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Volumn 274, Issue 14, 2007, Pages 3715-3727

Identification of the gene encoding a type 1 RNase H with an N-terminal double-stranded RNA binding domain from a psychrotrophic bacterium

Author keywords

Double stranded RNA binding domain (RBD); Gel mobility shift assay; Psychrotrophic bacterium; RNase H; Shewanella sp. SIB1

Indexed keywords

DNA HYBRID; DOUBLE STRANDED RNA; OLIGOMER; RECOMBINANT PROTEIN; RIBONUCLEASE H;

EID: 34447318875     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.05903.x     Document Type: Article
Times cited : (9)

References (43)
  • 1
    • 0001711937 scopus 로고
    • Ribonuclease H
    • In: Linn, S.M. Roberts, R.J., eds), pp. Cold Spring Harbor Laboratory, New York, NY.
    • Crouch RJ Dirksen M-L (1982) Ribonuclease H. In : Nuclease (Linn SM Roberts RJ, eds), pp. 211 241. Cold Spring Harbor Laboratory, New York, NY.
    • (1982) Nuclease , pp. 211-241
    • Crouch, R.J.1    Dirksen, M.-L.2
  • 2
    • 0033547793 scopus 로고    scopus 로고
    • Identification of the genes encoding Mn2+-dependent RNase HII and Mg2+-dependent RNase HIII from Bacillus subtilis: Classification of RNases H into three families
    • Ohtani N, Haruki M, Morikawa M, Crouch RJ, Itaya M Kanaya S (1999) Identification of the genes encoding Mn2+-dependent RNase HII and Mg2+-dependent RNase HIII from Bacillus subtilis: classification of RNases H into three families. Biochemistry 38, 605 618.
    • (1999) Biochemistry , vol.38 , pp. 605-618
    • Ohtani, N.1    Haruki, M.2    Morikawa, M.3    Crouch, R.J.4    Itaya, M.5    Kanaya, S.6
  • 4
    • 7444232276 scopus 로고    scopus 로고
    • Cleavage of double-stranded RNA by RNase HI from a thermoacidophilic archaeon, Sulfolobus tokodaii
    • Ohtani N, Yanagawa H, Tomita M Itaya M (2004) Cleavage of double-stranded RNA by RNase HI from a thermoacidophilic archaeon, Sulfolobus tokodaii Nucleic Acids Res 32, 5809 5819.
    • (2004) Nucleic Acids Res , vol.32 , pp. 5809-5819
    • Ohtani, N.1    Yanagawa, H.2    Tomita, M.3    Itaya, M.4
  • 5
    • 0002929551 scopus 로고    scopus 로고
    • Physiological functions of E. coli RNase HI
    • In: Crouch, R.J. Toulme, J.J., eds), pp. INSERM, Paris.
    • Kogoma T Foster PL (1998) Physiological functions of E. coli RNase HI. In : Ribonucleases H (Crouch RJ Toulme JJ, eds), pp. 39 66. INSERM, Paris.
    • (1998) Ribonucleases H , pp. 39-66
    • Kogoma, T.1    Foster, P.L.2
  • 6
    • 0033512305 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae RNase H(35) functions in RNA primer removal during lagging-strand DNA synthesis, most efficiently in cooperation with Rad27 nuclease
    • Qiu J, Qian Y, Frank P, Wintersberger U Shen B (1999) Saccharomyces cerevisiae RNase H(35) functions in RNA primer removal during lagging-strand DNA synthesis, most efficiently in cooperation with Rad27 nuclease. Mol Cell Biol 19, 8361 8371.
    • (1999) Mol Cell Biol , vol.19 , pp. 8361-8371
    • Qiu, J.1    Qian, Y.2    Frank, P.3    Wintersberger, U.4    Shen, B.5
  • 7
    • 0033756041 scopus 로고    scopus 로고
    • The absence of ribonuclease H1 or H2 alters the sensitivity of Saccharomyces cerevisiae to hydroxyurea, caffeine and ethyl methanesulphonate: Implications for roles of RNases H in DNA replication and repair
    • Arudchandran A, Cerritelli S, Narimatsu S, Itaya M, Shin DY, Shimada Y Crouch RJ (2000) The absence of ribonuclease H1 or H2 alters the sensitivity of Saccharomyces cerevisiae to hydroxyurea, caffeine and ethyl methanesulphonate: implications for roles of RNases H in DNA replication and repair. Genes Cells 5, 789 802.
