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Volumn 36, Issue 18, 2008, Pages 5882-5895

The reverse gyrase helicase-like domain is a nucleotide-dependent switch that is attenuated by the topoisomerase domain

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DNA TOPOISOMERASE (ATP HYDROLYSING); PLASMID DNA;

EID: 54549124757     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkn587     Document Type: Article
Times cited : (25)

References (33)
  • 1
    • 0021154312 scopus 로고
    • Reverse gyrase-a topoisomerase which introduces positive superhelical turns into DNA
    • Kikuchi,A. and Asai,K. (1984) Reverse gyrase-a topoisomerase which introduces positive superhelical turns into DNA. Nature, 309 677-681.
    • (1984) Nature , vol.309 , pp. 677-681
    • Kikuchi, A.1    Asai, K.2
  • 2
    • 0036574857 scopus 로고    scopus 로고
    • A hot story from comparative genomics: Reverse gyrase is the only hyperthermophile-specific protein
    • Forterre,P. (2002) A hot story from comparative genomics: Reverse gyrase is the only hyperthermophile-specific protein. Trends Genet., 18, 236-237.
    • (2002) Trends Genet , vol.18 , pp. 236-237
    • Forterre, P.1
  • 3
    • 3042814762 scopus 로고    scopus 로고
    • Reverse gyrase is not a prerequisite for hyperthermophilic life
    • Atomi,H., Matsumi,R. and Imanaka,T. (2004) Reverse gyrase is not a prerequisite for hyperthermophilic life. J. Bacteriol., 186, 4829-4833.
    • (2004) J. Bacteriol , vol.186 , pp. 4829-4833
    • Atomi, H.1    Matsumi, R.2    Imanaka, T.3
  • 4
    • 3142753959 scopus 로고    scopus 로고
    • Reverse gyrase has heat-protective DNA chaperone activity independent of supercoiling
    • Kampmann,M. and Stock,D. (2004) Reverse gyrase has heat-protective DNA chaperone activity independent of supercoiling. Nucleic Acids Res. 32, 3537-3545.
    • (2004) Nucleic Acids Res , vol.32 , pp. 3537-3545
    • Kampmann, M.1    Stock, D.2
  • 5
    • 33646832425 scopus 로고    scopus 로고
    • Reverse gyrase functions as a DNA renaturase: Annealing of complementary single-stranded circles and positive supercoiling of a bubble substrate
    • Hsieh,T.S. and Plank,J.L. (2006) Reverse gyrase functions as a DNA renaturase: Annealing of complementary single-stranded circles and positive supercoiling of a bubble substrate. J. Biol. Chem., 281, 5640-5647.
    • (2006) J. Biol. Chem , vol.281 , pp. 5640-5647
    • Hsieh, T.S.1    Plank, J.L.2
  • 6
    • 0030052404 scopus 로고    scopus 로고
    • A two-subunit type I DNA topoisomerase (reverse gyrase) from an extreme hyperthermophile
    • Krah,R., Kozyavkin,S.A., Slesarev,A.I. and Gellert,M. (1996) A two-subunit type I DNA topoisomerase (reverse gyrase) from an extreme hyperthermophile. Proc. Natl Acad. Sci. USA, 93, 106-110.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 106-110
    • Krah, R.1    Kozyavkin, S.A.2    Slesarev, A.I.3    Gellert, M.4
  • 7
    • 0030999581 scopus 로고    scopus 로고
    • Reverse gyrase from Methanopyrus kandleri. Reconstitution of an active extremozyme from its two recombinant subunits
    • Krah,R., O'Dea,M.H. and Gellert,M. (1997) Reverse gyrase from Methanopyrus kandleri. Reconstitution of an active extremozyme from its two recombinant subunits. J. Biol. Chem., 272, 13986-13990.
