메뉴 건너뛰기




Volumn 68, Issue 6, 2008, Pages 1570-1582

Staphylococcus aureus primase has higher initiation specificity, interacts with single-stranded DNA stronger, but is less stimulated by its helicase than Escherichia coli primase

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; ESCHERICHIA COLI PRIMASE; ESCHERICHIA COLI PROTEIN; GLUTATHIONE TRANSFERASE; HELICASE; SINGLE STRANDED DNA; STAPHYLOCOCCUS AUREUS PRIMASE; SUGAR;

EID: 44249097571     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2008.06255.x     Document Type: Article
Times cited : (14)

References (35)
  • 1
    • 0035169689 scopus 로고    scopus 로고
    • Crystal structure of a DNA-dependent RNA polymerase (DNA primase)
    • Augustin, M.A., Huber, R. 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
  • 2
    • 35348979683 scopus 로고    scopus 로고
    • Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase
    • Bailey, S., Eliason, W.K. Steitz, T.A. (2007) Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. Science 318 : 459 463.
    • (2007) Science , vol.318 , pp. 459-463
    • Bailey, S.1    Eliason, W.K.2    Steitz, T.A.3
  • 3
    • 0034142263 scopus 로고    scopus 로고
    • DnaB helicase affects the initiation specificity of Escherichia coli primase on single-stranded DNA templates
    • Bhattacharyya, S. Griep, M.A. (2000) DnaB helicase affects the initiation specificity of Escherichia coli primase on single-stranded DNA templates. Biochemistry 39 : 745 752.
    • (2000) Biochemistry , vol.39 , pp. 745-752
    • Bhattacharyya, S.1    Griep, M.A.2
  • 4
    • 17444453249 scopus 로고    scopus 로고
    • Revised UV extinction coefficients for nucleoside-5′-monophosphates and unpaired DNA and RNA
    • Cavaluzzi, M.J. Borer, P.N. (2004) Revised UV extinction coefficients for nucleoside-5′-monophosphates and unpaired DNA and RNA. Nucleic Acids Res 32 : e13.
    • (2004) Nucleic Acids Res , vol.32
    • Cavaluzzi, M.J.1    Borer, P.N.2
  • 5
    • 33749119130 scopus 로고    scopus 로고
    • Regulation of bacterial priming and daughter strand synthesis through helicase-primase interactions
    • Corn, J.E. Berger, J.M. (2006) Regulation of bacterial priming and daughter strand synthesis through helicase-primase interactions. Nucleic Acids Res 34 : 4082 4088.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4082-4088
    • Corn, J.E.1    Berger, J.M.2
  • 6
    • 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. 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
  • 8
    • 8444236695 scopus 로고    scopus 로고
    • Primase
    • In. Brenner, S. Miller, J. (eds). New York: Academic Press, pp.
    • Griep, M.A. (2001) Primase. In Encyclopedia of Genetics. Brenner, S. Miller, J. (eds). New York : Academic Press, pp. 1542 1545.
    • (2001) Encyclopedia of Genetics. , pp. 1542-1545
    • Griep, M.A.1
  • 9
    • 0026057926 scopus 로고
    • Mutations in the Escherichia coli dnaG gene suggest coupling between DNA replication and chromosome partitioning
    • Grompe, M., Versalovic, J., Koeuth, T. Lupski, J.R. (1991) Mutations in the Escherichia coli dnaG gene suggest coupling between DNA replication and chromosome partitioning. J Bacteriol 173 : 1268 1278.
    • (1991) J Bacteriol , vol.173 , pp. 1268-1278
    • Grompe, M.1    Versalovic, J.2    Koeuth, T.3    Lupski, J.R.4
  • 10
    • 1842690078 scopus 로고    scopus 로고
    • Two new bacterial DNA primase inhibitors from the plant Polygonum cuspidatum
    • Hegde, V.R., Pu, H., Patel, M., Black, T., Soriano, A., Zhao, W., et al. (2004) Two new bacterial DNA primase inhibitors from the plant Polygonum cuspidatum. Bioorg Med Chem Lett 14 : 2275 2277.
    • (2004) Bioorg Med Chem Lett , vol.14 , pp. 2275-2277
    • Hegde, V.R.1    Pu, H.2    Patel, M.3    Black, T.4    Soriano, A.5    Zhao, W.6
  • 11
    • 0035666447 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of a DNA primase from hyperthermophilic archaeon Pyrococcus horikoshii
    • Ito, N., Nureki, O., Shirouzu, M., Yokoyama, S. Hanaoka, F. (2001) Crystallization and preliminary X-ray analysis of a DNA primase from hyperthermophilic archaeon Pyrococcus horikoshii. J Biochem 130 : 727 730.