    • (2000) Genes Cells , vol.5 , pp. 789-802
    • Arudchandran, A.1    Cerritelli, S.2    Narimatsu, S.3    Itaya, M.4    Shin, D.Y.5    Shimada, Y.6    Crouch, R.J.7
  • 8
    • 0037032428 scopus 로고    scopus 로고
    • Cleavage of a DNA-RNA-DNA/DNA chimeric substrate containing single ribonucleotide at the DNA-RNA junction with prokaryotic RNases HII
    • Haruki M, Tsunaka Y, Morikawa M Kanaya S (2002) Cleavage of a DNA-RNA-DNA/DNA chimeric substrate containing single ribonucleotide at the DNA-RNA junction with prokaryotic RNases HII. FEBS Lett 531, 204 208.
    • (2002) FEBS Lett , vol.531 , pp. 204-208
    • Haruki, M.1    Tsunaka, Y.2    Morikawa, M.3    Kanaya, S.4
  • 9
    • 0037168516 scopus 로고    scopus 로고
    • Excision of misincorporated ribonucleotides in DNA by RNase H (type 2) and FEN-1 in cell-free extracts
    • Rydberg B Game J (2002) Excision of misincorporated ribonucleotides in DNA by RNase H (type 2) and FEN-1 in cell-free extracts. Proc Natl Acad Sci USA 99, 16654 16659.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16654-16659
    • Rydberg, B.1    Game, J.2
  • 10
    • 0345354684 scopus 로고    scopus 로고
    • Failure to produce mitochondrial DNA results in embryonic lethality in Rnaseh1 null mice
    • Cerritelli SM, Frolova EG, Feng C, Grinberg A, Love PE Crouch RJ (2003) Failure to produce mitochondrial DNA results in embryonic lethality in Rnaseh1 null mice. Mol Cell 11, 807 815.
    • (2003) Mol Cell , vol.11 , pp. 807-815
    • Cerritelli, S.M.1    Frolova, E.G.2    Feng, C.3    Grinberg, A.4    Love, P.E.5    Crouch, R.J.6
  • 12
    • 0002615512 scopus 로고    scopus 로고
    • RNase H of retroviral reverse transcriptases
    • In: Crouch, R.J. Toulme, J.J., eds), pp. INSERM, Paris.
    • Hughes SH, Arnold E Hostomsky Z (1998) RNase H of retroviral reverse transcriptases. In : Ribonucleases H (Crouch RJ Toulme JJ, eds), pp. 195 224. INSERM, Paris.
    • (1998) Ribonucleases H , pp. 195-224
    • Hughes, S.H.1    Arnold, E.2    Hostomsky, Z.3
  • 13
    • 0032052258 scopus 로고    scopus 로고
    • A common 40 amino acid motif in eukaryotic RNases H1 and caulimovirus ORF VI proteins binds to duplex RNAs
    • Cerritelli SM, Fedoroff OY, Reid BR Crouch RJ (1998) A common 40 amino acid motif in eukaryotic RNases H1 and caulimovirus ORF VI proteins binds to duplex RNAs. Nucleic Acid Res 26, 1834 1840.
    • (1998) Nucleic Acid Res , vol.26 , pp. 1834-1840
    • Cerritelli, S.M.1    Fedoroff, O.Y.2    Reid, B.R.3    Crouch, R.J.4
  • 14
    • 0033588313 scopus 로고    scopus 로고
    • NMR structure of the N-terminal domain of Saccharomyces cerevisiae RNase HI reveals a fold with a strong resemblance to the N-terminal domain of ribosomal protein L9
    • Evans SP Bycroft M (1999) NMR structure of the N-terminal domain of Saccharomyces cerevisiae RNase HI reveals a fold with a strong resemblance to the N-terminal domain of ribosomal protein L9. J Mol Biol 291, 661 669.
