메뉴 건너뛰기




Volumn 4, Issue 7, 1996, Pages 759-762

Homomorphous hexameric helicases: Tales from the ring cycle

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0030586054     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00081-0     Document Type: Article
Times cited : (37)

References (35)
  • 1
    • 0024344173 scopus 로고
    • Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes
    • Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P. & Blinov, V.M. (1989). Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes. Nucleic Acids. Res. 17, 4713-4730.
    • (1989) Nucleic Acids. Res. , vol.17 , pp. 4713-4730
    • Gorbalenya, A.E.1    Koonin, E.V.2    Donchenko, A.P.3    Blinov, V.M.4
  • 2
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- And beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J.E., Saraste, M., Runswick, M.J. & Gay, N.J. (1982). Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1, 945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 3
    • 0027950513 scopus 로고
    • DNA helicases: Enzymes with essential roles in all aspects of DNA metabolism
    • Matson, S.W., Bean, D.W. & George, J.W. (1994). DNA helicases: enzymes with essential roles in all aspects of DNA metabolism. Bioessays 16, 13-22.
    • (1994) Bioessays , vol.16 , pp. 13-22
    • Matson, S.W.1    Bean, D.W.2    George, J.W.3
  • 4
    • 0026547088 scopus 로고
    • The XPD complementation group. Insights into xeroderma pigmentosum, Cockayne's syndrome and trichothiodystrophy
    • Johnson, R.T. & Squires, S. (1992). The XPD complementation group. Insights into xeroderma pigmentosum, Cockayne's syndrome and trichothiodystrophy. Mutat. Res. 273, 97-118.
    • (1992) Mutat. Res. , vol.273 , pp. 97-118
    • Johnson, R.T.1    Squires, S.2
  • 5
    • 0028785586 scopus 로고
    • The Bloom's syndrome gene product is homologous to RecQ helicases
    • Ellis, N.A., et al., & German, J. (1995). The Bloom's syndrome gene product is homologous to RecQ helicases. Cell 83, 655-666.
    • (1995) Cell , vol.83 , pp. 655-666
    • Ellis, N.A.1    German, J.2
  • 6
    • 15844409553 scopus 로고    scopus 로고
    • Positional cloning of the Werner's syndrome gene
    • Yu, C.-E., et al., & Schellenberg, G.D. (1996). Positional cloning of the Werner's syndrome gene. Science 272, 258-262.
    • (1996) Science , vol.272 , pp. 258-262
    • Yu, C.-E.1    Schellenberg, G.D.2
  • 7
    • 0028968305 scopus 로고
    • Structure of a multisubunit complex that promotes DNA branch migration
    • Parsons, C.A., Stasiak, A., Bennet, R.J. & West, S.C. (1995). Structure of a multisubunit complex that promotes DNA branch migration. Nature 374, 375-378.
    • (1995) Nature , vol.374 , pp. 375-378
    • Parsons, C.A.1    Stasiak, A.2    Bennet, R.J.3    West, S.C.4
  • 8
    • 0029893874 scopus 로고    scopus 로고
    • Mechanisms of helicase-catalyzed DNA unwinding
    • Lohman, T.M. & Bjornson, K.P. (1996). Mechanisms of helicase-catalyzed DNA unwinding. Annu. Rev. Biochem. 65, 169-214.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 169-214
    • Lohman, T.M.1    Bjornson, K.P.2
  • 9
    • 0022977660 scopus 로고
    • The Escherichia coli dnaB replication protein is a DNA helicase
    • LeBowitz, J.H. & McMacken, R. (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.H.1    McMacken, R.2
  • 10
    • 0017842412 scopus 로고
    • The dnaB gene product of Escherichia coli. I. Purification, homogeneity, and physical properties
    • Reha-Krantz, L.J. & Hurwitz, J. (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.J.1    Hurwitz, J.2
  • 11
    • 0026091055 scopus 로고
    • Structure and assembly of the Escherichia coli transcription termination factor rho and its interactions with RNA. I. Cryoelectron microscopic studies
    • Gogol, E.P., Seifried, S.E. & von Hippel, P.H. (1991). Structure and assembly of the Escherichia coli transcription termination factor rho and its interactions with RNA. I. Cryoelectron microscopic studies. J. Mol. Biol. 221, 1127-1138.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1127-1138
    • Gogol, E.P.1    Seifried, S.E.2    Von Hippel, P.H.3
  • 13
    • 0024550638 scopus 로고
    • ATP-dependent assembly of double hexamers of SV40 T antigen at the viral origin of DNA replication
    • Mastrangelo, I.A., Hough, P.V.C., Wall, J.S., Dobson, M., Dean, F.B. & Hurwitz, J. (1989). ATP-dependent assembly of double hexamers of SV40 T antigen at the viral origin of DNA replication. Nature 338, 658-662.
