메뉴 건너뛰기




Volumn 8, Issue 1, 1998, Pages 14-18

Helicases: A unifying structural theme?

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; HELICASE; RECA PROTEIN; RNA HELICASE;

EID: 0032007298     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(98)80004-3     Document Type: Article
Times cited : (150)

References (47)
  • 1
    • 0029893874 scopus 로고    scopus 로고
    • Mechanisms of helicase-catalyzed DNA unwinding
    • of special interest. An excellent review of the current literature within the field of study.
    • of special interest Lohman TM, Bjornson KP. Mechanisms of helicase-catalyzed DNA unwinding. Annu Rev Biochem. 65:1996;169-214 An excellent review of the current literature within the field of study.
    • (1996) Annu Rev Biochem , vol.65 , pp. 169-214
    • Lohman, T.M.1    Bjornson, K.P.2
  • 2
    • 0027950513 scopus 로고
    • DNA helicases: Enzymes with essential roles in all aspects of DNA metabolism
    • Matson SW, Bean DW, George JW. DNA helicases: enzymes with essential roles in all aspects of DNA metabolism. Bioessays. 16:1994;13-22.
    • (1994) Bioessays , vol.16 , pp. 13-22
    • Matson, S.W.1    Bean, D.W.2    George, J.W.3
  • 3
    • 0026569419 scopus 로고
    • D-E-A-D protein family of putative RNA helicases
    • Schmid SR, Linder P. D-E-A-D protein family of putative RNA helicases. Mol Microbiol. 6:1992;283-292.
    • (1992) Mol Microbiol , vol.6 , pp. 283-292
    • Schmid, S.R.1    Linder, P.2
  • 4
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequence comparisons and structure - Function relationships
    • Gorbalenya AE, Koonin EV. Helicases: amino acid sequence comparisons and structure - function relationships. Curr Opin Struct Biol. 3:1993;419-429.
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 5
    • 0029856618 scopus 로고    scopus 로고
    • Crystal structure of a DExx box helicase
    • of outstanding interest. This paper describes the first crystal structure of any helicase. The structure reveals an unexpected homology with the ATP-binding domain of RecA and tandem repeat of this fold, with the ATP-binding site situated between them.
    • of outstanding interest Subramanya HS, Bird LE, Brannigan JA, Wigley DB. Crystal structure of a DExx box helicase. Nature. 384:1996;379-383 This paper describes the first crystal structure of any helicase. The structure reveals an unexpected homology with the ATP-binding domain of RecA and tandem repeat of this fold, with the ATP-binding site situated between them.
    • (1996) Nature , vol.384 , pp. 379-383
    • Subramanya, H.S.1    Bird, L.E.2    Brannigan, J.A.3    Wigley, D.B.4
  • 6
    • 0026500416 scopus 로고
    • The structure of the E. coli RecA protein monomer and polymer
    • Story RM, Steitz TA. The structure of the E. coli RecA protein monomer and polymer. Nature. 355:1992;318-325.
    • (1992) Nature , vol.355 , pp. 318-325
    • Story, R.M.1    Steitz, T.A.2
  • 7
    • 0026584599 scopus 로고
    • Structure of the RecA protein - ADP complex
    • Story RM, Weber IT, Steitz TA. Structure of the RecA protein - ADP complex. Nature. 355:1992;374-376.
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Weber, I.T.2    Steitz, T.A.3
  • 8
    • 0030979410 scopus 로고    scopus 로고
    • Structure of the hepatitis C virus RNA helicase domain
    • of outstanding interest. The authors present the first crystal structure of an RNA helicase.
    • of outstanding interest Yao NH, Hesson T, Cable M, Hong Z, Kwong AD, Le HV, Weber PC. Structure of the hepatitis C virus RNA helicase domain. Nat Struct Biol. 4:1997;463-467 The authors present the first crystal structure of an RNA helicase.
    • (1997) Nat Struct Biol , vol.4 , pp. 463-467
    • Yao, N.H.1    Hesson, T.2    Cable, M.3    Hong, Z.4    Kwong, A.D.5    Le, H.V.6    Weber, P.C.7
  • 9
    • 0030740262 scopus 로고    scopus 로고
    • Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP
    • of outstanding interest. The structure of the complex of Rep helicase with a single-stranded 16 base DNA oligonucleotide is described. Two protein monomers bind to the same DNA molecule but each molecule adopts a different conformation. These different conformations are thought to be essential for the overall mechanism of the enzyme.
