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Volumn 290, Issue 9, 2015, Pages 5635-5646

Crystal structure of the human primase

Author keywords

[No Author keywords available]

Indexed keywords

DNA; ELONGATION; ENZYMES; NUCLEIC ACIDS; RNA; SYNTHESIS (CHEMICAL);

EID: 84923862728     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.624742     Document Type: Article
Times cited : (63)

References (51)
  • 1
    • 84876319685 scopus 로고    scopus 로고
    • The Pol α-primase complex
    • Pellegrini, L. (2012) The Pol α-primase complex. Subcell. Biochem. 62, 157-169
    • (2012) Subcell. Biochem. , vol.62 , pp. 157-169
    • Pellegrini, L.1
  • 2
    • 67650409702 scopus 로고    scopus 로고
    • 3D architecture of DNA Pol α reveals the functional core of multi-subunit replicative polymerases
    • Klinge, S., Núñez-Ramirez, R., Llorca, O., and Pellegrini, L. (2009) 3D architecture of DNA Pol α reveals the functional core of multi-subunit replicative polymerases. EMBO J. 28, 1978-1987
    • (2009) EMBO J. , vol.28 , pp. 1978-1987
    • Klinge, S.1    Núez-Ramirez, R.2    Llorca, O.3    Pellegrini, L.4
  • 3
    • 84863615796 scopus 로고    scopus 로고
    • A conserved motif in the C-terminal tail of DNA polymerase α tethers primase to the eukaryotic replisome
    • Kilkenny, M. L., De Piccoli, G., Perera, R. L., Labib, K., and Pellegrini, L. (2012) A conserved motif in the C-terminal tail of DNA polymerase α tethers primase to the eukaryotic replisome. J. Biol. Chem. 287, 23740-23747
    • (2012) J. Biol. Chem. , vol.287 , pp. 23740-23747
    • Kilkenny, M.L.1    De Piccoli, G.2    Perera, R.L.3    Labib, K.4    Pellegrini, L.5
  • 4
    • 0032747634 scopus 로고    scopus 로고
    • Molecular architecture of the mouseDNApolymerase α-primase complex
    • Mizuno, T., Yamagishi, K., Miyazawa, H., and Hanaoka, F. (1999) Molecular architecture of the mouseDNApolymerase α-primase complex. Mol. Cell. Biol. 19, 7886-7896
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7886-7896
    • Mizuno, T.1    Yamagishi, K.2    Miyazawa, H.3    Hanaoka, F.4
  • 5
    • 84905867880 scopus 로고    scopus 로고
    • The C-terminal domain of theDNApolymerase catalytic subunit regulates the primase and polymerase activities of the human DNA polymerase α-primase complex
    • Zhang, Y., Baranovskiy, A. G., Tahirov, T. H., and Pavlov, Y. I. (2014) The C-terminal domain of theDNApolymerase catalytic subunit regulates the primase and polymerase activities of the human DNA polymerase α-primase complex. J. Biol. Chem. 289, 22021-22034
    • (2014) J. Biol. Chem. , vol.289 , pp. 22021-22034
    • Zhang, Y.1    Baranovskiy, A.G.2    Tahirov, T.H.3    Pavlov, Y.I.4
  • 6
    • 0028331879 scopus 로고
    • Calf thymus DNA polymerase α-primase: "communication" and primer-template movement between the two active sites
    • Sheaff, R. J., Kuchta, R. D., and Ilsley, D. (1994) Calf thymus DNA polymerase α-primase: "communication" and primer-template movement between the two active sites. Biochemistry 33, 2247-2254
    • (1994) Biochemistry , vol.33 , pp. 2247-2254
    • Sheaff, R.J.1    Kuchta, R.D.2    Ilsley, D.3
  • 8
    • 0027379095 scopus 로고
    • Enzymatic characterization of the individual mammalian primase subunits reveals a biphasic mechanism for initiation of DNA replication
    • Copeland, W. C., and Wang, T. S. (1993) Enzymatic characterization of the individual mammalian primase subunits reveals a biphasic mechanism for initiation of DNA replication. J. Biol. Chem. 268, 26179-26189
    • (1993) J. Biol. Chem. , vol.268 , pp. 26179-26189
    • Copeland, W.C.1    Wang, T.S.2
  • 9
    • 0027513148 scopus 로고
    • Mechanism of calf thymus DNA primase: Slow initiation, rapid polymerization, and intelligent termination