    • (1999) J Mol Biol , vol.291 , pp. 661-669
    • Evans, S.P.1    Bycroft, M.2
  • 16
    • 0029295965 scopus 로고
    • The non-RNase H domain of Saccharomyces cerevisiae RNase H1 binds double-stranded RNA: Magnesium modulates the switch between double-stranded RNA binding and RNase H activity
    • Cerritelli SM Crouch RJ (1995) The non-RNase H domain of Saccharomyces cerevisiae RNase H1 binds double-stranded RNA: magnesium modulates the switch between double-stranded RNA binding and RNase H activity. RNA 1, 246 259.
    • (1995) RNA , vol.1 , pp. 246-259
    • Cerritelli, S.M.1    Crouch, R.J.2
  • 17
    • 21244451435 scopus 로고    scopus 로고
    • Crystal structures of RNase H bound to an RNA/DNA hybrid: Substrate specificity and metal-dependent catalysis
    • Nowotny M, Gaidamakov SA, Crouch RJ Yang W (2005) Crystal structures of RNase H bound to an RNA/DNA hybrid: substrate specificity and metal-dependent catalysis. Cell 121, 1005 1016.
    • (2005) Cell , vol.121 , pp. 1005-1016
    • Nowotny, M.1    Gaidamakov, S.A.2    Crouch, R.J.3    Yang, W.4
  • 18
    • 0034742629 scopus 로고    scopus 로고
    • Isolation and characterization of psychrotrophic bacteria from oil-reservoir water and oil sands
    • Kato T, Haruki M, Imanaka T, Morikawa M Kanaya S (2001) Isolation and characterization of psychrotrophic bacteria from oil-reservoir water and oil sands. Appl Microbiol Biotechnol 55, 794 800.
    • (2001) Appl Microbiol Biotechnol , vol.55 , pp. 794-800
    • Kato, T.1    Haruki, M.2    Imanaka, T.3    Morikawa, M.4    Kanaya, S.5
  • 19
    • 0035712765 scopus 로고    scopus 로고
    • Heat labile ribonuclease HI from a psychrotrophic bacterium: Gene cloning, characterization and site-directed mutagenesis
    • Ohtani N, Haruki M, Morikawa M Kanaya S (2001) Heat labile ribonuclease HI from a psychrotrophic bacterium: gene cloning, characterization and site-directed mutagenesis. Protein Eng 14, 975 982.
    • (2001) Protein Eng , vol.14 , pp. 975-982
    • Ohtani, N.1    Haruki, M.2    Morikawa, M.3    Kanaya, S.4
  • 20
    • 33646229804 scopus 로고    scopus 로고
    • Identification of RNase HII form psychrotrophic bacterium, Shewanella sp. SIB1 as a high-activity type RNase H
    • Chon H, Tadokoro T, Ohtani N, Koga Y, Takano K Kanaya S (2006) Identification of RNase HII form psychrotrophic bacterium, Shewanella sp. SIB1 as a high-activity type RNase H. FEBS J 273, 2264 2275.
    • (2006) FEBS J , vol.273 , pp. 2264-2275
    • Chon, H.1    Tadokoro, T.2    Ohtani, N.3    Koga, Y.4    Takano, K.5    Kanaya, S.6
  • 21
    • 0347379925 scopus 로고    scopus 로고
    • Human RNase H1 uses one tryptophan and two lysines to position the enzyme at the 3′-DNA/5′-RNA terminus of the heteroduplex substrate
    • Lima WF, Wu H, Nichols JG, Prakash TP, Ravikumer V Crooke ST (2003) Human RNase H1 uses one tryptophan and two lysines to position the enzyme at the 3′-DNA/5′-RNA terminus of the heteroduplex substrate. J Biol Chem 278, 49860 49867.
    • (2003) J Biol Chem , vol.278 , pp. 49860-49867
    • Lima, W.F.1    Wu, H.2    Nichols, J.G.3    Prakash, T.P.4    Ravikumer, V.5    Crooke, S.T.6
  • 24
    • 20444452106 scopus 로고    scopus 로고
    • The SCO2299 gene from Streptomyces coelicolor A3(2) encodes a bifunctional enzyme consisting of an RNase H domain and an acid phosphatase domain
    • Ohtani N, Saito N, Tomita M, Itaya M Itoh A (2005) The SCO2299 gene from Streptomyces coelicolor A3(2) encodes a bifunctional enzyme consisting of an RNase H domain and an acid phosphatase domain. FEBS J 272, 2828 2837.