    • of outstanding interest Korolev S, Hsieh J, Gauss GH, Lohman TM, Waksman G. Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell. 90:1997;635-647 The structure of the complex of Rep helicase with a single-stranded 16 base DNA oligonucleotide is described. Two protein monomers bind to the same DNA molecule but each molecule adopts a different conformation. These different conformations are thought to be essential for the overall mechanism of the enzyme.
    • (1997) Cell , vol.90 , pp. 635-647
    • Korolev, S.1    Hsieh, J.2    Gauss, G.H.3    Lohman, T.M.4    Waksman, G.5
  • 10
    • 0030065608 scopus 로고    scopus 로고
    • Two domains of superfamily I helicases may exist as separate proteins
    • of outstanding interest
    • of outstanding interest Koonin EV, Rudd KE. Two domains of superfamily I helicases may exist as separate proteins. Protein Sci. 5:1996;178-180.
    • (1996) Protein Sci , vol.5 , pp. 178-180
    • Koonin, E.V.1    Rudd, K.E.2
  • 11
    • 0030586054 scopus 로고    scopus 로고
    • Homomorphous hexameric helicases: Tales from the ring cycle
    • An excellent mini review of the present electron microscopy evidence for a common structure amongst hexameric DNA helicases.
    • Egelman EH. Homomorphous hexameric helicases: tales from the ring cycle. Structure. 4:1996;759-762 An excellent mini review of the present electron microscopy evidence for a common structure amongst hexameric DNA helicases.
    • (1996) Structure , vol.4 , pp. 759-762
    • Egelman, E.H.1
  • 13
    • 0029039925 scopus 로고
    • Bacteriophage T7 helicase/primase form rings around single-stranded DNA that suggest a general structure for hexameric helicases
    • Egelman EH, Yu X, Wild R, Hingorani M, Patel SS. Bacteriophage T7 helicase/primase form rings around single-stranded DNA that suggest a general structure for hexameric helicases. Proc Natl Acad Sci USA. 92:1995;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.4    Patel, S.S.5
  • 14
    • 0024550638 scopus 로고
    • ATP-dependent assembly of double hexamers of SV40 T-antigen at the viral origin of DNA-replication
    • Mastrangelo IA, Hough PVC, Wall JS, Dodson M, Dean FB, Hurwitz J. ATP-dependent assembly of double hexamers of SV40 T-antigen at the viral origin of DNA-replication. Nature. 338:1989;658-662.
    • (1989) Nature , vol.338 , pp. 658-662
    • Mastrangelo, I.A.1    Hough, P.V.C.2    Wall, J.S.3    Dodson, M.4    Dean, F.B.5    Hurwitz, J.6
  • 15
    • 0031585985 scopus 로고    scopus 로고
    • Six molecules of SV40 large T antigen assemble in a propeller-shaped particle around a channel
    • San Martin MC, Gruss C, Carazo JM. Six molecules of SV40 large T antigen assemble in a propeller-shaped particle around a channel. J Mol Biol. 268:1997;15-20.
    • (1997) J Mol Biol , vol.268 , pp. 15-20
    • San Martin, M.C.1    Gruss, C.2    Carazo, J.M.3
  • 16
    • 0029147295 scopus 로고
    • A structural model for the Escherichia coli DnaB helicase based on electron microscopy data
    • San Martin MC, Stamford NPJ, Dammerova N, Dixon NE, Carazo JM. A structural model for the Escherichia coli DnaB helicase based on electron microscopy data. J Struct Biol. 114:1995;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
  • 17
    • 0026444104 scopus 로고
    • Purification and properties of the RuvA and RuvB proteins of Escherichia coli
    • Tsaneva IR, Illing GT, Lloyd R, West SC. Purification and properties of the RuvA and RuvB proteins of Escherichia coli. Mol Gen Genet. 235:1992;1-10.
