메뉴 건너뛰기




Volumn 1400, Issue 1-3, 1998, Pages 19-27

Bacterial and archeal type I topoisomerases

Author keywords

Covalent protein DNA complex; DNA supercoiling; Nucleotidyl transfer; Reverse gyrase; Topoisomerase I

Indexed keywords

DNA TOPOISOMERASE;

EID: 0032189214     PISSN: 01674781     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4781(98)00125-0     Document Type: Review
Times cited : (54)

References (42)
  • 1
    • 0024324482 scopus 로고
    • A hyper-recombination mutation in S. cerevisiae identifies a novel eukaryotic topoisomerase
    • Wallis J.W., Chrebet G., Brodsky G., Rolfe M., Rothstein R. A hyper-recombination mutation in S. cerevisiae identifies a novel eukaryotic topoisomerase. Cell. 58:1989;409-419.
    • (1989) Cell , vol.58 , pp. 409-419
    • Wallis, J.W.1    Chrebet, G.2    Brodsky, G.3    Rolfe, M.4    Rothstein, R.5
  • 2
    • 0029986401 scopus 로고    scopus 로고
    • Human TOP3: A single-copy gene encoding DNA topoisomerase III
    • Hanai R., Caron P.R., Wang J.C. Human TOP3: a single-copy gene encoding DNA topoisomerase III. Proc. Natl. Acad. Sci. USA. 93:1996;3653-3657.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3653-3657
    • Hanai, R.1    Caron, P.R.2    Wang, J.C.3
  • 3
    • 0030014783 scopus 로고    scopus 로고
    • DNA topoisomerases
    • Wang J.C. DNA topoisomerases. Annu. Rev. Biochem. 65:1996;635-692.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 635-692
    • Wang, J.C.1
  • 4
    • 0026555506 scopus 로고
    • Control of bacterial DNA supercoiling
    • Drlica K. Control of bacterial DNA supercoiling. Mol. Microbiol. 6:1992;425-433.
    • (1992) Mol. Microbiol. , vol.6 , pp. 425-433
    • Drlica, K.1
  • 5
    • 0028935227 scopus 로고
    • The twisted 'life' of DNA in the cell: Bacterial topoisomerases
    • Luttinger A. The twisted 'life' of DNA in the cell: bacterial topoisomerases. Mol. Microbiol. 15:1995;601-606.
    • (1995) Mol. Microbiol. , vol.15 , pp. 601-606
    • Luttinger, A.1
  • 6
    • 0025807972 scopus 로고
    • Prolonged environmental stress via a two step process selects mutants of Escherichia, Salmonella and Pseudomonas that grows at 54°C
    • Droffner M.L., Yamamoto N. Prolonged environmental stress via a two step process selects mutants of Escherichia, Salmonella and Pseudomonas that grows at 54°C. Arch. Microbiol. 156:1991;307-311.
    • (1991) Arch. Microbiol. , vol.156 , pp. 307-311
    • Droffner, M.L.1    Yamamoto, N.2
  • 7
    • 0026474537 scopus 로고
    • Role of nalidixic acid in isolation of Salmonella typhimurium strains capable of growth at 48°C
    • Droffner M.L., Yamamoto N. Role of nalidixic acid in isolation of Salmonella typhimurium strains capable of growth at 48°C. Curr. Microbiol. 25:1992;257-260.
    • (1992) Curr. Microbiol. , vol.25 , pp. 257-260
    • Droffner, M.L.1    Yamamoto, N.2
  • 8
    • 0029150703 scopus 로고
    • DNA supercoiling in a thermotolerant mutant of Escherichia coli
    • Friedman S.M., Malik M., Drlica K. DNA supercoiling in a thermotolerant mutant of Escherichia coli. Mol. Gen. Genet. 248:1995;417-422.