    • Sheaff, R. J., and Kuchta, R. D. (1993) Mechanism of calf thymus DNA primase: slow initiation, rapid polymerization, and intelligent termination. Biochemistry 32, 3027-3037
    • (1993) Biochemistry , vol.32 , pp. 3027-3037
    • Sheaff, R.J.1    Kuchta, R.D.2
  • 10
    • 77949570959 scopus 로고    scopus 로고
    • Mechanism and evolution of DNA primases
    • Kuchta, R. D., and Stengel, G. (2010) Mechanism and evolution of DNA primases. Biochim. Biophys. Acta 1804, 1180-1189
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 1180-1189
    • Kuchta, R.D.1    Stengel, G.2
  • 11
    • 0037117724 scopus 로고    scopus 로고
    • The p58 subunit of human DNA primase is important for primer initiation, elongation, and counting
    • Zerbe, L. K., and Kuchta, R. D. (2002) The p58 subunit of human DNA primase is important for primer initiation, elongation, and counting. Biochemistry 41, 4891-4900
    • (2002) Biochemistry , vol.41 , pp. 4891-4900
    • Zerbe, L.K.1    Kuchta, R.D.2
  • 12
    • 0033613231 scopus 로고    scopus 로고
    • Interac-tions ofDNAwith humanDNAprimase monitored with photoactivatable cross-linking agents: Implications for the role of the p58 subunit
    • Arezi, B., Kirk, B. W., Copeland, W. C., and Kuchta, R. D. (1999) Interac-tions ofDNAwith humanDNAprimase monitored with photoactivatable cross-linking agents: implications for the role of the p58 subunit. Biochemistry 38, 12899-12907
    • (1999) Biochemistry , vol.38 , pp. 12899-12907
    • Arezi, B.1    Kirk, B.W.2    Copeland, W.C.3    Kuchta, R.D.4
  • 13
    • 0029563220 scopus 로고
    • Highly selective affinity labeling of DNA polymerase α-primase from human placenta by reactive analogs of ATP
    • Zakharova, O. D., Podust, V. N., Mustaev, A. A., Anarbaev, R. O., and Lavrik, O. I. (1995) Highly selective affinity labeling of DNA polymerase α-primase from human placenta by reactive analogs of ATP. Biochimie 77, 699-702
    • (1995) Biochimie , vol.77 , pp. 699-702
    • Zakharova, O.D.1    Podust, V.N.2    Mustaev, A.A.3    Anarbaev, R.O.4    Lavrik, O.I.5
  • 14
    • 0031076274 scopus 로고    scopus 로고
    • Expression, purification, and characterization of the two human primase subunits and truncated complexes from Escherichia coli
    • Copeland, W. C. (1997) Expression, purification, and characterization of the two human primase subunits and truncated complexes from Escherichia coli. Protein Expr. Purif. 9, 1-9
    • (1997) Protein Expr. Purif. , vol.9 , pp. 1-9
    • Copeland, W.C.1
  • 15
    • 0024961711 scopus 로고
    • Affinity labeling of the active center and ribonucleoside triphosphate binding site of yeast DNA primase
    • Foiani, M., Lindner, A. J., Hartmann, G. R., Lucchini, G., and Plevani, P. (1989) Affinity labeling of the active center and ribonucleoside triphosphate binding site of yeast DNA primase. J. Biol. Chem. 264, 2189-2194
    • (1989) J. Biol. Chem. , vol.264 , pp. 2189-2194
    • Foiani, M.1    Lindner, A.J.2    Hartmann, G.R.3    Lucchini, G.4    Plevani, P.5
  • 16
    • 84885048683 scopus 로고    scopus 로고
    • Structures of human primase reveal design of nucleotide elongation site and mode of Pol α tethering
    • Kilkenny, M. L., Longo, M. A., Perera, R. L., and Pellegrini, L. (2013) Structures of human primase reveal design of nucleotide elongation site and mode of Pol α tethering. Proc. Natl. Acad. Sci. U.S.A. 110, 15961-15966
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 15961-15966
    • Kilkenny, M.L.1    Longo, M.A.2    Perera, R.L.3    Pellegrini, L.4
  • 17
    • 77956325209 scopus 로고    scopus 로고
    • Shared active site architecture between the large subunit of eukaryotic primase and DNA photolyase
