메뉴 건너뛰기




Volumn 125, Issue 5, 1999, Pages 939-946

Molecular cloning of mouse p47, a second group mammalian RuvB DNA helicase-like protein: Homology with those from human and Saccharomyces cerevisiae

Author keywords

cDNA cloning; DNA helicase; p47; RuvB; RUVB like protein

Indexed keywords

BACTERIAL DNA; BUFFER; COMPLEMENTARY DNA; DNA BINDING PROTEIN; DNA FRAGMENT; HELICASE; PROTEIN P47; UNCLASSIFIED DRUG; WHEAT GERM AGGLUTININ;

EID: 0033023915     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022372     Document Type: Article
Times cited : (19)

References (34)
  • 1
    • 0029995337 scopus 로고    scopus 로고
    • Processing the Holliday junction in homologous recombination
    • Shinagawa, H. and Iwasaki, H. (1996) Processing the Holliday junction in homologous recombination. Trends Biochem. Sci. 21, 107-111
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 107-111
    • Shinagawa, H.1    Iwasaki, H.2
  • 2
    • 0031453378 scopus 로고    scopus 로고
    • Processing of recombination intermediates by the RuvABC proteins
    • West, S.C. (1997) Processing of recombination intermediates by the RuvABC proteins. Annu. Rev. Genet. 31, 213-244
    • (1997) Annu. Rev. Genet. , vol.31 , pp. 213-244
    • West, S.C.1
  • 3
    • 0026751086 scopus 로고
    • Semidominant suppressors of srs2 helicase mutations of Saccharomyces cereviciae map in the RAD51 gene whose sequence predicts a protein with similarities to prokaryotic RecA proteins
    • Aboussekhara, A., Chanet, R., Adjira, A., and Fabre, F. (1992) Semidominant suppressors of srs2 helicase mutations of Saccharomyces cereviciae map in the RAD51 gene whose sequence predicts a protein with similarities to prokaryotic RecA proteins. Mol. Cell. Biol. 12, 3224-3234
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3224-3234
    • Aboussekhara, A.1    Chanet, R.2    Adjira, A.3    Fabre, F.4
  • 4
    • 0031004885 scopus 로고    scopus 로고
    • A single-stranded DNA-binding protein is needed for efficient complex formation by the Saccharomyces cerevisiae Rad51 protein
    • Sugiyama, T., Zaitseva, E.M., and Kowalczykowski, S.C. (1997) A single-stranded DNA-binding protein is needed for efficient complex formation by the Saccharomyces cerevisiae Rad51 protein. J. Biol. Chem. 272, 7940-7945
    • (1997) J. Biol. Chem. , vol.272 , pp. 7940-7945
    • Sugiyama, T.1    Zaitseva, E.M.2    Kowalczykowski, S.C.3
  • 5
    • 0029148844 scopus 로고
    • Rad51 homologs in Xenopus laevis: Two distinct genes are highly expressed in ovary and testis
    • Maeshima, K., Morimatsu, K., Shinohara, A., and Horii, T. (1995) Rad51 homologs in Xenopus laevis: Two distinct genes are highly expressed in ovary and testis. Gene 160, 195-200
    • (1995) Gene , vol.160 , pp. 195-200
    • Maeshima, K.1    Morimatsu, K.2    Shinohara, A.3    Horii, T.4
  • 7
    • 0030584084 scopus 로고    scopus 로고
    • Human Rad51 protein promotes ATP-dependent homologous pairing and strand transfer reactions in vitro
    • Baumann, P., Benson, F.E., and West, S.C. (1996) Human Rad51 protein promotes ATP-dependent homologous pairing and strand transfer reactions in vitro. Cell 87, 757-766
    • (1996) Cell , vol.87 , pp. 757-766
    • Baumann, P.1    Benson, F.E.2    West, S.C.3
  • 11
    • 0024344173 scopus 로고
    • Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes
    • Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., and Blinov, V.M. (1989) Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes. Nucleic Acids Res. 17, 4713-4730
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4713-4730
    • Gorbalenya, A.E.1    Koonin, E.V.2    Donchenko, A.P.3    Blinov, V.M.4
  • 12