    • (1992) Mol Gen Genet , vol.235 , pp. 1-10
    • Tsaneva, I.R.1    Illing, G.T.2    Lloyd, R.3    West, S.C.4
  • 18
    • 0026597267 scopus 로고
    • Physical properties of the Escherichia coli transcription termination factor Rho. II. Quaternary structure of the Rho hexamer
    • Geiselmann J, Seifreid SE, Yager TD, Liang C, von Hippel PH. Physical properties of the Escherichia coli transcription termination factor Rho. II. Quaternary structure of the Rho hexamer. Biochemistry. 31:1992;121-132.
    • (1992) Biochemistry , vol.31 , pp. 121-132
    • Geiselmann, J.1    Seifreid, S.E.2    Yager, T.D.3    Liang, C.4    Von Hippel, P.H.5
  • 19
    • 0028905501 scopus 로고
    • The phage T4-coded DNA replication helicase (gp41) forms a hexamer upon activation by nucleoside triphosphate
    • Dong F, Gogol EP, von Hippel PH. The phage T4-coded DNA replication helicase (gp41) forms a hexamer upon activation by nucleoside triphosphate. J Biol Chem. 270:1995;7462-7473.
    • (1995) J Biol Chem , vol.270 , pp. 7462-7473
    • Dong, F.1    Gogol, E.P.2    Von Hippel, P.H.3
  • 20
    • 0029984117 scopus 로고    scopus 로고
    • The hexameric E. coli DnaB helicase exists in several different quaternary states
    • Yu X, Jezewska MJ, Bujalowski W, Egelman EH. The hexameric E. coli DnaB helicase exists in several different quaternary states. J Mol Biol. 259:1996;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
  • 21
    • 0023689074 scopus 로고
    • UL5, a protein required for HSV DNA synthesis. Genetic analysis, overexpression in Escherichia coli, and generation of polyclonal antibodies
    • Zhu L, Weller SK. UL5, a protein required for HSV DNA synthesis. Genetic analysis, overexpression in Escherichia coli, and generation of polyclonal antibodies. Virology. 166:1988;366-378.
    • (1988) Virology , vol.166 , pp. 366-378
    • Zhu, L.1    Weller, S.K.2
  • 22
    • 0024296969 scopus 로고
    • A DNA helicase induced by herpes simplex virus type 1
    • Crute JJ, Mocarski ES, Lehman IR. A DNA helicase induced by herpes simplex virus type 1. Nucleic Acids Res. 16:1988;6585-6596.
    • (1988) Nucleic Acids Res , vol.16 , pp. 6585-6596
    • Crute, J.J.1    Mocarski, E.S.2    Lehman, I.R.3
  • 23
    • 0023903468 scopus 로고
    • The unwinding of duplex regions in DNA by the simian virus 40 large tumour antigen-associated DNA helicase activity
    • Goetz GS, Dean FB, Hurwitz J, Matson SW. The unwinding of duplex regions in DNA by the simian virus 40 large tumour antigen-associated DNA helicase activity. J Biol Chem. 263:1988;383-392.
    • (1988) J Biol Chem , vol.263 , pp. 383-392
    • Goetz, G.S.1    Dean, F.B.2    Hurwitz, J.3    Matson, S.W.4
  • 24
    • 0023906245 scopus 로고
    • Simian virus 40 large T antigen DNA helicase: Characterisation of the ATPase dependent unwinding activity and its substrate requirements
    • Wiekowski M, Schwarz MW, Stahl H. Simian virus 40 large T antigen DNA helicase: Characterisation of the ATPase dependent unwinding activity and its substrate requirements. J Biol Chem. 263:1988;436-442.
    • (1988) J Biol Chem , vol.263 , pp. 436-442
    • Wiekowski, M.1    Schwarz, M.W.2    Stahl, H.3
  • 25
    • 0030924142 scopus 로고    scopus 로고
    • Reversal in the direction of movement of a molecular motor
    • Henningsen U, Schliwa M. Reversal in the direction of movement of a molecular motor. Nature. 389:1997;93-96.
    • (1997) Nature , vol.389 , pp. 93-96
    • Henningsen, U.1    Schliwa, M.2
  • 26
    • 0030874883 scopus 로고    scopus 로고
    • The directional preference of kinesin motors is specified by an element outside of the motor catalytic domain
    • Case RB, Pierce DW, Hom-Booher N, Hart CL, Vale RD. The directional preference of kinesin motors is specified by an element outside of the motor catalytic domain. Cell. 90:1997;959-966.