    • Sauguet, L., Klinge, S., Perera, R. L., Maman, J. D., and Pellegrini, L. (2010) Shared active site architecture between the large subunit of eukaryotic primase and DNA photolyase. PLoS One 5, e10083
    • (2010) PLoS One , vol.5 , pp. e10083
    • Sauguet, L.1    Klinge, S.2    Perera, R.L.3    Maman, J.D.4    Pellegrini, L.5
  • 18
    • 77956363679 scopus 로고    scopus 로고
    • Insights into eukaryotic DNA priming from the structure and functional interactions of the 4Fe-4S cluster domain of human DNA primase
    • Vaithiyalingam, S., Warren, E. M., Eichman, B. F., and Chazin, W. J. (2010) Insights into eukaryotic DNA priming from the structure and functional interactions of the 4Fe-4S cluster domain of human DNA primase. Proc. Natl. Acad. Sci. U.S.A. 107, 13684-13689
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 13684-13689
    • Vaithiyalingam, S.1    Warren, E.M.2    Eichman, B.F.3    Chazin, W.J.4
  • 20
    • 34548492954 scopus 로고    scopus 로고
    • An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis
    • Klinge, S., Hirst, J., Maman, J. D., Krude, T., and Pellegrini, L. (2007) An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis. Nat. Struct. Mol. Biol. 14, 875-877
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 875-877
    • Klinge, S.1    Hirst, J.2    Maman, J.D.3    Krude, T.4    Pellegrini, L.5
  • 21
    • 79952674723 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal domain of human DNA primase large subunit: Implications for the mechanism of the primase-polymerase α switch
    • Agarkar, V. B., Babayeva, N. D., Pavlov, Y. I., and Tahirov, T. H. (2011) Crystal structure of the C-terminal domain of human DNA primase large subunit: implications for the mechanism of the primase-polymerase α switch. Cell Cycle 10, 926-931
    • (2011) Cell Cycle , vol.10 , pp. 926-931
    • Agarkar, V.B.1    Babayeva, N.D.2    Pavlov, Y.I.3    Tahirov, T.H.4
  • 22
    • 36348995555 scopus 로고    scopus 로고
    • An iron-sulfur cluster in the C-terminal domain of the p58 subunit of humanDNAprimase
    • Weiner, B. E., Huang, H., Dattilo, B. M., Nilges, M. J., Fanning, E., and Chazin, W. J. (2007) An iron-sulfur cluster in the C-terminal domain of the p58 subunit of humanDNAprimase. J. Biol. Chem. 282, 33444-33451
    • (2007) J. Biol. Chem. , vol.282 , pp. 33444-33451
    • Weiner, B.E.1    Huang, H.2    Dattilo, B.M.3    Nilges, M.J.4    Fanning, E.5    Chazin, W.J.6
  • 23
    • 0033199713 scopus 로고    scopus 로고
    • Did DNA replication evolve twice independently?
    • Leipe, D. D., Aravind, L., and Koonin, E. V. (1999) Did DNA replication evolve twice independently? Nucleic Acids Res. 27, 3389-3401
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3389-3401
    • Leipe, D.D.1    Aravind, L.2    Koonin, E.V.3
  • 24
    • 0035169689 scopus 로고    scopus 로고
    • Crystal structure of a DNA-dependent RNA polymerase (DNA primase)
    • Augustin, M. A., Huber, R., and Kaiser, J. T. (2001) Crystal structure of a DNA-dependent RNA polymerase (DNA primase). Nat. Struct. Biol. 8, 57-61
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 57-61
    • Augustin, M.A.1    Huber, R.2    Kaiser, J.T.3
  • 25
    • 0346025633 scopus 로고    scopus 로고
    • Crystal structure of the Pyrococcus horikoshii DNAprimase-UTP complex: Implications for the mechanism of primer synthesis
    • Ito, N., Nureki, O., Shirouzu, M., Yokoyama, S., and Hanaoka, F. (2003) Crystal structure of the Pyrococcus horikoshii DNAprimase-UTP complex: implications for the mechanism of primer synthesis. Genes Cells 8, 913-923
    • (2003) Genes Cells , vol.8 , pp. 913-923