    • (1995) Mol. Gen. Genet. , vol.248 , pp. 417-422
    • Friedman, S.M.1    Malik, M.2    Drlica, K.3
  • 9
    • 9444291891 scopus 로고    scopus 로고
    • 32-dependent promoter (P1) of the Escherichia coli topoisomerase I gene on thermotolerance
    • 32-dependent promoter (P1) of the Escherichia coli topoisomerase I gene on thermotolerance. Mol. Microbiol. 21:1996;703-711.
    • (1996) Mol. Microbiol. , vol.21 , pp. 703-711
    • Qi, H.1    Menzel, R.2    Tse-Dinh, Y.-C.3
  • 10
    • 0030755365 scopus 로고    scopus 로고
    • DNA supercoiling and bacterial adaptation: Thermotolerance and thermoresistance
    • Tse-Dinh Y.-C., Menzel R., Qi H. DNA supercoiling and bacterial adaptation: thermotolerance and thermoresistance. Trends Microbiol. 5:1997;323-326.
    • (1997) Trends Microbiol. , vol.5 , pp. 323-326
    • Tse-Dinh, Y.-C.1    Menzel, R.2    Qi, H.3
  • 11
    • 0004738888 scopus 로고
    • Regulation of bacterial DNA supercoiling: Plasmid linking numbers vary with growth temperature
    • Goldstein R., Drlica K. Regulation of bacterial DNA supercoiling: plasmid linking numbers vary with growth temperature. Proc. Natl. Acad. Sci. USA. 81:1984;4046-4050.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4046-4050
    • Goldstein, R.1    Drlica, K.2
  • 12
    • 0027158654 scopus 로고
    • Relaxation of supercoiled DNA associated with the induction of heat shock proteins in Escherichia coli
    • Mizushima T., Shunji N., Sekimizu K. Relaxation of supercoiled DNA associated with the induction of heat shock proteins in Escherichia coli. Mol. Gen. Genet. 238:1993;1-5.
    • (1993) Mol. Gen. Genet. , vol.238 , pp. 1-5
    • Mizushima, T.1    Shunji, N.2    Sekimizu, K.3
  • 13
    • 0028015723 scopus 로고
    • Identification of DNA topoisomerases involved in immediate and transient relaxation induced by heat shock in Escherichia coli
    • Ogata Y., Mizushima T., Kataoka K., Miki T., Sekimizu K. Identification of DNA topoisomerases involved in immediate and transient relaxation induced by heat shock in Escherichia coli. Mol. Gen. Genet. 244:1994;451-455.
    • (1994) Mol. Gen. Genet. , vol.244 , pp. 451-455
    • Ogata, Y.1    Mizushima, T.2    Kataoka, K.3    Miki, T.4    Sekimizu, K.5
  • 14
    • 0023433855 scopus 로고
    • Supercoiling of the DNA template during RNA transcription
    • Liu L.F., Wang J.C. Supercoiling of the DNA template during RNA transcription. Proc. Natl. Acad. Sci. USA. 84:1987;7024-7027.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7024-7027
    • Liu, L.F.1    Wang, J.C.2
  • 15
    • 0028006543 scopus 로고
    • Hypernegative supercoiling of the DNA template during transcription elongation in vitro
    • Drolet M., Bi X., Liu L.F. Hypernegative supercoiling of the DNA template during transcription elongation in vitro. J. Biol. Chem. 269:1994;2068-2074.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2068-2074
    • Drolet, M.1    Bi, X.2    Liu, L.F.3
  • 16
    • 0028966185 scopus 로고
    • Overexpression of RNase H partially complements the growth defect of an Escherichia coli topA mutant: R-loop formation is a major problem in the absence of DNA topoisomerase I
    • Drolet M., Phoenix P., Menzel R., Masse E., Liu L.F., Crouch R.J. Overexpression of RNase H partially complements the growth defect of an Escherichia coli topA mutant: R-loop formation is a major problem in the absence of DNA topoisomerase I. Proc. Natl. Acad. Sci. USA. 92:1995;3526-3530.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3526-3530
    • Drolet, M.1    Phoenix, P.2    Menzel, R.3    Masse, E.4    Liu, L.F.5    Crouch, R.J.6
  • 18
    • 0028589156 scopus 로고
    • Topoisomerase III, but not topoisomerase I, can support nascent chain elongation during theta-type DNA replication
    • Hiasa H., Marians K.J. Topoisomerase III, but not topoisomerase I, can support nascent chain elongation during theta-type DNA replication. J. Biol. Chem. 51:1994;32655-32659.
