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Volumn 53, Issue 3, 1998, Pages 300-307

Cloning, expression, and mapping of ribonucleases H of human and mouse related to bacterial RNase HI

Author keywords

[No Author keywords available]

Indexed keywords

RIBONUCLEASE H;

EID: 0032213759     PISSN: 08887543     EISSN: None     Source Type: Journal    
DOI: 10.1006/geno.1998.5497     Document Type: Article
Times cited : (52)

References (36)
  • 3
    • 0016667143 scopus 로고
    • Distinct ribonuclease H activities in calf thymus
    • Büsen W., Hausen P. Distinct ribonuclease H activities in calf thymus. Eur. J. Biochem. 52:1975;179-190.
    • (1975) Eur. J. Biochem. , vol.52 , pp. 179-190
    • Büsen, W.1    Hausen, P.2
  • 4
    • 0027366669 scopus 로고
    • Functional complementation of anEscherichia coliCrithidia fasciculata
    • Campbell A. G., Ray D. S. Functional complementation of anEscherichia coliCrithidia fasciculata. Proc. Natl. Acad. Sci. USA. 90:1993;9350-9354.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9350-9354
    • Campbell, A.G.1    Ray, D.S.2
  • 5
    • 0019204859 scopus 로고
    • Isolation and mapping of a mutation inEscherichia coli
    • Carl P. L., Bloom L., Crouch R. J. Isolation and mapping of a mutation inEscherichia coli. J. Bacteriol. 144:1980;28-35.
    • (1980) J. Bacteriol. , vol.144 , pp. 28-35
    • Carl, P.L.1    Bloom, L.2    Crouch, R.J.3
  • 6
    • 0028077064 scopus 로고
    • Characterization and subcellular localization of ribonuclease H activities fromXenopus laevis
    • Cazenave C., Frank P., Toulme J. J., Büsen W. Characterization and subcellular localization of ribonuclease H activities fromXenopus laevis. J. Biol. Chem. 269:1994;25185-25192.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25185-25192
    • Cazenave, C.1    Frank, P.2    Toulme, J.J.3    Büsen, W.4
  • 7
    • 0029295965 scopus 로고
    • The non-RNase H domain ofSaccharomyces cerevisiae
    • Cerritelli S. M., Crouch R. J. The non-RNase H domain ofSaccharomyces cerevisiae. RNA. 1:1995;246-259.
    • (1995) RNA , vol.1 , pp. 246-259
    • Cerritelli, S.M.1    Crouch, R.J.2
  • 8
    • 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., Crouch R. J. A common 40 amino acid motif in eukaryotic RNases H1 and caulimovirus ORF VI proteins binds to duplex RNAs. Nucleic Acids Res. 26:1998;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
  • 10
    • 0030881588 scopus 로고    scopus 로고
    • Homologous recombination of a flanking repeat gene cluster is a mechanism for a common contiguous gene deletion syndrome
    • Chen K. S., Manian P., Koeuth T., Potocki L., Zhao Q., Chinault A. C., Lee C. C., Lupski J. R. Homologous recombination of a flanking repeat gene cluster is a mechanism for a common contiguous gene deletion syndrome. Nat. Genet. 17:1997;154-163.
    • (1997) Nat. Genet. , vol.17 , pp. 154-163
    • Chen, K.S.1    Manian, P.2    Koeuth, T.3    Potocki, L.4    Zhao, Q.5    Chinault, A.C.6    Lee, C.C.7    Lupski, J.R.8
  • 12
    • 0025084228 scopus 로고
    • Ribonuclease H: From discovery to 3D structure
    • Crouch R. J. Ribonuclease H: From discovery to 3D structure. New Biol. 2:1990;771-777.
    • (1990) New Biol. , vol.2 , pp. 771-777
    • Crouch, R.J.1
  • 13
    • 0025908083 scopus 로고
    • Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase
    • Davies J. F. II, Hostomska Z., Hostomsky Z., Jordan S. R., Matthews D. Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase. Science. 252:1991;88-95.
    • (1991) Science , vol.252 , pp. 88-95
    • Davies J.F. II1    Hostomska, Z.2    Hostomsky, Z.3    Jordan, S.R.4    Matthews, D.5
  • 14
    • 0027317932 scopus 로고