    • (1997) J. Biol. Chem , vol.272 , pp. 13986-13990
    • Krah, R.1    O'Dea, M.H.2    Gellert, M.3
  • 8
    • 0039172550 scopus 로고    scopus 로고
    • Reverse gyrase, the two domains intimately cooperate to promote positive supercoiling
    • Declais,A.C., Marsault,J., Confalonieri,F., de La Tour,C.B. and Duguet,M. (2000) Reverse gyrase, the two domains intimately cooperate to promote positive supercoiling. J. Biol. Chem., 275, 19498-19504.
    • (2000) J. Biol. Chem , vol.275 , pp. 19498-19504
    • Declais, A.C.1    Marsault, J.2    Confalonieri, F.3    de La Tour, C.B.4    Duguet, M.5
  • 10
    • 0036470564 scopus 로고    scopus 로고
    • Crystal structure of reverse gyrase: Insights into the positive supercoiling of DNA
    • Rodriguez,A.C. and Stock,D. (2002) Crystal structure of reverse gyrase: insights into the positive supercoiling of DNA. EMBO J., 21, 418-426.
    • (2002) EMBO J , vol.21 , pp. 418-426
    • Rodriguez, A.C.1    Stock, D.2
  • 11
    • 0037119393 scopus 로고    scopus 로고
    • Studies of a positive supercoiling machine. Nucleotide hydrolysis and a multifunctional "latch" in the mechanism of reverse gyrase
    • Rodriguez,A.C. (2002) Studies of a positive supercoiling machine. Nucleotide hydrolysis and a multifunctional "latch" in the mechanism of reverse gyrase. J. Biol. Chem., 277, 29865-29873.
    • (2002) J. Biol. Chem , vol.277 , pp. 29865-29873
    • Rodriguez, A.C.1
  • 12
    • 0037508506 scopus 로고    scopus 로고
    • Investigating the role of the latch in the positive supercoiling mechanism of reverse gyrase
    • Rodriguez,A.C. (2003) Investigating the role of the latch in the positive supercoiling mechanism of reverse gyrase. Biochemistry, 42, 5993-6004.
    • (2003) Biochemistry , vol.42 , pp. 5993-6004
    • Rodriguez, A.C.1
  • 13
    • 38649106732 scopus 로고    scopus 로고
    • Cooperative binding of ATP and RNA induces a closed conformation in a DEAD box RNA helicase
    • Theissen,B., Karow,A.R., Kohler,J., Gubaev,A. and Klostermeier,D. (2008) Cooperative binding of ATP and RNA induces a closed conformation in a DEAD box RNA helicase. Proc. Natl Acad. Sci. USA, 105, 548-553.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 548-553
    • Theissen, B.1    Karow, A.R.2    Kohler, J.3    Gubaev, A.4    Klostermeier, D.5
  • 14
    • 34447103886 scopus 로고    scopus 로고
    • Adenosine 5′-O-(3-thio)-triphosphate (ATPgammaS) promotes positive supercoiling of DNA by T. maritima reverse gyrase
    • Jungblut,S.P. and Klostermeier,D. (2007) Adenosine 5′-O-(3-thio)-triphosphate (ATPgammaS) promotes positive supercoiling of DNA by T. maritima reverse gyrase. J. Mol. Biol., 371 197-209.
    • (2007) J. Mol. Biol , vol.371 , pp. 197-209
    • Jungblut, S.P.1    Klostermeier, D.2
  • 15
    • 0141856111 scopus 로고    scopus 로고
    • Adenosine 5′-O-(3-thio triphosphate (ATPgammaS) is a substrate for the nucleotide hydrolysis and RNA unwinding activities of eukaryotic translation initiation factor eIF4A
    • Peck,M.L. and Herschlag,D. (2003) Adenosine 5′-O-(3-thio triphosphate (ATPgammaS) is a substrate for the nucleotide hydrolysis and RNA unwinding activities of eukaryotic translation initiation factor eIF4A. RNA, 9, 1180-1187.
    • (2003) RNA , vol.9 , pp. 1180-1187
    • Peck, M.L.1    Herschlag, D.2
  • 16
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier,F.W. (2005) Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif., 41, 207-234.