    • (1994) J. Biol. Chem. , vol.51 , pp. 32655-32659
    • Hiasa, H.1    Marians, K.J.2
  • 19
    • 0027976667 scopus 로고
    • Decatenating activity of Escherichia coli DNA gyrase and topoisomerase I and III during oriC and pBR322 DNA replication in vitro
    • Hiasa H., DiGate R.J., Marians K.J. Decatenating activity of Escherichia coli DNA gyrase and topoisomerase I and III during oriC and pBR322 DNA replication in vitro. J. Biol. Chem. 269:1994;2093-2099.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2093-2099
    • Hiasa, H.1    Digate, R.J.2    Marians, K.J.3
  • 20
    • 0026683424 scopus 로고
    • Cloning and sequencing of Escherichia coli mutR shows its identity to topB, encoding topoisomerase III
    • Schofield M.A., Agbunag R., Michaels M.L., Miller J.H. Cloning and sequencing of Escherichia coli mutR shows its identity to topB, encoding topoisomerase III. J. Bacteriol. 174:1992;5168-5170.
    • (1992) J. Bacteriol. , vol.174 , pp. 5168-5170
    • Schofield, M.A.1    Agbunag, R.2    Michaels, M.L.3    Miller, J.H.4
  • 21
    • 0024997668 scopus 로고
    • The role of DNA topoisomerases in recombination and genome stability: A double edged sword?
    • Wang J.C., Caron P.R., Kim R.A. The role of DNA topoisomerases in recombination and genome stability: a double edged sword? Cell. 62:1990;403-406.
    • (1990) Cell , vol.62 , pp. 403-406
    • Wang, J.C.1    Caron, P.R.2    Kim, R.A.3
  • 23
    • 0029886852 scopus 로고    scopus 로고
    • The unique DNA topology and DNA topoisomerases of hyperthermophilic archaea
    • Forterre P., Bergeret A., Lopez-Garcia P. The unique DNA topology and DNA topoisomerases of hyperthermophilic archaea. FEMS Microbiol. Rev. 18:1996;237-248.
    • (1996) FEMS Microbiol. Rev. , vol.18 , pp. 237-248
    • Forterre, P.1    Bergeret, A.2    Lopez-Garcia, P.3
  • 24
    • 0028345358 scopus 로고
    • Comparison of plasmid DNA topology among mesophilic and thermophilic eubacteria and archaebacteria
    • Charbonnier F., Forterre P. Comparison of plasmid DNA topology among mesophilic and thermophilic eubacteria and archaebacteria. J. Bacteriol. 176:1994;1252-1259.
    • (1994) J. Bacteriol. , vol.176 , pp. 1252-1259
    • Charbonnier, F.1    Forterre, P.2
  • 25
    • 0029826565 scopus 로고    scopus 로고
    • Reverse gyrase gene from Sulfolobus shibatae B12: Gene structure, transcription unit and comparative sequence analysis of the two domains
    • Jaxel C., Bouthier de la Tour C., Duguet M., Nadal M. Reverse gyrase gene from Sulfolobus shibatae B12: gene structure, transcription unit and comparative sequence analysis of the two domains. Nucleic Acids Res. 24:1996;4668-4675.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4668-4675
    • Jaxel, C.1    Bouthier De La Tour, C.2    Duguet, M.3    Nadal, M.4
  • 26
    • 0031936513 scopus 로고    scopus 로고
    • Reverse gyrase from the hyperthermophilic bacterium Thermotoga maritima: Properties and gene structure
    • Bouthier de la Tour C., Portemer C., Kaltoum H., Duguet M. Reverse gyrase from the hyperthermophilic bacterium Thermotoga maritima: properties and gene structure. J. Bacteriol. 180:1998;274-281.
