메뉴 건너뛰기




Volumn 381, Issue 3, 2004, Pages 795-802

Identification of the first archaeal Type 1 RNase H gene from Halobacterium sp. NRC-1: Archaeal RNase HI can cleave an RNA-DNA junction

Author keywords

Archaea; Catalytic mechanism; Halobacterium; Okazaki fragment; RNA DNA junction; RNase H

Indexed keywords

AMINO ACIDS; GENES; PROTEINS; RNA;

EID: 4344595870     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040153     Document Type: Article
Times cited : (33)

References (42)
  • 1
    • 0001711937 scopus 로고
    • Linn, S. M. and Crouch, R. J., eds., Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • Crouch, R. J. and Dirksen, M.-L. (1982) Ribonucleases H in Nuclease (Linn, S. M. and Crouch, R. J., eds.), pp. 211-241, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • (1982) Ribonucleases H in Nuclease , pp. 211-241
    • Crouch, R.J.1    Dirksen, M.-L.2
  • 2
    • 0002929551 scopus 로고    scopus 로고
    • Physiological function of E. coli RNase HI
    • Crouch, R. J. and Toulme, J. J., eds., INSERM, Paris
    • Kogoma, T. and Foster, P. L. (1998) Physiological function of E. coli RNase HI. In Ribonucleases H (Crouch, R. J. and Toulme, J. J., eds.), pp. 39-66, INSERM, Paris
    • (1998) Ribonucleases H , pp. 39-66
    • Kogoma, T.1    Foster, P.L.2
  • 3
    • 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. and 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
  • 4
    • 0030929525 scopus 로고    scopus 로고
    • Creation and removal of embedded ribonucleotides in chromosomal DNA during mammalian Okazaki fragment processing
    • Rumbaugh, J. A., Murante, R. S., Shi, S. and Bambara, R. A. (1997) Creation and removal of embedded ribonucleotides in chromosomal DNA during mammalian Okazaki fragment processing. J. Biol. Chem. 272, 22591-22599
    • (1997) J. Biol. Chem. , vol.272 , pp. 22591-22599
    • Rumbaugh, J.A.1    Murante, R.S.2    Shi, S.3    Bambara, R.A.4
  • 5
    • 0028966185 scopus 로고
    • Overexpression of RNase H partially complements the growth defect of an Escherichia coli Δ 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. and Crouch, R. J. (1995) Overexpression of RNase H partially complements the growth defect of an Escherichia coli Δ topA mutant: R-loop formation is a major problem in the absence of DNA topoisomerase I. Proc. Natl. Acad. Sci. U.S.A. 92, 3526-3530
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , 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
  • 6
    • 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, D. Y., Shimada, Y. and Crouch, R. J. (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
  • 9
    • 0020660180 scopus 로고
    • DNA sequence of the gene coding for Escherichia coli ribonuclease H
    • Kanaya, S. and Crouch, R. J. (1983) DNA sequence of the gene coding for Escherichia coli ribonuclease H. J. Biol. Chem. 258, 1276-1281
    • (1983) J. Biol. Chem. , vol.258 , pp. 1276-1281
    • Kanaya, S.1    Crouch, R.J.2
  • 10
    • 0025147609 scopus 로고
    • Isolation and characterization of a second RNase H (RNase HII) of Escherichia coli K-12 encoded by the rnhB gene
    • Itaya, M. (1990) Isolation and characterization of a second RNase H (RNase HII) of Escherichia coli K-12 encoded by the rnhB gene. Proc. Natl. Acad. Sci. U.S.A. 87, 8587-8591
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 8587-8591
    • Itaya, M.1
  • 11
    • 0034038243 scopus 로고    scopus 로고
    • Characterization of ribonuclease HII from Escherichia coli overproduced in a soluble form
    • Tokyo
    • Ohtani, N., Haruki, M., Muroya, A., Morikawa, M. and Kanaya, S. (2000) Characterization of ribonuclease HII from Escherichia coli overproduced in a soluble form. J. Biochem. (Tokyo) 127, 895-899