    • (2005) Protein Expr. Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 17
    • 0025363622 scopus 로고
    • Archaebacterial reverse gyrase cleavage-site specificity is similar to that of eubacterial DNA topoisomerases I
    • Kovalsky,O.I., Kozyavkin,S.A. and Slesarev,A.I. (1990) Archaebacterial reverse gyrase cleavage-site specificity is similar to that of eubacterial DNA topoisomerases I. Nucleic Acids Res., 18, 2801-2805.
    • (1990) Nucleic Acids Res , vol.18 , pp. 2801-2805
    • Kovalsky, O.I.1    Kozyavkin, S.A.2    Slesarev, A.I.3
  • 18
    • 0033558173 scopus 로고    scopus 로고
    • Analysis of DNA cleavage by reverse gyrase from Sulfolobus shibatae B12
    • Jaxel,C., Duguet,M. and Nadal,M. (1999) Analysis of DNA cleavage by reverse gyrase from Sulfolobus shibatae B12. Eur. J. Biochem. 260, 103-111.
    • (1999) Eur. J. Biochem , vol.260 , pp. 103-111
    • Jaxel, C.1    Duguet, M.2    Nadal, M.3
  • 19
    • 0020674810 scopus 로고
    • New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes
    • Hiratsuka,T. (1983) New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes. Biochim. Biophys. Acta, 742, 496-508.
    • (1983) Biochim. Biophys. Acta , vol.742 , pp. 496-508
    • Hiratsuka, T.1
  • 20
    • 0040142238 scopus 로고    scopus 로고
    • Biochemical and kinetic characterization of the RNA helicase activity of eukaryotic initiation factor 4A
    • Rogers,G.W. Jr, Richter,N.J. and Merrick,W.C. (1999) Biochemical and kinetic characterization of the RNA helicase activity of eukaryotic initiation factor 4A. J. Biol. Chem., 274, 12236-12244.
    • (1999) J. Biol. Chem , vol.274 , pp. 12236-12244
    • Rogers Jr, G.W.1    Richter, N.J.2    Merrick, W.C.3
  • 21
    • 0023645211 scopus 로고
    • Intrinsic DNA-dependent ATPase activity of reverse gyrase
    • Shibata,T., Nakasu,S., Yasui,K. and Kikuchi,A. (1987) Intrinsic DNA-dependent ATPase activity of reverse gyrase. J. Biol. Chem., 262, 10419-10421.
    • (1987) J. Biol. Chem , vol.262 , pp. 10419-10421
    • Shibata, T.1    Nakasu, S.2    Yasui, K.3    Kikuchi, A.4
  • 22
    • 0032562239 scopus 로고    scopus 로고
    • The DEAD box protein eIF4A. 1. A minimal kinetic and thermodynamic framework reveals coupled binding of RNA and nucleotide
    • Lorsch,J.R. and Herschlag,D. (1998) The DEAD box protein eIF4A. 1. A minimal kinetic and thermodynamic framework reveals coupled binding of RNA and nucleotide. Biochemistry, 37, 2180-2193.
    • (1998) Biochemistry , vol.37 , pp. 2180-2193
    • Lorsch, J.R.1    Herschlag, D.2
  • 23
    • 0032562221 scopus 로고    scopus 로고
    • The DEAD box protein eIF4A. 2. A cycle of nucleotide and RNA-dependent conformational changes
    • Lorsch,J.R. and Herschlag,D. (1998) The DEAD box protein eIF4A. 2. A cycle of nucleotide and RNA-dependent conformational changes. Biochemistry, 37, 2194-2206.
    • (1998) Biochemistry , vol.37 , pp. 2194-2206
    • Lorsch, J.R.1    Herschlag, D.2
  • 24
    • 0037133527 scopus 로고    scopus 로고
    • Cooperative binding of ATP and RNA substrates to the DEAD/H protein DbpA
    • Polach,K.J. and Uhlenbeck,O.C. (2002) Cooperative binding of ATP and RNA substrates to the DEAD/H protein DbpA. Biochemistry, 41, 3693-3702.