    • (1998) J. Bacteriol. , vol.180 , pp. 274-281
    • Bouthier De La Tour, C.1    Portemer, C.2    Kaltoum, H.3    Duguet, M.4
  • 27
    • 0028115776 scopus 로고
    • Three-dimensional structure of the 67K N-terminal fragment of E. coli DNA topoisomerase I
    • Lima C.D., Wang J.C., Mondragon A. Three-dimensional structure of the 67K N-terminal fragment of E. coli DNA topoisomerase I. Nature. 367:1994;138-146.
    • (1994) Nature , vol.367 , pp. 138-146
    • Lima, C.D.1    Wang, J.C.2    Mondragon, A.3
  • 28
    • 0027179285 scopus 로고
    • Crystallization of a 67 kDa fragment of Escherichia coli DNA topoisomerase I
    • Lima C.D., Wang J.C., Mondragon A. Crystallization of a 67 kDa fragment of Escherichia coli DNA topoisomerase I. J. Mol. Biol. 232:1993;1213-1216.
    • (1993) J. Mol. Biol. , vol.232 , pp. 1213-1216
    • Lima, C.D.1    Wang, J.C.2    Mondragon, A.3
  • 29
    • 0028240122 scopus 로고
    • The carboxyl-terminal residues of Escherichia coli DNA topoisomerase III are involved in substrate binding
    • Zhang H.L., DiGate R.J. The carboxyl-terminal residues of Escherichia coli DNA topoisomerase III are involved in substrate binding. J. Biol. Chem. 269:1994;9052-9059.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9052-9059
    • Zhang, H.L.1    Digate, R.J.2
  • 30
    • 0024818386 scopus 로고
    • The carboxyl terminal domain of Escherichia coli DNA topoisomerase I confers higher affinity to DNA
    • Beran-Steed R.K., Tse-Dinh Y.-C. The carboxyl terminal domain of Escherichia coli DNA topoisomerase I confers higher affinity to DNA. Proteins Struct. Funct. Genet. 2:1989;249-258.
    • (1989) Proteins Struct. Funct. Genet. , vol.2 , pp. 249-258
    • Beran-Steed, R.K.1    Tse-Dinh, Y.-C.2
  • 31
    • 0028824645 scopus 로고
    • Escherichia coli DNA topoisomerase III is a site-specific DNA binding protein that binds asymmetrically to its cleavage site
    • Zhang H.L., DiGate R.J. Escherichia coli DNA topoisomerase III is a site-specific DNA binding protein that binds asymmetrically to its cleavage site. J. Biol. Chem. 270:1995;23700-23705.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23700-23705
    • Zhang, H.L.1    Digate, R.J.2
  • 32
    • 0029553684 scopus 로고
    • Expression and DNA-binding properties of the 14 kD carboxyl terminal fragment of Escherichia coli DNA topoisomerase I
    • Zhu C.-X., Samuel M., Pound A., Ahumada A., Tse-Dinh Y.-C. Expression and DNA-binding properties of the 14 kD carboxyl terminal fragment of Escherichia coli DNA topoisomerase I. Biochem. Mol. Biol. Int. 35:1995;375-385.
    • (1995) Biochem. Mol. Biol. Int. , vol.35 , pp. 375-385
    • Zhu, C.-X.1    Samuel, M.2    Pound, A.3    Ahumada, A.4    Tse-Dinh, Y.-C.5
  • 33
    • 0029078107 scopus 로고
    • Solution structure of the C-terminal single-stranded DNA binding domain of E. coli topoisomerase I
    • Yu L., Zhu C.-X., Tse-Dinh Y.-C., Fesik S.W. Solution structure of the C-terminal single-stranded DNA binding domain of E. coli topoisomerase I. Biochemistry. 34:1995;7622-7629.
