • 11
    • 69449090233 scopus 로고    scopus 로고
    • The actin-like MreB cytoskeleton organizes viral DNA replication in bacteria
    • Muñoz-Espín D, et al. (2009) The actin-like MreB cytoskeleton organizes viral DNA replication in bacteria. Proc Natl Acad Sci USA 106:13347-13352.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13347-13352
    • Muñoz-Espín, D.1
  • 12
    • 33645303495 scopus 로고    scopus 로고
    • The φ29 DNA polymerase:protein-primer structure suggests a model for the initiation to elongation transition
    • Kamtekar S, et al. (2006) The φ29 DNA polymerase:protein-primer structure suggests a model for the initiation to elongation transition. EMBO J 25:1335-1343.
    • (2006) EMBO J , vol.25 , pp. 1335-1343
    • Kamtekar, S.1
  • 13
    • 0024821323 scopus 로고
    • Functional domains in the bacteriophage φ29 terminal protein for interaction with the φ29 DNA polymerase and with DNA
    • Zaballos A, Salas M (1989) Functional domains in the bacteriophage φ29 terminal protein for interaction with the φ29 DNA polymerase and with DNA. Nucleic Acids Res 17:10353-10366. (Pubitemid 20012190)
    • (1989) Nucleic Acids Research , vol.17 , Issue.24 , pp. 10353-10366
    • Zaballos, A.1    Salas, M.2
  • 14
    • 0034704082 scopus 로고    scopus 로고
    • The putative coiled coil domain of the φ29 terminal protein is a major determinant involved in recognition of the origin of replication
    • DOI 10.1074/jbc.M007855200
    • Serna-Rico A, Illana B, Salas M, Meijer WJJ (2000) The putative coiled coil domain of the φ29 terminal protein is a major determinant involved in recognition of the origin of replication. J Biol Chem 275:40529-40538. (Pubitemid 32064690)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.51 , pp. 40529-40538
    • Serna-Rico, A.1    Illana, B.2    Salas, M.3    Meijer, W.J.J.4
  • 15
    • 0034640059 scopus 로고    scopus 로고
    • Specific recognation of parental terminal protein by DNA polymerase for initiation of protein-primed DNA replication
    • DOI 10.1074/jbc.M910058199
    • González-Huici V, Lázaro JM, Salas M, Hermoso JM (2000) Specific recognition of parental terminal protein by DNA polymerase for initiation of protein-primed DNA replication. J Biol Chem 275:14678-14683. (Pubitemid 30339759)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.19 , pp. 14678-14683
    • Gonzalez-Huici, V.1    Lazaro, J.M.2    Salas, M.3    Hermoso, J.M.4
  • 16
    • 4344592253 scopus 로고    scopus 로고
    • Binding of phage φ29 architectural protein p6 to the viral genome: Evidence for topological restriction of the phage linear DNA
    • DOI 10.1093/nar/gkh668
    • González-Huici V, Alcorlo M, Salas M, Hermoso JM (2004) Binding of phage φ29 architectural protein p6 to the viral genome: Evidence for topological restriction of the phage linear DNA. Nucleic Acids Res 32:3493-3502. (Pubitemid 39117466)
    • (2004) Nucleic Acids Research , vol.32 , Issue.11 , pp. 3493-3502
    • Gonzalez-Huici, V.1    Alcorlo, M.2    Salas, M.3    Hermoso, J.M.4
  • 18
    • 0141864658 scopus 로고    scopus 로고
    • Dysfunctional MreB inhibits chromosome segregation in Escherichia coli
    • DOI 10.1093/emboj/cdg504
    • Kruse T, Møller-Jensen J, Løbner-Olesen A, Gerdes K (2003) Dysfunctional MreB inhibits chromosome segregation in Escherichia coli. EMBO J 22:5283-5292. (Pubitemid 37222047)
    • (2003) EMBO Journal , vol.22 , Issue.19 , pp. 5283-5292
    • Kruse, T.1    Moeller-Jensen, J.2    Lobner-Olesen, A.3    Gerdes, K.4
  • 20
    • 13544274210 scopus 로고    scopus 로고
    • MreB actin-mediated segregation of a specific region of a bacterial chromosome
    • DOI 10.1016/j.cell.2005.01.007
    • Gitai Z, Dye NA, Reisenauer A, Wachi M, Shapiro L (2005) MreB actin-mediated segregation of a specific region of a bacterial chromosome. Cell 120:329-341. (Pubitemid 40222428)
    • (2005) Cell , vol.120 , Issue.3 , pp. 329-341
    • Gitai, Z.1    Dye, N.A.2    Reisenauer, A.3    Wachi, M.4    Shapiro, L.5
  • 21
    • 0242381270 scopus 로고    scopus 로고
    • Actin-like proteins MreB and Mbl from Bacillus subtilis are required for bipolar positioning of replication origins
    • Soufo HJ, Graumann PL (2003) Actin-like proteins MreB and Mbl from Bacillus subtilis are required for bipolar positioning of replication origins. Curr Biol 13:1916-1920.
    • (2003) Curr Biol , vol.13 , pp. 1916-1920
    • Soufo, H.J.1    Graumann, P.L.2
  • 22
    • 22944489133 scopus 로고    scopus 로고
    • Bacillus subtilis actin-like protein MreB influences the positioning of the replication machinery and requires membrane proteins MreC/D and other actin-like proteins for proper localization
    • Defeu Soufo HJ, Graumann PL (2005) Bacillus subtilis actin-like protein MreB influences the positioning of the replication machinery and requires membrane proteins MreC/D and other actin-like proteins for proper localization. BMC Cell Biol 6:10.