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequence comparisons and structure-function relationships
    • Gorbalenya, A.E. and Koonin, E. V. (1993) Helicases: amino acid sequence comparisons and structure-function relationships. Curr. Opin. Struct. Biol. 3, 419-429
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 14
    • 0014032729 scopus 로고
    • Nuclei from rat liver: Isolation method that combines purity with high yield
    • Blobel, G. and Potter, V.R. (1966) Nuclei from rat liver: Isolation method that combines purity with high yield. Science 154, 1662-1665
    • (1966) Science , vol.154 , pp. 1662-1665
    • Blobel, G.1    Potter, V.R.2
  • 15
    • 0027503111 scopus 로고
    • Purification and characterization of a nuclear pore glycoprotein complex containing p62
    • Kita, K., Omata, S., and Horigome, T. (1993) Purification and characterization of a nuclear pore glycoprotein complex containing p62. J. Biochem. 113, 377-382
    • (1993) J. Biochem. , vol.113 , pp. 377-382
    • Kita, K.1    Omata, S.2    Horigome, T.3
  • 16
    • 0345070452 scopus 로고    scopus 로고
    • Reversed-phase high-performance liquid chromatography of membrane proteins on perfusion-type polystyrene resin columns in 60% formic acid
    • Kikuchi, N., Yamakawa, Y., Ichimura, T., Omata, S., and Horigome, T. (1997) Reversed-phase high-performance liquid chromatography of membrane proteins on perfusion-type polystyrene resin columns in 60% formic acid. Chromatography 18, 175-184
    • (1997) Chromatography , vol.18 , pp. 175-184
    • Kikuchi, N.1    Yamakawa, Y.2    Ichimura, T.3    Omata, S.4    Horigome, T.5
  • 17
    • 0031001130 scopus 로고    scopus 로고
    • cDNA cloning of nuclear localization signal binding protein NBP60, a rat homologue of lamin B receptor, and identification of binding sites of human lamin B receptor for nuclear localization signals and chromatin
    • Kawahire, S., Takeuchi, M., Gohshi, T., Sasagawa, S., Shimada, M., Takahashi, M., Abe, T.K., Ueda, T., Kuwano, R., Hikawa, A., Ichimura, T., Omata, S., and Horigome, T. (1997) cDNA cloning of nuclear localization signal binding protein NBP60, a rat homologue of lamin B receptor, and identification of binding sites of human lamin B receptor for nuclear localization signals and chromatin. J. Biochem. 121, 881-889
    • (1997) J. Biochem. , vol.121 , pp. 881-889
    • Kawahire, S.1    Takeuchi, M.2    Gohshi, T.3    Sasagawa, S.4    Shimada, M.5    Takahashi, M.6    Abe, T.K.7    Ueda, T.8    Kuwano, R.9    Hikawa, A.10    Ichimura, T.11    Omata, S.12    Horigome, T.13
  • 19
    • 0038066022 scopus 로고
    • Purification of 39 kDa and 50 kDa putative nucleoporins from rat liver nuclear envelopes
    • Imai, N., Saito, M., Denta, K., Ichimura, T., Omata, S., and Horigome, T. (1995) Purification of 39 kDa and 50 kDa putative nucleoporins from rat liver nuclear envelopes. Biochem. (Life Sci. Adv.) 14, 59-66
    • (1995) Biochem. (Life Sci. Adv.) , vol.14 , pp. 59-66
    • Imai, N.1    Saito, M.2    Denta, K.3    Ichimura, T.4    Omata, S.5    Horigome, T.6
  • 20
    • 0028170790 scopus 로고
    • Hexameric rings of Escherichia coli RuvB protein. Cooperative assembly, processivity and ATPase activity
    • Mitchell, A.H. and West, S.C. (1994) Hexameric rings of Escherichia coli RuvB protein. Cooperative assembly, processivity and ATPase activity. J. Mol Biol. 243, 208-215
    • (1994) J. Mol Biol. , vol.243 , pp. 208-215
    • Mitchell, A.H.1    West, S.C.2
  • 22
    • 0024546509 scopus 로고
    • The scanning model for translation: An update
    • Kozak, M. (1989) The scanning model for translation: An update. J. Cell Biol. 108, 229-241
    • (1989) J. Cell Biol. , vol.108 , pp. 229-241
    • Kozak, M.1
  • 23
    • 0029904186 scopus 로고    scopus 로고