    • (2000) J. Biochem. , vol.127 , pp. 895-899
    • Ohtani, N.1    Haruki, M.2    Muroya, A.3    Morikawa, M.4    Kanaya, S.5
  • 12
    • 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, R. J., Tanaka, T. and 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
  • 13
    • 0037432714 scopus 로고    scopus 로고
    • Far different levels of gene expression provided by an oriented cloning system in Bacillus subtilis and Escherichia coli
    • Ohashi, Y., Ohshima, H., Tsuge, K. and Itaya, M. (2003) Far different levels of gene expression provided by an oriented cloning system in Bacillus subtilis and Escherichia coli. FEMS Microbiol. Lett. 221, 125-130
    • (2003) FEMS Microbiol. Lett. , vol.221 , pp. 125-130
    • Ohashi, Y.1    Ohshima, H.2    Tsuge, K.3    Itaya, M.4
  • 14
    • 0024971027 scopus 로고
    • Overproduction and preliminary crystallographic study of ribonuclease H from Escherichia coli
    • Kanaya, S., Kohara, A., Miyagawa, M., Matsuzaki, T., Morikawa, K. and Ikehara, M. (1989) Overproduction and preliminary crystallographic study of ribonuclease H from Escherichia coli. J. Biol. Chem. 264, 11546-11549
    • (1989) J. Biol. Chem. , vol.264 , pp. 11546-11549
    • Kanaya, S.1    Kohara, A.2    Miyagawa, M.3    Matsuzaki, T.4    Morikawa, K.5    Ikehara, M.6
  • 15
    • 0027939197 scopus 로고
    • A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions
    • Haruki, M., Noguchi, E., Akasako, A., Oobatake, M., Itaya, M. and Kanaya, S. (1994) A novel strategy for stabilization of Escherichia 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
  • 16
    • 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. and 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
  • 17
    • 0027477879 scopus 로고
    • H-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions
    • Kanaya, S., Oobatake, M., Nakamura, H. and Ikehara, M. (1993) pH-dependent thermostabilization of Escherichia 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
  • 18
    • 0025155311 scopus 로고
    • Role of cysteine residues in ribonuclease H from Escherichia coli. Site-directed mutagenesis and chemical modification
    • Kanaya, S., Kimura, S., Katsuda, C. and Ikehara, M. (1990) Role of cysteine residues in ribonuclease H from Escherichia coli. Site-directed mutagenesis and chemical modification. Biochem. J. 271, 59-66
    • (1990) Biochem. J. , vol.271 , pp. 59-66
    • Kanaya, S.1    Kimura, S.2    Katsuda, C.3    Ikehara, M.4
  • 19
    • 84871693371 scopus 로고
    • The spectrophotometric determination of tyrosine and tryptophan in proteins
    • Goodwin, T. W. and Morton, R. A. (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
  • 22
    • 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, S. M., Fedoroff, O. Y., Reid, B. R. and Crouch, R. J. (1998) A common 40 amino acid motif in eukaryotic RNases H1 and caulimovirus ORF VI proteins binds to duplex RNAs. Nucleic Acids Res. 26, 1834-1840
    • (1998) Nucleic Acids Res. , vol.26 , pp. 1834-1840
    • Cerritelli, S.M.1    Fedoroff, O.Y.2    Reid, B.R.3    Crouch, R.J.4
  • 23
    • 0026095261 scopus 로고
    • Importance of the positive charge cluster in Escherichia coli ribonuclease HI for the effective binding of the substrate
    • Kanaya, S., Katsuda-Nakai, C. and Ikehara, M. (1991) Importance of the positive charge cluster in Escherichia coli ribonuclease HI for the effective binding of the substrate. J. Biol. Chem. 266, 11621-11627
    • (1991) J. Biol. Chem. , vol.266 , pp. 11621-11627
    • Kanaya, S.1    Katsuda-Nakai, C.2    Ikehara, M.3
  • 24
    • 0025908083 scopus 로고
    • Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase
