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Volumn 178, Issue 15, 1996, Pages 4620-4627

Defect in general priming conferred by linker region mutants of Escherichia coli dnaB

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYRIBONUCLEOPROTEIN;

EID: 0029772574     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.15.4620-4627.1996     Document Type: Article
Times cited : (16)

References (40)
  • 1
    • 0038931706 scopus 로고
    • A general priming system employing only DnaB protein and primase for DNA replication
    • Arai, K., and A. Kornberg. 1979. A general priming system employing only DnaB protein and primase for DNA replication. Proc. Natl. Acad. Sci. USA 76:4308-4312.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4308-4312
    • Arai, K.1    Kornberg, A.2
  • 2
    • 0019400815 scopus 로고
    • Mechanism of DnaB protein. II. ATP hydrolysis by DnaB protein dependent on single- Or double-stranded DNA
    • Arai, K., and A. Kornberg. 1981. Mechanism of DnaB protein. II. ATP hydrolysis by DnaB protein dependent on single- or double-stranded DNA. J. Biol. Chem. 256:5253-5259.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5253-5259
    • Arai, K.1    Kornberg, A.2
  • 3
    • 0019490027 scopus 로고
    • Mechanism of DnaB protein. III. Allosteric role of ATP in the alteration of DNA structure by dnaB protein in priming replication
    • Arai, K., and A. Kornberg. 1981. Mechanism of DnaB protein. III. Allosteric role of ATP in the alteration of DNA structure by dnaB protein in priming replication. J. Biol. Chem. 256:5260-5256.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5260-15256
    • Arai, K.1    Kornberg, A.2
  • 4
    • 0019447096 scopus 로고
    • Mechanism of DnaB protein. IV. General priming of DNA replication by dnaB protein and primase compared with RNA polymerase
    • Arai, K., and A. Kornberg. 1981. Mechanism of DnaB protein. IV. General priming of DNA replication by dnaB protein and primase compared with RNA polymerase. J. Biol. Chem. 256:5267-5272.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5267-5272
    • Arai, K.1    Kornberg, A.2
  • 5
    • 0019487030 scopus 로고
    • Mechanism of dnaB protein action. I. Crystallization and properties of dnaB protein, an essential replication protein in Escherichia coli
    • Arai, K., S. Yasuda, and A. Kornberg. 1981. Mechanism of dnaB protein action. I. Crystallization and properties of dnaB protein, an essential replication protein in Escherichia coli. J. Biol. Chem. 256:5247-5252.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5247-5252
    • Arai, K.1    Yasuda, S.2    Kornberg, A.3
  • 6
    • 0023654911 scopus 로고
    • Helicase action of dnaB protein during replication from the Escherichia coli chromosomal origin in vitro
    • Baker, T., B. Funnell, and A. Kornberg. 1987. Helicase action of dnaB protein during replication from the Escherichia coli chromosomal origin in vitro. J. Biol. Chem. 262:6877-6885.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6877-6885
    • Baker, T.1    Funnell, B.2    Kornberg, A.3
  • 7
    • 0028068822 scopus 로고
    • Structure and function of Escherichia coli DnaB protein: Role of the N-terminal domain in helicase activity
    • Biswas, S. B., P. Chen, and E. E. Biswas. 1994. Structure and function of Escherichia coli DnaB protein: role of the N-terminal domain in helicase activity. Biochemistry 33:11307-11314.
    • (1994) Biochemistry , vol.33 , pp. 11307-11314
    • Biswas, S.B.1    Chen, P.2    Biswas, E.E.3
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0028046581 scopus 로고
    • Oligomeric structure of Escherichia coli primary replicative helicase DnaB protein
    • Bujalowski, W., M. M. Klonowska, and M. J. Jezewska. 1994. Oligomeric structure of Escherichia coli primary replicative helicase DnaB protein. J. Biol. Chem. 269:31350-31358.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31350-31358
    • Bujalowski, W.1    Klonowska, M.M.2    Jezewska, M.J.3
  • 11
    • 0025870077 scopus 로고
    • An over-expression plasmid for Escherichia coli primase
    • Godson, G. N. 1991. An over-expression plasmid for Escherichia coli primase. Gene 100:59-64.
    • (1991) Gene , vol.100 , pp. 59-64
    • Godson, G.N.1
  • 13
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. 1985. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82:488-492.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.1
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0017813212 scopus 로고
    • Escherichia coli dnaB mutant defective in DNA initiation: Isolation and properties of the dnaB protein