    • (1995) Biochemistry , vol.34 , pp. 7622-7629
    • Yu, L.1    Zhu, C.-X.2    Tse-Dinh, Y.-C.3    Fesik, S.W.4
  • 34
    • 0029148212 scopus 로고
    • Mutation in Cys662 of Escherichia coli DNA topoisomerase I confers temperature sensitivity and change in DNA cleavage specificity
    • Zhu C.-X., Qi H., Tse-Dinh Y.-C. Mutation in Cys662 of Escherichia coli DNA topoisomerase I confers temperature sensitivity and change in DNA cleavage specificity. J. Mol. Biol. 250:1995;609-616.
    • (1995) J. Mol. Biol. , vol.250 , pp. 609-616
    • Zhu, C.-X.1    Qi, H.2    Tse-Dinh, Y.-C.3
  • 35
    • 0010107939 scopus 로고    scopus 로고
    • The role of the carboxyl-terminal amino acid residues in Escherichia coli DNA topoisomerase III-mediated catalysis
    • Zhang H.L., Malpure S., Li Z., Hiasa H., DiGate R. The role of the carboxyl-terminal amino acid residues in Escherichia coli DNA topoisomerase III-mediated catalysis. J. Biol. Chem. 271:1996;9039-9045.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9039-9045
    • Zhang, H.L.1    Malpure, S.2    Li, Z.3    Hiasa, H.4    Digate, R.5
  • 36
    • 0027992338 scopus 로고
    • Purification and characterization of reverse gyrase from Sulfolobus shibatae
    • Nadal M., Couderc E., Duguet M., Jaxel C. Purification and characterization of reverse gyrase from Sulfolobus shibatae. J. Biol. Chem. 269:1994;5255-5263.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5255-5263
    • Nadal, M.1    Couderc, E.2    Duguet, M.3    Jaxel, C.4
  • 37
    • 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., Gellert M. A two-subunit type I DNA topoisomerase (reverse gyrase) from an extreme hyperthermophile. Proc. Natl. Acad. Sci. USA. 93:1996;106-111.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 106-111
    • Krah, R.1    Kozyavkin, S.A.2    Slesarev, A.I.3    Gellert, M.4
  • 40
    • 0030960325 scopus 로고    scopus 로고
    • Effect of Mg(II) binding on the structure and activity of Escherichia coli DNA topoisomerase I
    • Zhu C.-X., Roche C.J., Tse-Dinh Y.-C. Effect of Mg(II) binding on the structure and activity of Escherichia coli DNA topoisomerase I. J. Biol. Chem. 272:1997;16206-16210.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16206-16210
    • Zhu, C.-X.1    Roche, C.J.2    Tse-Dinh, Y.-C.3
  • 41
    • 0032513296 scopus 로고    scopus 로고
    • Identification of active site residues in Escherichia coli DNA topoisomerase I
    • Chen S.-J., Wang J.C. Identification of active site residues in Escherichia coli DNA topoisomerase I. J. Biol. Chem. 273:1998;6050-6056.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6050-6056
    • Chen, S.-J.1    Wang, J.C.2
  • 42
    • 0032502767 scopus 로고    scopus 로고
    • Site-directed mutagenesis of conserved aspartates, glutamates and arginines in the active site region of Escherichia coli DNA topoisomerase I
    • Zhu C.-X., Roche C.J., Papanicolaou N., DiPietrantonio A., Tse-Dinh Y.-C. Site-directed mutagenesis of conserved aspartates, glutamates and arginines in the active site region of Escherichia coli DNA topoisomerase I. J. Biol. Chem. 273:1998;8783-8789.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8783-8789
    • Zhu, C.-X.1    Roche, C.J.2    Papanicolaou, N.3    Dipietrantonio, A.4    Tse-Dinh, Y.-C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.