    • (2001) J Biochem , vol.130 , pp. 727-730
    • Ito, N.1    Nureki, O.2    Shirouzu, M.3    Yokoyama, S.4    Hanaoka, F.5
  • 12
    • 0346025633 scopus 로고    scopus 로고
    • Crystal structure of the Pyrococcus horikoshii DNA primase-UTP complex: Implications for the mechanism of primer synthesis
    • Ito, N., Nureki, O., Shirouzu, M., Yokoyama, S. Hanaoka, F. (2003) Crystal structure of the Pyrococcus horikoshii DNA primase-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
  • 13
    • 0034141871 scopus 로고    scopus 로고
    • DnaB helicase stimulates primer synthesis activity on short oligonucleotide templates
    • Johnson, S.K., Bhattacharyya, S. Griep, M.A. (2000) DnaB helicase stimulates primer synthesis activity on short oligonucleotide templates. Biochemistry 39 : 736 744.
    • (2000) Biochemistry , vol.39 , pp. 736-744
    • Johnson, S.K.1    Bhattacharyya, S.2    Griep, M.A.3
  • 14
    • 0035164892 scopus 로고    scopus 로고
    • Primus inter pares (first among equals)
    • Keck, J.L. Berger, J.M. (2001) Primus inter pares (first among equals). Nat Struct Biol 8 : 2 4.
    • (2001) Nat Struct Biol , vol.8 , pp. 2-4
    • Keck, J.L.1    Berger, J.M.2
  • 15
    • 0034737468 scopus 로고    scopus 로고
    • Structure of the RNA polymerase domain of E. coli primase
    • Keck, J.L., Roche, D.D., Lynch, A.S. Berger, J.M. (2000) Structure of the RNA polymerase domain of E. coli primase. Science 287 : 2482 2486.
    • (2000) Science , vol.287 , pp. 2482-2486
    • Keck, J.L.1    Roche, D.D.2    Lynch, A.S.3    Berger, J.M.4
  • 16
    • 0037126718 scopus 로고    scopus 로고
    • Affinity and sequence specificity of DNA binding and site selection for primer synthesis by Escherichia coli primase
    • Khopde, S., Biswas, E.E. Biswas, S.B. (2002) Affinity and sequence specificity of DNA binding and site selection for primer synthesis by Escherichia coli primase. Biochemistry 41 : 14820 14830.
    • (2002) Biochemistry , vol.41 , pp. 14820-14830
    • Khopde, S.1    Biswas, E.E.2    Biswas, S.B.3
  • 17
    • 8444222286 scopus 로고    scopus 로고
    • Thermally-denaturing HPLC analysis of primase activity
    • Koepsell, S., Bastola, D., Hinrichs, S.H. Griep, M.A. (2004) Thermally-denaturing HPLC analysis of primase activity. Anal Biochem 332 : 330 336.
    • (2004) Anal Biochem , vol.332 , pp. 330-336
    • Koepsell, S.1    Bastola, D.2    Hinrichs, S.H.3    Griep, M.A.4
  • 18
    • 33745477005 scopus 로고    scopus 로고
    • Staphylococcus aureus helicase but not Escherichia coli helicase stimulates S. aureus primase activity and maintains initiation specificity
    • Koepsell, S.A., Larson, M.A., Griep, M.A. Hinrichs, S.H. (2006) Staphylococcus aureus helicase but not Escherichia coli helicase stimulates S. aureus primase activity and maintains initiation specificity. J Bacteriol 188 : 4673 4680.
    • (2006) J Bacteriol , vol.188 , pp. 4673-4680
    • Koepsell, S.A.1    Larson, M.A.2    Griep, M.A.3    Hinrichs, S.H.4
  • 19
    • 0028593398 scopus 로고
    • Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV
    • Lim, K., Ho, J.X., Keeling, K., Gilliland, G.L., Ji, X., Ruker, F. Carter, D.C. (1994) Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV. Protein Sci 3 : 2233 2244.