    • Lanka, E., B. Geschke, and H. Schuster. 1978. Escherichia coli dnaB mutant defective in DNA initiation: isolation and properties of the dnaB protein. Proc. Natl. Acad. Sci. USA 75:799-803.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 799-803
    • Lanka, E.1    Geschke, B.2    Schuster, H.3
  • 16
    • 0022977660 scopus 로고
    • The Escherichia coli DnaB replication protein is a DNA helicase
    • LeBowitz, J., and R. McMacken. 1986. The Escherichia coli DnaB replication protein is a DNA helicase. J. Biol. Chem. 261:4738-4748.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4738-4748
    • LeBowitz, J.1    McMacken, R.2
  • 19
    • 0026726799 scopus 로고
    • Defective replication activity of a dominant-lethal dnaB gene product from Escherichia coli
    • Marzalek, J., and J. M. Kaguni. 1992. Defective replication activity of a dominant-lethal dnaB gene product from Escherichia coli. J. Biol. Chem. 267:19334-19340.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19334-19340
    • Marzalek, J.1    Kaguni, J.M.2
  • 20
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira, P. 1987. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262:10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 21
    • 0023812834 scopus 로고
    • Dominant-lethal mutations in the dnaB helicase gene of Salmonella typhimurium
    • Maurer, R., and A. Wong. 1988. Dominant-lethal mutations in the dnaB helicase gene of Salmonella typhimurium. J. Bacteriol. 170:3682-3688.
    • (1988) J. Bacteriol. , vol.170 , pp. 3682-3688
    • Maurer, R.1    Wong, A.2
  • 22
    • 0021759105 scopus 로고
    • Nucleotide sequence of dnaB and the primary structure of the dnaB protein from Escherichia coli
    • Nakayama, N., N. Arai, M. W. Bonds, Y. Kaziro, and K. Arai. 1984. Nucleotide sequence of dnaB and the primary structure of the dnaB protein from Escherichia coli. J. Biol. Chem. 259:97-101.
    • (1984) J. Biol. Chem. , vol.259 , pp. 97-101
    • Nakayama, N.1    Arai, N.2    Bonds, M.W.3    Kaziro, Y.4    Arai, K.5
  • 23
    • 0021759104 scopus 로고
    • Structural and functional studies of the DnaB protein using limited proteolysis. Characterization of domains for DNA-dependent ATP hydrolysis and for protein association in the primosome
    • Nakayama, N., N. Arai, Y. Kaziro, and K. Arai. 1984. Structural and functional studies of the DnaB protein using limited proteolysis. Characterization of domains for DNA-dependent ATP hydrolysis and for protein association in the primosome. J. Biol. Chem. 259:88-96.
    • (1984) J. Biol. Chem. , vol.259 , pp. 88-96
    • Nakayama, N.1    Arai, N.2    Kaziro, Y.3    Arai, K.4
  • 24
    • 0017842412 scopus 로고
    • The dnaB gene product of Escherichia coli. I. Purification, homogeneity, and physical properties
    • Reha-Krantz, L., and J. Hurwitz. 1978. The dnaB gene product of Escherichia coli. I. Purification, homogeneity, and physical properties. J. Biol. Chem. 253:4043-4050.
    • (1978) J. Biol. Chem. , vol.253 , pp. 4043-4050
    • Reha-Krantz, L.1    Hurwitz, J.2
  • 25
    • 0017809781 scopus 로고
    • The dnaB gene product of Escherichia coli. II. Single-stranded DNA-dependent ribonucleotide triphosphatase activity
    • Reha-Krantz, L., and J. Hurwitz. 1978. The dnaB gene product of Escherichia coli. II. Single-stranded DNA-dependent ribonucleotide triphosphatase activity. J. Biol. Chem. 253:4051-4057.
    • (1978) J. Biol. Chem. , vol.253 , pp. 4051-4057
    • Reha-Krantz, L.1    Hurwitz, J.2
  • 26
    • 0018101448 scopus 로고
    • Primase, the dnaG protein of Escherichia coli. An enzyme which starts DNA chains
    • Rowen, L., and A. Kornberg. 1978. Primase, the dnaG protein of Escherichia coli. An enzyme which starts DNA chains. J. Biol. Chem. 253:758-764.
    • (1978) J. Biol. Chem. , vol.253 , pp. 758-764
    • Rowen, L.1    Kornberg, A.2
  • 27
    • 0028821014 scopus 로고
    • Biochemical characterization of Escherichia coli temperature-sensitive dnaB mutants dnaB8, dnaB252, dnaB70, dnaB43, and dnaB454
    • Saluja, D., and G. N. Godson. 1995. Biochemical characterization of Escherichia coli temperature-sensitive dnaB mutants dnaB8, dnaB252, dnaB70, dnaB43, and dnaB454. J. Bacteriol. 177:1104-1111.
    • (1995) J. Bacteriol. , vol.177 , pp. 1104-1111
    • Saluja, D.1    Godson, G.N.2
  • 28
    • 0029147295 scopus 로고
    • A structural model for the Escherichia coli DnaB helicase based on electron microscopy data
    • San Martin, M. C., N. P. J. Stamford, N. Dammerova, N. E. Dixon, and J. M. Carazo. 1995. A structural model for the Escherichia coli DnaB helicase based on electron microscopy data. J. Struct. Biol. 114:167-176.