    • Molecular dissection of the cauliflower mosaic virus translation transactivator
    • De Tapia M., Himmelbach A., Hohn T. Molecular dissection of the cauliflower mosaic virus translation transactivator. EMBO J. 12:1993;3305-3314.
    • (1993) EMBO J. , vol.12 , pp. 3305-3314
    • De Tapia, M.1    Himmelbach, A.2    Hohn, T.3
  • 15
    • 0031587425 scopus 로고    scopus 로고
    • Functional characterization of RNase H1 fromDrosophila melanogaster
    • Filippov V., Filippova M., Gill S. S. Functional characterization of RNase H1 fromDrosophila melanogaster. Biochem. Biophys. Res. Commun. 240: 1997;844-849.
    • (1997) Biochem. Biophys. Res. Commun. , vol.240 , pp. 844-849
    • Filippov, V.1    Filippova, M.2    Gill, S.S.3
  • 16
    • 0028618222 scopus 로고
    • Purification and characterization of human ribonuclease HII
    • Frank P., Albert S., Cazenave C., Toulme J. J. Purification and characterization of human ribonuclease HII. Nucleic Acid Res. 22:1994;5247-5254.
    • (1994) Nucleic Acid Res. , vol.22 , pp. 5247-5254
    • Frank, P.1    Albert, S.2    Cazenave, C.3    Toulme, J.J.4
  • 17
    • 0032472275 scopus 로고    scopus 로고
    • Yeast RNase H(35) is the counterpart of the mammalian RNase H1, and is evolutionarily related to prokaryotic RNase HII
    • Frank P., Braunshofer-Reiter C., Wintersberger U. Yeast RNase H(35) is the counterpart of the mammalian RNase H1, and is evolutionarily related to prokaryotic RNase HII. FEBS Lett. 421:1998;23-26.
    • (1998) FEBS Lett. , vol.421 , pp. 23-26
    • Frank, P.1    Braunshofer-Reiter, C.2    Wintersberger, U.3
  • 18
    • 0030723133 scopus 로고    scopus 로고
    • Human genes encoding U3 snRNA associate with coiled bodies in interphase cells and are clustered on chromosome 17p11.2 in a complex inverted repeat structure
    • Gao L., Frey M. R., Matera A. G. Human genes encoding U3 snRNA associate with coiled bodies in interphase cells and are clustered on chromosome 17p11.2 in a complex inverted repeat structure. Nucleic Acids Res. 25:1997;4740-4747.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4740-4747
    • Gao, L.1    Frey, M.R.2    Matera, A.G.3
  • 19
    • 0029278868 scopus 로고
    • Localization of two mouse genes encoding the protein tyrosine kinase receptor-related protein RYK
    • Gough N. M., Rakar S., Hovens C. M., Wilks A. Localization of two mouse genes encoding the protein tyrosine kinase receptor-related protein RYK. Mamm. Genome. 6:1995;255-256.
    • (1995) Mamm. Genome , vol.6 , pp. 255-256
    • Gough, N.M.1    Rakar, S.2    Hovens, C.M.3    Wilks, A.4
  • 20
    • 0027105279 scopus 로고
    • Two RNA-binding motifs in the double-stranded RNA-activated protein kinase, DAI
    • Green S. R., Mathews M. B. Two RNA-binding motifs in the double-stranded RNA-activated protein kinase, DAI. Genes Dev. 6:1992;2478-2490.
    • (1992) Genes Dev. , vol.6 , pp. 2478-2490
    • Green, S.R.1    Mathews, M.B.2
  • 21
    • 0027225483 scopus 로고
    • Modes of DAPI banding and simultaneousin-situ
    • Heng H. H., Tsui L. C. Modes of DAPI banding and simultaneousin-situ. Chromosoma. 102:1993;325-332.
    • (1993) Chromosoma , vol.102 , pp. 325-332
    • Heng, H.H.1    Tsui, L.C.2
  • 22
    • 0031007919 scopus 로고    scopus 로고
    • Molecular cloning and expression of a ribonuclease H from the kinetoplastid,Trypanosoma brucei
    • Hesslein D. G., Campbell A. G. Molecular cloning and expression of a ribonuclease H from the kinetoplastid,Trypanosoma brucei. Mol. Biochem. Parasitol. 86: 1997;121-126.
    • (1997) Mol. Biochem. Parasitol. , vol.86 , pp. 121-126
    • Hesslein, D.G.1    Campbell, A.G.2
  • 23
    • 0025147609 scopus 로고