    • (1997) Cell , vol.90 , pp. 959-966
    • Case, R.B.1    Pierce, D.W.2    Hom-Booher, N.3    Hart, C.L.4    Vale, R.D.5
  • 27
    • 0024278984 scopus 로고
    • Structure of helical RecA-DNA complexes. 3. The structural polarity of RecA filaments and functional polarity in the RecA-mediated strand exchange-reaction
    • Stasiak A, Egelman EH, Howard-Flanders P. Structure of helical RecA-DNA complexes. 3. The structural polarity of RecA filaments and functional polarity in the RecA-mediated strand exchange-reaction. J Mol Biol. 202:1988;659-662.
    • (1988) J Mol Biol , vol.202 , pp. 659-662
    • Stasiak, A.1    Egelman, E.H.2    Howard-Flanders, P.3
  • 29
    • 0024843435 scopus 로고
    • Visualization of RecA protein and its complexes with DNA by quick-freeze deep-etch electron-microscopy
    • Heuser J, Griffith J. Visualization of RecA protein and its complexes with DNA by quick-freeze deep-etch electron-microscopy. J Mol Biol. 210:1989;473-484.
    • (1989) J Mol Biol , vol.210 , pp. 473-484
    • Heuser, J.1    Griffith, J.2
  • 30
    • 0025661990 scopus 로고
    • RecA protein self-assembly. 2. Analytical equilibrium ultracentrifugation studies of the entropy-driven self-association of RecA
    • Brenner SL, Zlotnick A, Stafford WFI. RecA protein self-assembly. 2. Analytical equilibrium ultracentrifugation studies of the entropy-driven self-association of RecA. J Mol Biol. 216:1990;949-964.
    • (1990) J Mol Biol , vol.216 , pp. 949-964
    • Brenner, S.L.1    Zlotnick, A.2    Stafford, W.F.I.3
  • 32
    • 0020405926 scopus 로고
    • New properties of simian virus 40 large T antigen
    • Seif R. New properties of simian virus 40 large T antigen. Mol Cell Biol. 2:1982;1463-1471.
    • (1982) Mol Cell Biol , vol.2 , pp. 1463-1471
    • Seif, R.1
  • 33
    • 0028128864 scopus 로고
    • Phylogenetic analysis of sequences from diverse bacteria with homology to Escherichia coli rho gene
    • Opperman T, Richardson JP. Phylogenetic analysis of sequences from diverse bacteria with homology to Escherichia coli rho gene. J Bacteriol. 176:1994;5033-5043.
    • (1994) J Bacteriol , vol.176 , pp. 5033-5043
    • Opperman, T.1    Richardson, J.P.2
  • 34
    • 0029565119 scopus 로고
    • Structural and functional dissections of transcription factor terminator factor Rho by random mutagenesis
    • Miwa Y, Horiguchi T, Shigesada K. Structural and functional dissections of transcription factor terminator factor Rho by random mutagenesis. J Mol Biol. 254:1995;815-837.
    • (1995) J Mol Biol , vol.254 , pp. 815-837
    • Miwa, Y.1    Horiguchi, T.2    Shigesada, K.3
  • 35
    • 1842328563 scopus 로고    scopus 로고
    • Characterisation and crystallisation of the helicase domain of bacteriophage T7 gene 4 protein
    • Bird LE, Häkannsson K, Pan H, Wigley DB. Characterisation and crystallisation of the helicase domain of bacteriophage T7 gene 4 protein. Nucleic Acids Res. 25:1997;2020-2026.
    • (1997) Nucleic Acids Res , vol.25 , pp. 2020-2026
    • Bird, L.E.1    Häkannsson, K.2    Pan, H.3    Wigley, D.B.4
  • 36
    • 10244263498 scopus 로고    scopus 로고
    • Biochemical analysis of mutant T7 primase/helicase proteins defective in DNA binding, nucleotide hydrolysis, and the coupling of hydrolysis with DNA unwinding
    • Washington MT, Rosenberg AH, Griffin K, Studier FW, Patel SS. Biochemical analysis of mutant T7 primase/helicase proteins defective in DNA binding, nucleotide hydrolysis, and the coupling of hydrolysis with DNA unwinding. J Biol Chem. 271:1996;26825-26834.