    • (1995) J. Struct. Biol. , vol.114 , pp. 167-176
    • San Martin, M.C.1    Stamford, N.P.J.2    Dammerova, N.3    Dixon, N.E.4    Carazo, J.M.5
  • 29
    • 0026437716 scopus 로고
    • Purification and characterization of a mutant DnaB protein specifically defective in ATP hydrolysis
    • Shrimankar, P., L. Stordal, and R. Maurer. 1992. Purification and characterization of a mutant DnaB protein specifically defective in ATP hydrolysis. J. Bacteriol. 174:7689-7696.
    • (1992) J. Bacteriol. , vol.174 , pp. 7689-7696
    • Shrimankar, P.1    Stordal, L.2    Maurer, R.3
  • 30
    • 0014007813 scopus 로고
    • Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductases
    • Siegel, L. M., and K. J. Monty. 1966. Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductases. Biochim. Biophys. Acta 112:346-362.
    • (1966) Biochim. Biophys. Acta , vol.112 , pp. 346-362
    • Siegel, L.M.1    Monty, K.J.2
  • 31
    • 0026802050 scopus 로고
    • Enriched sources of Escherichia coli replication proteins. the dnaG primasc is a zinc metallo-protein
    • Stamford, N. P. J., P. E. Lilley, and N. E. Dixon. 1992. Enriched sources of Escherichia coli replication proteins. The dnaG primasc is a zinc metallo-protein. Biochim. Biophys. Acta 1132:17-25.
    • (1992) Biochim. Biophys. Acta , vol.1132 , pp. 17-25
    • Stamford, N.P.J.1    Lilley, P.E.2    Dixon, N.E.3
  • 33
    • 0027999421 scopus 로고
    • Domains of Escherichia coli primasc: Functional activity of a 47-kDa N-terminal proteolytic fragment
    • Sun, W., J. Tormo, T. A. Steitz, and G. N. Godson. 1994. Domains of Escherichia coli primasc: functional activity of a 47-kDa N-terminal proteolytic fragment. Proc. Natl. Acad. Sci. USA 91:11462-11466.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11462-11466
    • Sun, W.1    Tormo, J.2    Steitz, T.A.3    Godson, G.N.4
  • 34
    • 0027160455 scopus 로고
    • Primase from Escherichia coli primes single-stranded templates in the absence of single-stranded DNA-binding protein or other auxiliary proteins
    • Swart, J., and M. Griep. 1993. Primase from Escherichia coli primes single-stranded templates in the absence of single-stranded DNA-binding protein or other auxiliary proteins. J. Biol. Chem. 268:12970-12976.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12970-12976
    • Swart, J.1    Griep, M.2
  • 35
    • 0028049949 scopus 로고
    • Identification of a domain of Escherichia coli primase required for functional interaction with the DnaB helicase at the replication fork
    • Tougu, K., H. Peng, and K. J. Marians. 1994. Identification of a domain of Escherichia coli primase required for functional interaction with the DnaB helicase at the replication fork. J. Biol. Chem. 269:4675-4682.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4675-4682
    • Tougu, K.1    Peng, H.2    Marians, K.J.3
  • 36
    • 0018264533 scopus 로고
    • dnaB protein of Escherichia coli. Purification and role in the replication of φX174 DNA
    • Ueda, K., R. McMacken, and A. Kornberg. 1977. dnaB protein of Escherichia coli. Purification and role in the replication of φX174 DNA. J. Biol. Chem. 253:261-269.
    • (1977) J. Biol. Chem. , vol.253 , pp. 261-269
    • Ueda, K.1    McMacken, R.2    Kornberg, A.3
  • 38
    • 0026706674 scopus 로고
    • Coordinated leading- And lagging-strand synthesis at the Escherichia coli DNA replication fork. I. Multiple effectors act to modulate Okazaki fragment size
    • Wu, C. A., E. L. Zechner, and K. J. Marians. 1992. Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork. I. Multiple effectors act to modulate Okazaki fragment size. J. Biol. Chem. 267:4030-4044.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4030-4044
    • Wu, C.A.1    Zechner, E.L.2    Marians, K.J.3
  • 39
    • 0029984117 scopus 로고    scopus 로고
    • The hexameric E. coli DnaB helicase can exist in different quaternary states
    • Yu, X., M. J. Jezewska, W. Bujalowski, and E. H. Egelman. 1996. The hexameric E. coli DnaB helicase can exist in different quaternary states. J. Mol. Biol. 259:7-14.
    • (1996) J. Mol. Biol. , vol.259 , pp. 7-14
    • Yu, X.1    Jezewska, M.J.2    Bujalowski, W.3    Egelman, E.H.4
  • 40
    • 0021282250 scopus 로고
    • Cloning vectors that yield high levels of single-stranded DNA for rapid DNA sequencing
    • Zagursky, R., and M. Herman. 1984. Cloning vectors that yield high levels of single-stranded DNA for rapid DNA sequencing. Gene 27:183-191.
    • (1984) Gene , vol.27 , pp. 183-191
    • Zagursky, R.1    Herman, M.2


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