    • Isolation and characterization of a second RNase H (RNase HII) ofEscherichia colirnhB
    • Itaya M. Isolation and characterization of a second RNase H (RNase HII) ofEscherichia colirnhB. Proc. Natl. Acad. Sci. USA. 87:1990;8587-8591.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8587-8591
    • Itaya, M.1
  • 24
    • 0025734265 scopus 로고
    • Selective cloning of genes encoding RNase H fromSalmonella typhimurium, Saccharomyces cerevisiaeEscherichia coli rnh
    • Itaya M., McKelvin D., Chatterjie S. K., Crouch R. J. Selective cloning of genes encoding RNase H fromSalmonella typhimurium, Saccharomyces cerevisiaeEscherichia coli rnh. Mol. Gen. Genet. 227:1991;438-445.
    • (1991) Mol. Gen. Genet. , vol.227 , pp. 438-445
    • Itaya, M.1    McKelvin, D.2    Chatterjie, S.K.3    Crouch, R.J.4
  • 25
    • 0020660180 scopus 로고
    • DNA sequence of the gene coding forEscherichia coli
    • Kanaya S., Crouch R. J. DNA sequence of the gene coding forEscherichia coli. J. Biol. Chem. 258:1983;1276-1281.
    • (1983) J. Biol. Chem. , vol.258 , pp. 1276-1281
    • Kanaya, S.1    Crouch, R.J.2
  • 26
    • 0023767485 scopus 로고
    • In addition to RNase H(70) two other proteins ofSaccharomyces cerevisiae
    • Karwan R., Wintersberger U. In addition to RNase H(70) two other proteins ofSaccharomyces cerevisiae. J. Biol. Chem. 263:1988;14970-14977.
    • (1988) J. Biol. Chem. , vol.263 , pp. 14970-14977
    • Karwan, R.1    Wintersberger, U.2
  • 28
    • 0023665902 scopus 로고
    • An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs
    • Kozak M. An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res. 15:1987;8125-8148.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 8125-8148
    • Kozak, M.1
  • 29
    • 0027985464 scopus 로고
    • Eukaryotic RNase H shares a conserved domain with caulimovirus proteins that facilitate translation of polycistronic RNA
    • Mushegian A. M., Edskes H. K., Koonin E. V. Eukaryotic RNase H shares a conserved domain with caulimovirus proteins that facilitate translation of polycistronic RNA. Nucleic Acids Res. 22:1994;4163-4166.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4163-4166
    • Mushegian, A.M.1    Edskes, H.K.2    Koonin, E.V.3
  • 31
    • 0030977397 scopus 로고    scopus 로고
    • Alanine-scanning mutations in the "primer grip" of p66 HIV-1 reverse transcriptase resultin selective loss of RNA priming activity
    • Powell M. D., Ghosh M., Jacques P. S., Howard K. J., Le Grice S. F., Levin J. G. Alanine-scanning mutations in the "primer grip" of p66 HIV-1 reverse transcriptase resultin selective loss of RNA priming activity. J. Biol. Chem. 272:1997;13262-13269.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13262-13269
    • Powell, M.D.1    Ghosh, M.2    Jacques, P.S.3    Howard, K.J.4    Le Grice, S.F.5    Levin, J.G.6
  • 32
    • 0014682495 scopus 로고
    • Enzyme from calf thymus degrading the RNA moiety of DNA-RNA hybrids: Effect on DNA dependent RNA polymerase
    • Stein H., Hausen P. Enzyme from calf thymus degrading the RNA moiety of DNA-RNA hybrids: Effect on DNA dependent RNA polymerase. Science. 166:1969;393-395.
    • (1969) Science , vol.166 , pp. 393-395
    • Stein, H.1    Hausen, P.2
  • 36
    • 0025129937 scopus 로고
    • Structure of ribonuclease H phased at 2 Å resolution by MAD analysis of the selenomethionyl protein
    • Yang W., Hendrickson W. A., Crouch R. J., Satow Y. Structure of ribonuclease H phased at 2 Å resolution by MAD analysis of the selenomethionyl protein. Science. 249:1990;1398-1405.
    • (1990) Science , vol.249 , pp. 1398-1405
    • Yang, W.1    Hendrickson, W.A.2    Crouch, R.J.3    Satow, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.