    • (2002) Biochemistry , vol.41 , pp. 3693-3702
    • Polach, K.J.1    Uhlenbeck, O.C.2
  • 25
    • 33750593917 scopus 로고    scopus 로고
    • The DEAD-box protein Ded1 unwinds RNA duplexes by a mode distinct from translocating helicases
    • Yang,Q. and Jankowsky,E. (2006) The DEAD-box protein Ded1 unwinds RNA duplexes by a mode distinct from translocating helicases. Nat. Struct. Mol. Biol., 13, 981-986.
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 981-986
    • Yang, Q.1    Jankowsky, E.2
  • 26
    • 26644450709 scopus 로고    scopus 로고
    • ATP- and ADP-dependent modulation of RNA unwinding and strand annealing activities by the DEAD-box protein DED1
    • Yang,Q. and Jankowsky,E. (2005) ATP- and ADP-dependent modulation of RNA unwinding and strand annealing activities by the DEAD-box protein DED1. Biochemistry, 44, 13591-13601.
    • (2005) Biochemistry , vol.44 , pp. 13591-13601
    • Yang, Q.1    Jankowsky, E.2
  • 27
    • 0021930945 scopus 로고
    • Bacterial DNA topoisomerase I can relax positively supercoiled DNA containing a single-stranded loop
    • Kirkegaard,K. and Wang,J.C. (1985) Bacterial DNA topoisomerase I can relax positively supercoiled DNA containing a single-stranded loop. J. Mol. Biol., 185, 625-637.
    • (1985) J. Mol. Biol , vol.185 , pp. 625-637
    • Kirkegaard, K.1    Wang, J.C.2
  • 28
    • 48249113056 scopus 로고    scopus 로고
    • Translocation and unwinding mechanisms of RNA and DNA helicases
    • Pyle,A.M. (2008) Translocation and unwinding mechanisms of RNA and DNA helicases. Annu. Rev. Biophys., 37, 317-336.
    • (2008) Annu. Rev. Biophys , vol.37 , pp. 317-336
    • Pyle, A.M.1
  • 29
    • 0344129033 scopus 로고    scopus 로고
    • Hera from Thermus thermophilus: The first thermostable DEAD-box helicase with an RNase P protein motif
    • Morlang,S., Weglohner,W. and Franceschi,F. (1999) Hera from Thermus thermophilus: The first thermostable DEAD-box helicase with an RNase P protein motif. J. Mol. Biol., 294, 795-805.
    • (1999) J. Mol. Biol , vol.294 , pp. 795-805
    • Morlang, S.1    Weglohner, W.2    Franceschi, F.3
  • 30
    • 0035903136 scopus 로고    scopus 로고
    • Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F
    • Rogers,G.W. Jr, Richter,N.J., Lima,W.F. and Merrick,W.C. (2001) Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F. J. Biol. Chem., 276, 30914-30922.
    • (2001) J. Biol. Chem , vol.276 , pp. 30914-30922
    • Rogers Jr, G.W.1    Richter, N.J.2    Lima, W.F.3    Merrick, W.C.4
  • 31
    • 0036927393 scopus 로고    scopus 로고
    • The carboxy-terminal domain of the DExDH protein YxiN is sufficient to confer specificity for 23S rRNA
    • Kossen,K., Karginov,F.V. and Uhlenbeck,O.C. (2002) The carboxy-terminal domain of the DExDH protein YxiN is sufficient to confer specificity for 23S rRNA. J. Mol. Biol., 324, 625-636.
    • (2002) J. Mol. Biol , vol.324 , pp. 625-636
    • Kossen, K.1    Karginov, F.V.2    Uhlenbeck, O.C.3
  • 32
    • 44649136660 scopus 로고    scopus 로고
    • Autoinhibition of human dicer by its internal helicase domain
    • Ma,E., MacRae,I.J., Kirsch,J.F. and Doudna,J.A. (2008) Autoinhibition of human dicer by its internal helicase domain. J. Mol. Biol., 380 237-243.
    • (2008) J. Mol. Biol , vol.380 , pp. 237-243
    • Ma, E.1    MacRae, I.J.2    Kirsch, J.F.3    Doudna, J.A.4
  • 33


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.