    • Ito, N.1    Nureki, O.2    Shirouzu, M.3    Yokoyama, S.4    Hanaoka, F.5
  • 27
    • 0028917904 scopus 로고
    • Active site mapping of the catalytic mouse primase subunit by alanine scanning mutagenesis
    • Copeland, W. C., and Tan, X. (1995) Active site mapping of the catalytic mouse primase subunit by alanine scanning mutagenesis. J. Biol. Chem. 270, 3905-3913
    • (1995) J. Biol. Chem. , vol.270 , pp. 3905-3913
    • Copeland, W.C.1    Tan, X.2
  • 28
    • 84892496098 scopus 로고    scopus 로고
    • Insights into eukaryotic primer synthesis from structures of the p48 subunit of human DNA primase
    • Vaithiyalingam, S., Arnett, D. R., Aggarwal, A., Eichman, B. F., Fanning, E., and Chazin,W.J. (2014) Insights into eukaryotic primer synthesis from structures of the p48 subunit of human DNA primase. J. Mol. Biol. 426, 558-569
    • (2014) J. Mol. Biol. , vol.426 , pp. 558-569
    • Vaithiyalingam, S.1    Arnett, D.R.2    Aggarwal, A.3    Eichman, B.F.4    Fanning, E.5    Chazin, W.J.6
  • 29
    • 33645962475 scopus 로고    scopus 로고
    • Making and breaking nucleic acids: Two-Mg2 -ion catalysis and substrate specificity
    • Yang, W., Lee, J. Y., and Nowotny, M. (2006) Making and breaking nucleic acids: two-Mg2 -ion catalysis and substrate specificity. Mol. Cell 22, 5-13
    • (2006) Mol. Cell , vol.22 , pp. 5-13
    • Yang, W.1    Lee, J.Y.2    Nowotny, M.3
  • 30
    • 84905499549 scopus 로고    scopus 로고
    • Crystallization and preliminary x-ray diffraction analysis of human DNA primase. Acta Crystallogr. F Struct
    • Baranovskiy, A. G., Gu, J., Babayeva, N. D., Agarkar, V. B., Suwa, Y., and Tahirov, T. H. (2014) Crystallization and preliminary x-ray diffraction analysis of human DNA primase. Acta Crystallogr. F Struct. Biol. Commun. 70, 206-210
    • (2014) Biol. Commun. , vol.70 , pp. 206-210
    • Baranovskiy, A.G.1    Gu, J.2    Babayeva, N.D.3    Agarkar, V.B.4    Suwa, Y.5    Tahirov, T.H.6
  • 31
  • 32
    • 58949085244 scopus 로고    scopus 로고
    • An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol
    • Liu, H., and Naismith, J. H. (2008) An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol. BMC Biotechnol. 8, 91
    • (2008) BMC Biotechnol. , vol.8 , pp. 91
    • Liu, H.1    Naismith, J.H.2
  • 35
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the crystallography andNMRsystem
    • Brunger, A. T. (2007) Version 1.2 of the crystallography andNMRsystem. Nat. Protoc. 2, 2728-2733
    • (2007) Nat. Protoc. , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 37
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L., and Rosenström, P. (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549
    • (2010) Nucleic Acids Res. , vol.38 , pp. W545-W549
    • Holm, L.1    Rosenström, P.2
  • 38
    • 0038054465 scopus 로고    scopus 로고
    • Modular architecture of the bacteriophage T7 primase couples RNA primer synthesis to DNA synthesis
    • Kato, M., Ito, T., Wagner, G., Richardson, C. C., and Ellenberger, T. (2003) Modular architecture of the bacteriophage T7 primase couples RNA primer synthesis to DNA synthesis. Mol. Cell 11, 1349-1360
    • (2003) Mol. Cell , vol.11 , pp. 1349-1360
    • Kato, M.1    Ito, T.2    Wagner, G.3    Richardson, C.C.4    Ellenberger, T.5
  • 39
    • 27644594271 scopus 로고    scopus 로고
    • Crosstalk between primase subunits can act to regulate primer synthesis in trans
    • Corn, J. E., Pease, P. J., Hura, G. L., and Berger, J. M. (2005) Crosstalk between primase subunits can act to regulate primer synthesis in trans. Mol. Cell 20, 391-401
    • (2005) Mol. Cell , vol.20 , pp. 391-401
    • Corn, J.E.1    Pease, P.J.2    Hura, G.L.3    Berger, J.M.4
  • 40
    • 0034653865 scopus 로고    scopus 로고