    • (2005) BMC Cell Biol , vol.6 , pp. 10
    • Defeu Soufo, H.J.1    Graumann, P.L.2
  • 23
    • 15944399775 scopus 로고    scopus 로고
    • A magnesium-dependent mreB null mutant: Implications for the role of mreB in Bacillus subtilis
    • DOI 10.1111/j.1365-2958.2005.04506.x
    • Formstone A, Errington J (2005) A magnesium-dependent mreB null mutant: Implications for the role of mreB in Bacillus subtilis. Mol Microbiol 55:1646-1657. (Pubitemid 40445203)
    • (2005) Molecular Microbiology , vol.55 , Issue.6 , pp. 1646-1657
    • Formstone, A.1    Errington, J.2
  • 24
    • 0025314719 scopus 로고
    • Adenovirus terminal protein mediates both nuclear matrix association and efficient transcription of adenovirus DNA
    • Schaack J, Ho WY, Freimuth P, Shenk T (1990) Adenovirus terminal protein mediates both nuclear matrix association and efficient transcription of adenovirus DNA. Genes Dev 4:1197-1208.
    • (1990) Genes Dev , vol.4 , pp. 1197-1208
    • Schaack, J.1    Ho, W.Y.2    Freimuth, P.3    Shenk, T.4
  • 25
    • 0027168320 scopus 로고
    • Adenovirus precursor to terminal protein interacts with the nuclear matrix in vivo and in vitro
    • Fredman JN, Engler JA (1993) Adenovirus precursor to terminal protein interacts with the nuclear matrix in vivo and in vitro. J Virol 67:3384-3395.
    • (1993) J Virol , vol.67 , pp. 3384-3395
    • Fredman, J.N.1    Engler, J.A.2
  • 26
    • 0037901814 scopus 로고    scopus 로고
    • DNA binding properties of the adenovirus DNA replication priming protein pTP
    • de Jong RN, Meijer LA, van der Vliet PC (2003) DNA binding properties of the adenovirus DNA replication priming protein pTP. Nucleic Acids Res 31:3274-3286.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3274-3286
    • De Jong, R.N.1    Meijer, L.A.2    Van Der Vliet, P.C.3
  • 27
    • 37549048171 scopus 로고    scopus 로고
    • Involvement of phage φ29 DNA polymerase and terminal protein subdomains in conferring specificity during initiation of protein-primed DNA replication
    • Pérez-Arnaiz P, et al. (2007) Involvement of phage φ29 DNA polymerase and terminal protein subdomains in conferring specificity during initiation of protein-primed DNA replication. Nucleic Acids Res 35:7061-7073.
    • (2007) Nucleic Acids Res , vol.35 , pp. 7061-7073
    • Pérez-Arnaiz, P.1
  • 28
    • 33748066329 scopus 로고    scopus 로고
    • Spo0A, the key transcriptional regulator for entrance into sporulation, is an inhibitor of DNA replication
    • Castilla-Llorente V, Muñoz-Espín D, Villar L, Salas M, Meijer WJJ (2006) Spo0A, the key transcriptional regulator for entrance into sporulation, is an inhibitor of DNA replication. EMBO J 25:3890-3899.
    • (2006) EMBO J , vol.25 , pp. 3890-3899
    • Castilla-Llorente, V.1    Muñoz-Espín, D.2    Villar, L.3    Salas, M.4    Meijer, W.J.J.5
  • 29
    • 0024351953 scopus 로고
    • Dissection of the expression signals of the spoA gene of Bacillus subtilis: Glucose represses sporulation-specific expression
    • Yamashita S, et al. (1989) Dissection of the expression signals of the spoA gene of Bacillus subtilis: Glucose represses sporulation-specific expression. J Gen Microbiol 135:1335-1345.
    • (1989) J Gen Microbiol , vol.135 , pp. 1335-1345
    • Yamashita, S.1
  • 30
    • 9644303162 scopus 로고    scopus 로고
    • Phage φ29 DNA replication organizer membrane protein p16.7 contains a coiled coil and a dimeric, homeodomain-related, functional domain
    • Muñoz-Espín D, et al. (2004) Phage φ29 DNA replication organizer membrane protein p16.7 contains a coiled coil and a dimeric, homeodomain-related, functional domain. J Biol Chem 279:50437-50445.
    • (2004) J Biol Chem , vol.279 , pp. 50437-50445
    • Muñoz-Espín, D.1
  • 31
    • 20144370204 scopus 로고    scopus 로고
    • Structure of the functional domain of φ29 replication organizer: Insights into oligomerization and DNA binding
    • Asensio JL, et al. (2005) Structure of the functional domain of φ29 replication organizer: Insights into oligomerization and DNA binding. J Biol Chem 280:20730-20739.
    • (2005) J Biol Chem , vol.280 , pp. 20730-20739
    • Asensio, J.L.1
  • 32
    • 0030927986 scopus 로고    scopus 로고
    • Direct evidence for active segregation of oriC regions of the Bacillus subtilis chromosome and co-localization with the SpoOJ partitioning protein
    • Lewis PJ, Errington J (1997) Direct evidence for active segregation of oriC regions of the Bacillus subtilis chromosome and co-localization with the SpoOJ partitioning protein. Mol Microbiol 25:945-954.
    • (1997) Mol Microbiol , vol.25 , pp. 945-954
    • Lewis, P.J.1    Errington, J.2
  • 33
    • 1942501103 scopus 로고    scopus 로고
    • The push-pull mechanism of bacteriophage φ29 DNA injection
    • González-Huici V, Salas M, Hermoso JM (2004) The push-pull mechanism of bacteriophage φ29 DNA injection. Mol Microbiol 52:529-540.
    • (2004) Mol Microbiol , vol.52 , pp. 529-540
    • González-Huici, V.1    Salas, M.2    Hermoso, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.