    • Evidence for involvement of rores-acting factors in selection of the AUG start codon during eukaryotic translational initiation
    • Mcbratney, S. and Sarnow, P. (1996) Evidence for involvement of (rores-acting factors in selection of the AUG start codon during eukaryotic translational initiation. Mol. Cell. Biol. 16, 3523 3534
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3523-3534
    • McBratney, S.1    Sarnow, P.2
  • 24
    • 0001607723 scopus 로고
    • Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes, and a common nucleotide binding fold
    • Walker, J.E., Saraste, M., Runswick, M.J., and Gay, N.J. (1982) Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes, and a common nucleotide binding fold. EMBO J. 8, 945-951
    • (1982) EMBO J. , vol.8 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 25
    • 0027476446 scopus 로고
    • RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro
    • Tsaneva, I.R., Müller, B., and West, S.C. (1993) RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro. Proc. Natl. Acad. Sci. USA 90, 1315-1319
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1315-1319
    • Tsaneva, I.R.1    Müller, B.2    West, S.C.3
  • 26
    • 0029981226 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of ruvB, and characterization of RuvB proteins from two distantly related thermophilic eubacteria
    • Tong, J. and Wetmur, J.G. (1996) Cloning, sequencing, and expression of ruvB, and characterization of RuvB proteins from two distantly related thermophilic eubacteria. J. Bacteriol. 178, 2695-2700
    • (1996) J. Bacteriol. , vol.178 , pp. 2695-2700
    • Tong, J.1    Wetmur, J.G.2
  • 27
    • 0032005902 scopus 로고    scopus 로고
    • Mechanistic parallels between DNA replication, recombination and transcription
    • Kadadek, T. (1998) Mechanistic parallels between DNA replication, recombination and transcription. Trends Biochem. Sci. 23, 79-83
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 79-83
    • Kadadek, T.1
  • 28
    • 0028965153 scopus 로고
    • Branch migration during homologous recombination: Assembly of a RuvAB-Holliday junction complex in vitro
    • Hiom, K. and West, S.C. (1995) Branch migration during homologous recombination: Assembly of a RuvAB-Holliday junction complex in vitro. Cell 80, 787-793
    • (1995) Cell , vol.80 , pp. 787-793
    • Hiom, K.1    West, S.C.2
  • 30
    • 0000148238 scopus 로고
    • Purification and analysis of RNA polymerase II transcription factors by using wheat germ agglutinin affinity chromatography
    • Jackson, S.P. and Tjian, R. (1989) Purification and analysis of RNA polymerase II transcription factors by using wheat germ agglutinin affinity chromatography. Proc. Natl. Acad. Sci. USA 86, 1781-1785
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1781-1785
    • Jackson, S.P.1    Tjian, R.2
  • 31
    • 0024334772 scopus 로고
    • A glycosylated liver-specific transcription factor stimulates transcription of the albumin gene
    • Lichtsteiner, S. and Schibler, U. (1989) A glycosylated liver-specific transcription factor stimulates transcription of the albumin gene. Cell 57, 1179-1187
    • (1989) Cell , vol.57 , pp. 1179-1187
    • Lichtsteiner, S.1    Schibler, U.2
  • 32
    • 0027289130 scopus 로고
    • RNA polymerase II is a glycoprotein. Modification of the COOH-terminal domain by O-GlcNAc
    • Kelly, W.G., Dahmus, M.E., and Hart, G.W. (1993) RNA polymerase II is a glycoprotein. Modification of the COOH-terminal domain by O-GlcNAc. J. Biol. Chem. 268, 10416-10424
    • (1993) J. Biol. Chem. , vol.268 , pp. 10416-10424
    • Kelly, W.G.1    Dahmus, M.E.2    Hart, G.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.