    • (2005) FEBS J , vol.272 , pp. 2828-2837
    • Ohtani, N.1    Saito, N.2    Tomita, M.3    Itaya, M.4    Itoh, A.5
  • 25
    • 0017596525 scopus 로고
    • A numerical taxonomic study of some Pseudomonas-like marine bacteria
    • Lee JV, Gibson DM Ward FB (1977) A numerical taxonomic study of some Pseudomonas-like marine bacteria. J Gen Microbiol 98, 439 451.
    • (1977) J Gen Microbiol , vol.98 , pp. 439-451
    • Lee, J.V.1    Gibson, D.M.2    Ward, F.B.3
  • 26
    • 0032964545 scopus 로고    scopus 로고
    • Phylogeny of marine and freshwater Shewanella: Reclassification of Shewanella putrefaciens NCIMB 400 as Shewanella frigidimarina
    • Reid GA Gordon EH (1999) Phylogeny of marine and freshwater Shewanella: reclassification of Shewanella putrefaciens NCIMB 400 as Shewanella frigidimarina. Int J Syst Bacteriol 49, 189 191.
    • (1999) Int J Syst Bacteriol , vol.49 , pp. 189-191
    • Reid, G.A.1    Gordon, E.H.2
  • 27
    • 0036867531 scopus 로고    scopus 로고
    • Shewanella denitrificans sp. nov., a vigorously denitrifying bacterium isolated from the oxic-anoxic interface of the Gotland Deep in the central Baltic Sea
    • Brettar I, Christen R Hofle MG (2002) Shewanella denitrificans sp. nov., a vigorously denitrifying bacterium isolated from the oxic-anoxic interface of the Gotland Deep in the central Baltic Sea. Int J Syst Evol Microbiol 52, 2211 2217.
    • (2002) Int J Syst Evol Microbiol , vol.52 , pp. 2211-2217
    • Brettar, I.1    Christen, R.2    Hofle, M.G.3
  • 28
    • 0031671525 scopus 로고    scopus 로고
    • Photobacterium profundum sp. nov., a new, moderately barophilic bacterial species isolated from a deep-sea sediment
    • Nogi Y, Masui N Kato C (1998) Photobacterium profundum sp. nov., a new, moderately barophilic bacterial species isolated from a deep-sea sediment. Extremophiles 2, 1 7.
    • (1998) Extremophiles , vol.2 , pp. 1-7
    • Nogi, Y.1    Masui, N.2    Kato, C.3
  • 30
    • 0034548849 scopus 로고    scopus 로고
    • Remarkably low temperature optima for extracellular enzyme activity from Arctic bacteria and sea ice
    • Huston AL, Krieger-Brockett BB Deming JW (2000) Remarkably low temperature optima for extracellular enzyme activity from Arctic bacteria and sea ice. Appl Environ Microbiol 2, 383 388.
    • (2000) Appl Environ Microbiol , vol.2 , pp. 383-388
    • Huston, A.L.1    Krieger-Brockett, B.B.2    Deming, J.W.3
  • 33
    • 0025740545 scopus 로고
    • A combination of RNase H (rnh) and recBCD or sbcB mutations in E. coli K12 adversely affects growth
    • Itaya M Crouch RJ (1991) A combination of RNase H (rnh) and recBCD or sbcB mutations in E. coli K12 adversely affects growth. Mol Gen Genet 227, 424 432.
    • (1991) Mol Gen Genet , vol.227 , pp. 424-432
    • Itaya, M.1    Crouch, R.J.2
  • 34
    • 0032912813 scopus 로고    scopus 로고
    • Isolation of RNase H genes that are essential for growth of Bacillus subtilis 168
    • Itaya M, Omori A, Kanaya S, Crouch RJ, Tanaka T Kondo K (1999) Isolation of RNase H genes that are essential for growth of Bacillus subtilis 168. J Bacteriol 181, 2118 2123.