    • (1994) Protein Sci , vol.3 , pp. 2233-2244
    • Lim, K.1    Ho, J.X.2    Keeling, K.3    Gilliland, G.L.4    Ji, X.5    Ruker, F.6    Carter, D.C.7
  • 20
    • 0742323372 scopus 로고    scopus 로고
    • Antimicrobial drug discovery through bacteriophage genomics
    • Liu, J., Dehbi, M., Moeck, G., Arhin, F., Bauda, P., Bergeron, D., et al. (2004) Antimicrobial drug discovery through bacteriophage genomics. Nat Biotechnol 22 : 185 191.
    • (2004) Nat Biotechnol , vol.22 , pp. 185-191
    • Liu, J.1    Dehbi, M.2    Moeck, G.3    Arhin, F.4    Bauda, P.5    Bergeron, D.6
  • 21
    • 0028931691 scopus 로고
    • Crystal structures of a schistosomal drug and vaccine target: Glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel
    • McTigue, M.A., Williams, D.R. Tainer, J.A. (1995) Crystal structures of a schistosomal drug and vaccine target: glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel. J Mol Biol 246 : 21 27.
    • (1995) J Mol Biol , vol.246 , pp. 21-27
    • McTigue, M.A.1    Williams, D.R.2    Tainer, J.A.3
  • 22
    • 0034616957 scopus 로고    scopus 로고
    • A TOPRIM domain in the crystal structure of the catalytic core of Escherichia coli primase confirms a structural link to DNA topoisomerases
    • Podobnik, M., McInerney, P., O'Donnell, M. Kuriyan, J. (2000) A TOPRIM domain in the crystal structure of the catalytic core of Escherichia coli primase confirms a structural link to DNA topoisomerases. J Mol Biol 300 : 353 362.
    • (2000) J Mol Biol , vol.300 , pp. 353-362
    • Podobnik, M.1    McInerney, P.2    O'Donnell, M.3    Kuriyan, J.4
  • 23
    • 0027513148 scopus 로고
    • Mechanism of calf thymus DNA primase - Slow initiation, rapid polymerization, and intelligent termination
    • Sheaff, R.J. 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
  • 24
    • 0028038222 scopus 로고
    • Misincorporation of nucleotides by calf thymus DNA primase and elongation of primers containing multiple noncognate nucleotides by DNA-polymerase-alpha
    • Sheaff, R.J. Kuchta, R.D. (1994) Misincorporation of nucleotides by calf thymus DNA primase and elongation of primers containing multiple noncognate nucleotides by DNA-polymerase-alpha. J Biol Chem 269 : 19225 19231.
    • (1994) J Biol Chem , vol.269 , pp. 19225-19231
    • Sheaff, R.J.1    Kuchta, R.D.2
  • 25
    • 0021100251 scopus 로고
    • Complexes of Escherichia coli primase with the replication origin of G4 phage DNA
    • Stayton, M.M. Kornberg, A. (1983) Complexes of Escherichia coli primase with the replication origin of G4 phage DNA. J Biol Chem 258 : 13205 13212.
    • (1983) J Biol Chem , vol.258 , pp. 13205-13212
    • Stayton, M.M.1    Kornberg, A.2
  • 26
    • 33750055730 scopus 로고    scopus 로고
    • Monomeric solution structure of the helicase-binding domain of Escherichia coli DnaG primase
    • Su, X.C., Schaeffer, P.M., Loscha, K.V., Gan, P.H., Dixon, N.E. Otting, G. (2006) Monomeric solution structure of the helicase-binding domain of Escherichia coli DnaG primase. FEBS J 273 : 4997 5009.
    • (2006) FEBS J , vol.273 , pp. 4997-5009
    • Su, X.C.1    Schaeffer, P.M.2    Loscha, K.V.3    Gan, P.H.4    Dixon, N.E.5    Otting, G.6
  • 27
    • 0027412721 scopus 로고
    • Binding and phasing of Escherichia coli single-stranded DNA-binding protein by the secondary structure of phage-G4 origin of complementary-DNA strand synthesis (G4oriC)
    • Sun, W.L. Godson, G.N. (1993) Binding and phasing of Escherichia coli single-stranded DNA-binding protein by the secondary structure of phage-G4 origin of complementary-DNA strand synthesis (G4oriC). J Biol Chem 268 : 8026 8039.
    • (1993) J Biol Chem , vol.268 , pp. 8026-8039
    • Sun, W.L.1    Godson, G.N.2
  • 28
    • 10544227300 scopus 로고    scopus 로고
    • Interaction of Escherichia coli primase with a phage G4ori(c)-E. coli SSB complex
    • Sun, W.L. Godson, G.N. (1996) Interaction of Escherichia coli primase with a phage G4ori(c)-E. coli SSB complex. J Bacteriol 178 : 6701 6705.