    • (1989) Nature , vol.338 , pp. 658-662
    • Mastrangelo, I.A.1    Hough, P.V.C.2    Wall, J.S.3    Dobson, M.4    Dean, F.B.5    Hurwitz, J.6
  • 14
    • 0027195850 scopus 로고
    • Oligomeric structure of bacteriophage T7 DNA primase/helicase proteins
    • Patel, S.S. & Hingorani, M.M. (1993). Oligomeric structure of bacteriophage T7 DNA primase/helicase proteins. J. Biol. Chem. 268, 10668-10675.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10668-10675
    • Patel, S.S.1    Hingorani, M.M.2
  • 15
    • 0028905501 scopus 로고
    • The phage T4-coded DNA replication helicase (gp41) forms a hexamer upon activation by nucleoside triphosphate
    • Dong, F., Gogol, E.P. &von Hippel, P.H. (1995). The phage T4-coded DNA replication helicase (gp41) forms a hexamer upon activation by nucleoside triphosphate. J. Biol. Chem. 270, 7462-7473.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7462-7473
    • Dong, F.1    Gogol, E.P.2    Von Hippel, P.H.3
  • 16
    • 0026546001 scopus 로고
    • Allosteric effects of nucleotide cofactors on Escherichia coli Rep helicase-DNA binding
    • Wong, I. & Lohman, T.M. (1992). Allosteric effects of nucleotide cofactors on Escherichia coli Rep helicase-DNA binding. Science 256, 350-355.
    • (1992) Science , vol.256 , pp. 350-355
    • Wong, I.1    Lohman, T.M.2
  • 17
    • 0027455421 scopus 로고
    • Overexpression, purification, DNA binding, and dimerization of the Escherichia coli uvrD gene product (helicase II)
    • Runyon, G.T., Wong, I.& Lohman, T.M. (1993). Overexpression, purification, DNA binding, and dimerization of the Escherichia coli uvrD gene product (helicase II). Biochemistry 32, 602-612.
    • (1993) Biochemistry , vol.32 , pp. 602-612
    • Runyon, G.T.1    Wong, I.2    Lohman, T.M.3
  • 18
    • 0027905008 scopus 로고
    • DNA repair helicase: A component of BTF2 (TFIIH) basic transcription factor
    • Schaeffer, L, et al., & Egly, J.M. (1993). DNA repair helicase: a component of BTF2 (TFIIH) basic transcription factor. Science 260, 58-63.
    • (1993) Science , vol.260 , pp. 58-63
    • Schaeffer, L.1    Egly, J.M.2
  • 19
    • 0028127919 scopus 로고
    • Structures of large T antigen at the origin of SV40 DNA replication by atomic force microscopy
    • Mastrangelo, I.A., Bezanilla, M., Hansma, P.K., Hough, P.V. & Hansma, H.G. (1994). Structures of large T antigen at the origin of SV40 DNA replication by atomic force microscopy. Biophys. J. 66, 293-298.
    • (1994) Biophys. J. , vol.66 , pp. 293-298
    • Mastrangelo, I.A.1    Bezanilla, M.2    Hansma, P.K.3    Hough, P.V.4    Hansma, H.G.5
  • 20
    • 0029039925 scopus 로고
    • Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases
    • Egelman, E.H., Yu, X., Wild, R., Hingorani, M.M. & Patel, S.S. (1995). Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases. Proc. Natl. Acad. Sci. USA 92, 3869-3873.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3869-3873
    • Egelman, E.H.1    Yu, X.2    Wild, R.3    Hingorani, M.M.4    Patel, S.S.5
  • 21
    • 0029147295 scopus 로고
    • A structural model for the Escherichia coli DnaB helicase based on electron microscopy data
    • San Martin, M.C., Stamford, N.P.J., Dammerova, N., Dixon, N.E. & Carazo, J.M. (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
  • 22
    • 0029984117 scopus 로고    scopus 로고
    • The E. coli DnaB helicase exists in several different hexameric states
    • Yu, X., Jezewska, M.J., Bujalowski, W. & Egelman, E.H. (1996). The E. coli DnaB helicase exists in several different hexameric 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
  • 23
    • 0026045763 scopus 로고
    • Structure and assembly of the Escherichia coli transcription termination factor rho and its interactions with RNA. II. Physical chemical studies
    • Seifried, S.E., Bjornson, K.P. & von Hippel, P.H. (1991). Structure and assembly of the Escherichia coli transcription termination factor rho and its interactions with RNA. II. Physical chemical studies. J. Mol. Biol. 221, 1139-1151.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1139-1151
    • Seifried, S.E.1    Bjornson, K.P.2    Von Hippel, P.H.3
  • 24
    • 0026597267 scopus 로고
    • Physical properties of the Escherichia coli transcription termination factor rho. II. Quaternary structure of the rho hexamer
    • Geiselmann, J., Seifried, S.E., Yager, T.D., Liang, C. & von Hippel, P.H. (1992). Physical properties of the Escherichia coli transcription termination factor rho. II. Quaternary structure of the rho hexamer. Biochemistry 31, 121-132.