    • Structure of the zinc-binding domain of Bacillus stearothermophilus DNA primase
    • Pan, H., and Wigley, D. B. (2000) Structure of the zinc-binding domain of Bacillus stearothermophilus DNA primase. Structure 8, 231-239
    • (2000) Structure , vol.8 , pp. 231-239
    • Pan, H.1    Wigley, D.B.2
  • 41
    • 3142732108 scopus 로고    scopus 로고
    • A molecular handoff between bacteriophage T7 DNA primase and T7 DNA polymerase initiates DNA synthesis
    • Kato, M., Ito, T., Wagner, G., and Ellenberger, T. (2004) A molecular handoff between bacteriophage T7 DNA primase and T7 DNA polymerase initiates DNA synthesis. J. Biol. Chem. 279, 30554-30562
    • (2004) J. Biol. Chem. , vol.279 , pp. 30554-30562
    • Kato, M.1    Ito, T.2    Wagner, G.3    Ellenberger, T.4
  • 42
    • 0022477409 scopus 로고
    • DNA bending at ade-nine-thymine tracts
    • Koo, H. S., Wu, H. M., and Crothers, D. M. (1986) DNA bending at ade-nine-thymine tracts. Nature 320, 501-506
    • (1986) Nature , vol.320 , pp. 501-506
    • Koo, H.S.1    Wu, H.M.2    Crothers, D.M.3
  • 45
    • 66149123741 scopus 로고    scopus 로고
    • Direct detection of abortive RNA transcripts in vivo
    • Goldman, S. R., Ebright, R. H., and Nickels, B. E. (2009) Direct detection of abortive RNA transcripts in vivo. Science 324, 927-928
    • (2009) Science , vol.324 , pp. 927-928
    • Goldman, S.R.1    Ebright, R.H.2    Nickels, B.E.3
  • 46
    • 66049164017 scopus 로고    scopus 로고
    • Structure and function of primase RepB′ encoded by broad-host-range plasmid RSF1010 that replicates exclusively in leading-strand mode
    • Geibel, S., Banchenko, S., Engel, M., Lanka, E., and Saenger, W. (2009) Structure and function of primase RepB′ encoded by broad-host-range plasmid RSF1010 that replicates exclusively in leading-strand mode. Proc. Natl. Acad. Sci. U.S.A. 106, 7810-7815
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 7810-7815
    • Geibel, S.1    Banchenko, S.2    Engel, M.3    Lanka, E.4    Saenger, W.5
  • 48
    • 0018895114 scopus 로고
    • DiscontinuousDNAreplication
    • Ogawa, T., and Okazaki, T. (1980) DiscontinuousDNAreplication. Annu. Rev. Biochem. 49, 421-457
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 421-457
    • Ogawa, T.1    Okazaki, T.2
  • 49
    • 0026597780 scopus 로고
    • Eukaryotic DNA primase appears to act as oligomer in DNA-polymerase-α-primase complex
    • Podust, V. N., Vladimirova, O. V., Manakova, E. N., and Lavrik, O. I. (1992) Eukaryotic DNA primase appears to act as oligomer in DNA-polymerase-α-primase complex. Eur. J. Biochem. 206, 7-13
    • (1992) Eur. J. Biochem. , vol.206 , pp. 7-13
    • Podust, V.N.1    Vladimirova, O.V.2    Manakova, E.N.3    Lavrik, O.I.4
  • 50
    • 0022970582 scopus 로고
    • Yeast DNA primase and DNA polymerase activities. An analysis of RNA priming and its coupling to DNA synthesis
    • Singh, H., Brooke, R. G., Pausch, M. H., Williams, G. T., Trainor, C., and Dumas, L. B. (1986) Yeast DNA primase and DNA polymerase activities. An analysis of RNA priming and its coupling to DNA synthesis. J. Biol. Chem. 261, 8564-8569
    • (1986) J. Biol. Chem. , vol.261 , pp. 8564-8569
    • Singh, H.1    Brooke, R.G.2    Pausch, M.H.3    Williams, G.T.4    Trainor, C.5    Dumas, L.B.6
  • 51
    • 0028800990 scopus 로고
    • Interactions of calf thymus DNA polymerase α with primer/templates
    • Thompson, H. C., Sheaff, R. J., and Kuchta, R. D. (1995) Interactions of calf thymus DNA polymerase α with primer/templates. Nucleic Acids Res. 23, 4109-4115
    • (1995) Nucleic Acids Res. , vol.23 , pp. 4109-4115
    • Thompson, H.C.1    Sheaff, R.J.2    Kuchta, R.D.3


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