    • (1999) J Bacteriol , vol.181 , pp. 2118-2123
    • Itaya, M.1    Omori, A.2    Kanaya, S.3    Crouch, R.J.4    Tanaka, T.5    Kondo, K.6
  • 35
    • 0034038243 scopus 로고    scopus 로고
    • Characterization of ribonuclease HII from E. coli overproduced in a soluble form
    • Ohtani N, Haruki M, Muroya A, Morikawa M Kanaya S (2000) Characterization of ribonuclease HII from E. coli overproduced in a soluble form. J Biochem (Tokyo) 127, 895 899.
    • (2000) J Biochem (Tokyo) , vol.127 , pp. 895-899
    • Ohtani, N.1    Haruki, M.2    Muroya, A.3    Morikawa, M.4    Kanaya, S.5
  • 36
    • 0027939197 scopus 로고
    • A novel strategy for stabilization of E. coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions
    • Haruki M, Noguchi E, Akasako A, Oobatake M, Itaya M Kanaya S (1994) A novel strategy for stabilization of E. coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. J Biol Chem 269, 26904 26911.
    • (1994) J Biol Chem , vol.269 , pp. 26904-26911
    • Haruki, M.1    Noguchi, E.2    Akasako, A.3    Oobatake, M.4    Itaya, M.5    Kanaya, S.6
  • 37
    • 0019838194 scopus 로고
    • Cloning of the genes for penicillinase, penP and penI, of Bacillus licheniformis in some vector plasmids and their expression in E. coli, Bacillus subtilis, and Bacillus licheniformis
    • Imanaka T, Tanaka T, Tsunekawa H Aiba S (1981) Cloning of the genes for penicillinase, penP and penI, of Bacillus licheniformis in some vector plasmids and their expression in E. coli, Bacillus subtilis, and Bacillus licheniformis. J Bacteriol 147, 776 786.
    • (1981) J Bacteriol , vol.147 , pp. 776-786
    • Imanaka, T.1    Tanaka, T.2    Tsunekawa, H.3    Aiba, S.4
  • 38
    • 0027477879 scopus 로고
    • PH-dependent thermostabilization of E. coli ribonuclease HI by histidine to alanine substitutions
    • Kanaya S, Oobatake M, Nakamura H Ikehara M (1993) pH-dependent thermostabilization of E. coli ribonuclease HI by histidine to alanine substitutions. J Biotechnol 28, 117 136.
    • (1993) J Biotechnol , vol.28 , pp. 117-136
    • Kanaya, S.1    Oobatake, M.2    Nakamura, H.3    Ikehara, M.4
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680 685.
    • (1970) Nature , vol.227 , pp. 680-685
  • 40
    • 84871693371 scopus 로고
    • The spectrophotometric determination of tyrosine and tryptophan in proteins
    • Goodwin TW Morton RA (1946) The spectrophotometric determination of tyrosine and tryptophan in proteins. Biochem J 40, 628 632.
    • (1946) Biochem J , vol.40 , pp. 628-632
    • Goodwin, T.W.1    Morton, R.A.2
  • 42
    • 0033213981 scopus 로고    scopus 로고
    • Properties of cloned and expressed human RNase H1
    • Wu H, Lima WF Crooke ST (1999) Properties of cloned and expressed human RNase H1. J Biol Chem 274, 28270 28278.
    • (1999) J Biol Chem , vol.274 , pp. 28270-28278
    • Wu, H.1    Lima, W.F.2    Crooke, S.T.3
  • 43
    • 0016045397 scopus 로고
    • DNA sequence analysis: A general, simple and rapid method for sequencing large oligodeoxyribonucleotide fragments by mapping
    • Jay E, Bambara R, Padmanabham P Wu R (1974) DNA sequence analysis: a general, simple and rapid method for sequencing large oligodeoxyribonucleotide fragments by mapping. Nucleic Acids Res 1, 331 353.
    • (1974) Nucleic Acids Res , vol.1 , pp. 331-353
    • Jay, E.1    Bambara, R.2    Padmanabham, P.3    Wu, R.4


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