    • Davies, 2nd, J. F., Hostomska, Z., Hostomsky, Z., Jordan, S. R. and Matthews, D. A. (1991) Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase. Science 252, 88-95
    • (1991) Science , vol.252 , pp. 88-95
    • Davies II, J.F.1    Hostomska, Z.2    Hostomsky, Z.3    Jordan, S.R.4    Matthews, D.A.5
  • 25
    • 0025024911 scopus 로고
    • Purification and characterization of the RNase H domain of HIV-1 reverse transcriptase expressed in recombinant Escherichia coli
    • Becerra, S. P., Clore, G. M., Gronenborn, A. M., Karlstrom, A. R., Stahl, S. J., Wilson, S. H. and Wingfield, P. T. (1990) Purification and characterization of the RNase H domain of HIV-1 reverse transcriptase expressed in recombinant Escherichia coli. FEBS Lett. 270, 76-80
    • (1990) FEBS Lett. , vol.270 , pp. 76-80
    • Becerra, S.P.1    Clore, G.M.2    Gronenborn, A.M.3    Karlstrom, A.R.4    Stahl, S.J.5    Wilson, S.H.6    Wingfield, P.T.7
  • 26
    • 0025975174 scopus 로고
    • Reconstitution in vitro of RNase H activity by using purified N-terminal and C-terminal domains of human immunodeficiency virus type 1 reverse transcriptase
    • Hostomsky, Z., Hostomska, Z., Hudson, G. O., Moomaw, E. W. and Nodes, B. R. (1991) Reconstitution in vitro of RNase H activity by using purified N-terminal and C-terminal domains of human immunodeficiency virus type 1 reverse transcriptase. Proc. Natl. Acad. Sci. U.S.A. 88, 1148-1152
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 1148-1152
    • Hostomsky, Z.1    Hostomska, Z.2    Hudson, G.O.3    Moomaw, E.W.4    Nodes, B.R.5
  • 27
    • 0002457195 scopus 로고    scopus 로고
    • Enzymatic activity and protein stability of E. coli ribonuclease HI
    • Crouch, R. J. and Toulme, J. J., eds., INSERM, Paris
    • Kanaya, S. (1998) Enzymatic activity and protein stability of E. coli ribonuclease HI. In Ribonucleases H (Crouch, R. J. and Toulme, J. J., eds.), pp. 1-38, INSERM, Paris
    • (1998) Ribonucleases H , pp. 1-38
    • Kanaya, S.1
  • 28
    • 0029113187 scopus 로고
    • Kinetic analysis of Escherichia coli ribonuclease HI using oligomeric DNA/RNA substrates suggests an alternative mechanism for the interaction between the enzyme and the substrate
    • Kanaya, E. and Kanaya, S. (1995) Kinetic analysis of Escherichia coli ribonuclease HI using oligomeric DNA/RNA substrates suggests an alternative mechanism for the interaction between the enzyme and the substrate. Eur. J. Biochem. 231, 557-562
    • (1995) Eur. J. Biochem. , vol.231 , pp. 557-562
    • Kanaya, E.1    Kanaya, S.2
  • 29
    • 0029967916 scopus 로고    scopus 로고
    • Proposal for new catalytic roles for two invariant residues in Escherichia coli ribonuclease HI
    • Kashiwagi, T., Jeanteur, D., Haruki, M., Katayanagi, K., Kanaya, S. and Morikawa, K. (1996) Proposal for new catalytic roles for two invariant residues in Escherichia coli ribonuclease HI. Protein Eng. 9, 857-867
    • (1996) Protein Eng. , vol.9 , pp. 857-867
    • Kashiwagi, T.1    Jeanteur, D.2    Haruki, M.3    Katayanagi, K.4    Kanaya, S.5    Morikawa, K.6
  • 30
    • 0027213005 scopus 로고
    • Substrate specificity of human RNase H1 and its role in excision repair of ribose residues misincorporated in DNA
    • Eder, P. S., Walder, R. Y. and Walder, J. A. (1993) Substrate specificity of human RNase H1 and its role in excision repair of ribose residues misincorporated in DNA. Biochimie 75, 123-126
    • (1993) Biochimie , vol.75 , pp. 123-126
    • Eder, P.S.1    Walder, R.Y.2    Walder, J.A.3
  • 31
    • 0034805756 scopus 로고    scopus 로고
    • Archaeoglobus fulgidus RNase HII in DNA replication: Enzymological functions and activity regulation via metal cofactors