    • (1996) J Biol Chem , vol.271 , pp. 26825-26834
    • Washington, M.T.1    Rosenberg, A.H.2    Griffin, K.3    Studier, F.W.4    Patel, S.S.5
  • 37
    • 0027214787 scopus 로고
    • Negative cooperativity in the binding of nucleotides to Escherichia coli replicative helicase DnaB protein. Interactions with fluorescent nucleotide analogs
    • Bujalowski W, Klonowska MM. Negative cooperativity in the binding of nucleotides to Escherichia coli replicative helicase DnaB protein. Interactions with fluorescent nucleotide analogs. Biochemistry. 32:1993;5888-5900.
    • (1993) Biochemistry , vol.32 , pp. 5888-5900
    • Bujalowski, W.1    Klonowska, M.M.2
  • 39
    • 0026546001 scopus 로고
    • Allosteric effects of nucleotide cofactors on Escherichia coli Rep helicase-DNA binding
    • Wong I, Lohman TM. Allosteric effects of nucleotide cofactors on Escherichia coli Rep helicase-DNA binding. Science. 256:1992;350-355.
    • (1992) Science , vol.256 , pp. 350-355
    • Wong, I.1    Lohman, T.M.2
  • 40
    • 0018353521 scopus 로고
    • Enzyme-catalyzed DNA unwinding: Studies on Escherichia coli rep protein
    • Yarranton GT, Geftner ML. Enzyme-catalyzed DNA unwinding: studies on Escherichia coli rep protein. Proc Natl Acad Sci USA. 76:1979;1658-1662.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 1658-1662
    • Yarranton, G.T.1    Geftner, M.L.2
  • 41
    • 0031031958 scopus 로고    scopus 로고
    • Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase
    • of special interest. Using kinetic data, the step size of the UvrD helicase is shown to be 4-5 base pairs.
    • of special interest Ali JA, Lohman TM. Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase. Science. 275:1997;377-380 Using kinetic data, the step size of the UvrD helicase is shown to be 4-5 base pairs.
    • (1997) Science , vol.275 , pp. 377-380
    • Ali, J.A.1    Lohman, T.M.2
  • 42
    • 0026356376 scopus 로고
    • Bacterial DNA replication initiation protein PriA is related to proteins belonging to the 'DEAD-box' family
    • Ouzounis CA, Blencowe BJ. Bacterial DNA replication initiation protein PriA is related to proteins belonging to the 'DEAD-box' family. Nucleic Acids Res. 19:1991;6953.
    • (1991) Nucleic Acids Res , vol.19 , pp. 6953
    • Ouzounis, C.A.1    Blencowe, B.J.2
  • 44
    • 0028047404 scopus 로고
    • Genetic organisation of the conjugal DNA processing region of the IncW plasmid R388
    • Llosa M, Bolland S, de la Cruz F. Genetic organisation of the conjugal DNA processing region of the IncW plasmid R388. J Mol Biol. 235:1994;448-464.
    • (1994) J Mol Biol , vol.235 , pp. 448-464
    • Llosa, M.1    Bolland, S.2    De La Cruz, F.3
  • 45
    • 0029789574 scopus 로고    scopus 로고
    • Molecular cloning of Drosophila mus308, a gene involved in DNA cross-link repair with homology to prokaryotic DNA polymerase I genes
    • Harris PV, Mazina OM, Leonhardt EA, Case RB, Boyd JB, Burtis KC. Molecular cloning of Drosophila mus308, a gene involved in DNA cross-link repair with homology to prokaryotic DNA polymerase I genes. Mol Cell Biol. 16:1996;5764-5771.
    • (1996) Mol Cell Biol , vol.16 , pp. 5764-5771
    • Harris, P.V.1    Mazina, O.M.2    Leonhardt, E.A.3    Case, R.B.4    Boyd, J.B.5    Burtis, K.C.6
  • 47
    • 0029157378 scopus 로고
    • Evolution of the SNF2 family of proteins: Subfamilies with distinct sequences and functions
    • Eisen JA, Sweder KS, Hanawit PC. Evolution of the SNF2 family of proteins: subfamilies with distinct sequences and functions. Nucleic Acids Res. 23:1995;2715-2723.
    • (1995) Nucleic Acids Res , vol.23 , pp. 2715-2723
    • Eisen, J.A.1    Sweder, K.S.2    Hanawit, P.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.