    • (1992) Biochemistry , vol.31 , pp. 121-132
    • Geiselmann, J.1    Seifried, S.E.2    Yager, T.D.3    Liang, C.4    Von Hippel, P.H.5
  • 25
    • 0027250342 scopus 로고
    • A physical model for the translocation and helicase activities of Escherichia coli transcription termination protein Rho
    • Geiselmann, J., Wang, Y., Seifried, S.E. & von Hippel, P.H. (1993). A physical model for the translocation and helicase activities of Escherichia coli transcription termination protein Rho. Proc. Natl. Acad. Sci. USA 90, 7754-7758.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7754-7758
    • Geiselmann, J.1    Wang, Y.2    Seifried, S.E.3    Von Hippel, P.H.4
  • 26
    • 0026770783 scopus 로고
    • The Simian Virus 40 T antigen double hexamer assembles around the DNA at the replication origin
    • Dean, F.B., Borowiec, J.A., Eki, T. & Hurwitz, J. (1992). The Simian Virus 40 T antigen double hexamer assembles around the DNA at the replication origin. J. Biol. Chem. 267, 14129-14137.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14129-14137
    • Dean, F.B.1    Borowiec, J.A.2    Eki, T.3    Hurwitz, J.4
  • 27
    • 0029072199 scopus 로고
    • Interactions of Escherichia coli primary replicative helicase DnaB protein with single-stranded DNA. The nucleic acid does not wrap around the protein hexamer
    • Bujalowski, W. & Jezewska, M.J. (1995). Interactions of Escherichia coli primary replicative helicase DnaB protein with single-stranded DNA. The nucleic acid does not wrap around the protein hexamer. Biochemistry 34, 8513-8519.
    • (1995) Biochemistry , vol.34 , pp. 8513-8519
    • Bujalowski, W.1    Jezewska, M.J.2
  • 28
    • 0030045742 scopus 로고    scopus 로고
    • Cooperative interactions of nucleotide cofactors are linked to oligomerization and DNA binding in bacteriophage T7 gene 4 helicases
    • Hingorani, M.M. & Patel, S.S. (1996). Cooperative interactions of nucleotide cofactors are linked to oligomerization and DNA binding in bacteriophage T7 gene 4 helicases. Biochemistry 35, 2218-2228.
    • (1996) Biochemistry , vol.35 , pp. 2218-2228
    • Hingorani, M.M.1    Patel, S.S.2
  • 29
    • 0023770755 scopus 로고
    • Escherichia coli transcription termination protein rho has three hydrolytic sites for ATP
    • Stitt, B.L. (1988). Escherichia coli transcription termination protein rho has three hydrolytic sites for ATP. J. Biol. Chem. 263, 11130-11137.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11130-11137
    • Stitt, B.L.1
  • 30
    • 0026444104 scopus 로고
    • Purification and properties of the RuvA and RuvB proteins of Escherichia coli
    • Tsaneva, I.R., Illing, G.T., Lloyd, R.G. & West, S.C. (1992). Purification and properties of the RuvA and RuvB proteins of Escherichia coli. Mol. Gen. Genet. 235, 1-10.
    • (1992) Mol. Gen. Genet. , vol.235 , pp. 1-10
    • Tsaneva, I.R.1    Illing, G.T.2    Lloyd, R.G.3    West, S.C.4
  • 31
    • 0022829375 scopus 로고
    • The dnaB protein of Escherichia coli: Mechanism of nucleotide binding, hydrolysis, and modulation by dnaC protein
    • Biswas, E.E., Biswas, S.B. & Bishop, J.E. (1986). The dnaB protein of Escherichia coli: mechanism of nucleotide binding, hydrolysis, and modulation by dnaC protein. Biochemistry 25, 7368-7374.
    • (1986) Biochemistry , vol.25 , pp. 7368-7374
    • Biswas, E.E.1    Biswas, S.B.2    Bishop, J.E.3
  • 32
    • 0027214787 scopus 로고
    • Negative cooperativity in the binding of nucleotide to Escherichia coli replicative helicase DnaB protein. Interactions with fluorescent nucleotide analogs
    • Bujalowski, W. & Klonowska, M.M. (1993). Negative cooperativity in the binding of nucleotide to Escherichia coli replicative helicase DnaB protein. Interactions with fluorescent nucleotide analogs. Biochemistry 32, 5888-5900.
    • (1993) Biochemistry , vol.32 , pp. 5888-5900
    • Bujalowski, W.1    Klonowska, M.M.2
  • 33
    • 0030053611 scopus 로고    scopus 로고
    • Structural organization of transcription termination factor rho
    • Richardson, J.P. (1996). Structural organization of transcription termination factor rho. J. Biol. Chem. 271, 1251-1254.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1251-1254
    • Richardson, J.P.1
  • 34
    • 0029565119 scopus 로고
    • Structural and functional dissections of transcription termination factor rho by random mutagenesis
    • Miwa, Y., Horiguchi, T. & Shigesada, K. (1995). Structural and functional dissections of transcription termination factor rho by random mutagenesis. J. Mol. Biol. 254, 815-837.
    • (1995) J. Mol. Biol. , vol.254 , pp. 815-837
    • Miwa, Y.1    Horiguchi, T.2    Shigesada, K.3
  • 35
    • 0028114231 scopus 로고
    • Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams, J.P., Leslie, A.G., Lutter, R. & Walker, J.E. (1994). Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. Nature 370, 621-628.
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.