    • (1996) J Bacteriol , vol.178 , pp. 6701-6705
    • Sun, W.L.1    Godson, G.N.2
  • 29
    • 0027160455 scopus 로고
    • Primase from Escherichia coli primes single-stranded templates in the absence of single-stranded DNA-binding protein or other auxiliary proteins: Template sequence requirements based on the bacteriophage-G4 complementary strand origin and Okazaki fragment initiation sites
    • Swart, J.R. Griep, M.A. (1993) Primase from Escherichia coli primes single-stranded templates in the absence of single-stranded DNA-binding protein or other auxiliary proteins: template sequence requirements based on the bacteriophage-G4 complementary strand origin and Okazaki fragment initiation sites. J Biol Chem 268 : 12970 12976.
    • (1993) J Biol Chem , vol.268 , pp. 12970-12976
    • Swart, J.R.1    Griep, M.A.2
  • 30
    • 0028820262 scopus 로고
    • Primer synthesis kinetics by Escherichia coli primase on single-stranded DNA templates
    • Swart, J.R. Griep, M.A. (1995) Primer synthesis kinetics by Escherichia coli primase on single-stranded DNA templates. Biochemistry 34 : 16097 16106.
    • (1995) Biochemistry , vol.34 , pp. 16097-16106
    • Swart, J.R.1    Griep, M.A.2
  • 31
    • 17044371192 scopus 로고    scopus 로고
    • Solution structure of the helicase interaction domain of the primase DnaG: A model for helicase activation
    • Syson, K., Thirlway, J., Hounslow, A.M., Soultanas, P. Waltho, J.P. (2005) Solution structure of the helicase interaction domain of the primase DnaG: a model for helicase activation. Structure 13 : 609 616.
    • (2005) Structure , vol.13 , pp. 609-616
    • Syson, K.1    Thirlway, J.2    Hounslow, A.M.3    Soultanas, P.4    Waltho, J.P.5
  • 32
    • 32444436659 scopus 로고    scopus 로고
    • In the Bacillus stearothermophilus DnaB-DnaG complex, the activities of the two proteins are modulated by distinct but overlapping networks of residues
    • Thirlway, J. Soultanas, P. (2006) In the Bacillus stearothermophilus DnaB-DnaG complex, the activities of the two proteins are modulated by distinct but overlapping networks of residues. J Bacteriol 188 : 1534 1539.
    • (2006) J Bacteriol , vol.188 , pp. 1534-1539
    • Thirlway, J.1    Soultanas, P.2
  • 33
    • 16344368485 scopus 로고    scopus 로고
    • A macroscopic kinetic model for DNA polymerase elongation and high-fidelity nucleotide selection
    • Viljoen, S., Griep, M.A., Nelson, M. Viljoen, H. (2005) A macroscopic kinetic model for DNA polymerase elongation and high-fidelity nucleotide selection. Comp Biol Chem 29 : 101 110.
    • (2005) Comp Biol Chem , vol.29 , pp. 101-110
    • Viljoen, S.1    Griep, M.A.2    Nelson, M.3    Viljoen, H.4
  • 34
    • 0027434814 scopus 로고
    • Biochemical properties of cloned glutathione S-transferases from Schistosoma mansoni and Schistosoma japonicum
    • Walker, J., Crowley, P., Moreman, A.D. Barrett, J. (1993) Biochemical properties of cloned glutathione S-transferases from Schistosoma mansoni and Schistosoma japonicum. Mol Biochem Parasitol 61 : 255 264.
    • (1993) Mol Biochem Parasitol , vol.61 , pp. 255-264
    • Walker, J.1    Crowley, P.2    Moreman, A.D.3    Barrett, J.4
  • 35
    • 0037092968 scopus 로고    scopus 로고
    • Homogenous assays for Escherichia coli DnaB-stimulated DnaG primase and DnaB helicase and their use in screening for chemical inhibitors
    • Zhang, Y., Yang, F.D., Kao, Y.C., Kurilla, M.G., Pompliano, D.L. Dicker, I.B. (2002) Homogenous assays for Escherichia coli DnaB-stimulated DnaG primase and DnaB helicase and their use in screening for chemical inhibitors. Anal Biochem 304 : 174 179.
    • (2002) Anal Biochem , vol.304 , pp. 174-179
    • Zhang, Y.1    Yang, F.D.2    Kao, Y.C.3    Kurilla, M.G.4    Pompliano, D.L.5    Dicker, I.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.