    • Chai, Q., Qiu, J., Chapados, B. R. and Shen, B. (2001) Archaeoglobus fulgidus RNase HII in DNA replication: enzymological functions and activity regulation via metal cofactors. Biochem. Biophys. Res. Commun. 286, 1073-1081
    • (2001) Biochem. Biophys. Res. Commun. , vol.286 , pp. 1073-1081
    • Chai, Q.1    Qiu, J.2    Chapados, B.R.3    Shen, B.4
  • 32
    • 0021357260 scopus 로고
    • Function of RNase H in DNA replication revealed by RNase H defective mutants of Escherichia coli
    • Ogawa, T. and Okazaki, T. (1984) Function of RNase H in DNA replication revealed by RNase H defective mutants of Escherichia coli. Mol. Gen. Genet. 193, 231-237
    • (1984) Mol. Gen. Genet. , vol.193 , pp. 231-237
    • Ogawa, T.1    Okazaki, T.2
  • 33
    • 0041734767 scopus 로고    scopus 로고
    • Cooperative regulation for Okazaki fragment processing by RNase HII and Fen-1 purified from a hyperthermophilic archaeon, P. furiosus
    • Sato, A., Kanai, A., Itaya, M. and Tomita, M. (2003) Cooperative regulation for Okazaki fragment processing by RNase HII and Fen-1 purified from a hyperthermophilic archaeon, P. furiosus. Biochem. Biophys. Res. Commun. 309, 247-252
    • (2003) Biochem. Biophys. Res. Commun. , vol.309 , pp. 247-252
    • Sato, A.1    Kanai, A.2    Itaya, M.3    Tomita, M.4
  • 34
    • 0037135570 scopus 로고    scopus 로고
    • Mutating conserved residues in the ribonuclease H domain of Ty3 reverse transcriptase affects specialized cleavage events
    • Lener, D., Budihas, S. R. and Le-Grice, S. F. (2002) Mutating conserved residues in the ribonuclease H domain of Ty3 reverse transcriptase affects specialized cleavage events. J. Biol. Chem. 277, 26486-26495
    • (2002) J. Biol. Chem. , vol.277 , pp. 26486-26495
    • Lener, D.1    Budihas, S.R.2    Le-Grice, S.F.3
  • 35
    • 0029831105 scopus 로고    scopus 로고
    • An unusual mechanism of self-primed reverse transcription requires the RNase H domain of reverse transcriptase to cleave an RNA duplex
    • Levin, H. L. (1996) An unusual mechanism of self-primed reverse transcription requires the RNase H domain of reverse transcriptase to cleave an RNA duplex. Mol. Cell. Biol. 16, 5645-5654
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5645-5654
    • Levin, H.L.1
  • 36
    • 3242878430 scopus 로고    scopus 로고
    • A Corynebacterium glutamicum rnhA recG double mutant showing lysozyme-sensitivity, temperature-sensitive growth, and UV-Sensitivity
    • Hirasawa, T., Kumagai, Y., Nagai, K. and Wachi, M. (2003) A Corynebacterium glutamicum rnhA recG double mutant showing lysozyme-sensitivity, temperature-sensitive growth, and UV-Sensitivity. Biosci. Biotechnol. Biochem. 67, 2416-2424
    • (2003) Biosci. Biotechnol. Biochem. , vol.67 , pp. 2416-2424
    • Hirasawa, T.1    Kumagai, Y.2    Nagai, K.3    Wachi, M.4
  • 39
    • 0032545251 scopus 로고    scopus 로고
    • Activation/attenuation model for RNase H. A one-metal mechanism with second-metal inhibition
    • Keck, J. L., Goedken, E. R. and Marqusee, S. (1998) Activation/ attenuation model for RNase H. A one-metal mechanism with second-metal inhibition. J. Biol. Chem. 273, 34128-34133
    • (1998) J. Biol. Chem. , vol.273 , pp. 34128-34133
    • Keck, J.L.1    Goedken, E.R.2    Marqusee, S.3
  • 40
    • 0029834664 scopus 로고    scopus 로고
    • The putative substrate recognition loop of Escherichia coli ribonuclease H is not essential for activity
    • Keck, J. L. and Marqusee, S. (1996) The putative substrate recognition loop of Escherichia coli ribonuclease H is not essential for activity. J. Biol. Chem. 271, 19883-19887
    • (1996) J. Biol. Chem. , vol.271 , pp. 19883-19887
    • Keck, J.L.1    Marqusee, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.