메뉴 건너뛰기




Volumn 38, Issue 5, 1998, Pages 797-806

Molecular characterization of tobacco ribonucleotide reductase RNR1 and RNR2 cDNAs and cell cycle-regulated expression in synchronized plant cells

Author keywords

Cell cycle; Gene expression; Ribonucleotide reductase; S phase; Tobacco BY2 cell suspension

Indexed keywords

CDNA LIBRARY; CELL CYCLE; DEOXYRIBONUCLEOTIDE; DNA SYNTHESIS; GENE EXPRESSION; MESSENGER RNA; PLANT CELL; RIBONUCLEOTIDE REDUCTASE; SOUTHERN BLOTTING;

EID: 0032215053     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006083318906     Document Type: Article
Times cited : (30)

References (38)
  • 2
    • 0029840345 scopus 로고    scopus 로고
    • Defining a novel cis element in the 3′ untranslated region of mammalian ribonucleotide reductase component R2 mRNA
    • Amara FM, Sun J, Wright JA: Defining a novel cis element in the 3′ untranslated region of mammalian ribonucleotide reductase component R2 mRNA. J Biol Chem 271: 20126-20131 (1996).
    • (1996) J Biol Chem , vol.271 , pp. 20126-20131
    • Amara, F.M.1    Sun, J.2    Wright, J.A.3
  • 3
    • 0027086428 scopus 로고
    • An S-phase specific release from a transcriptional block regulates the expression of mouse ribonucleotide reductase R2 subunit
    • Björklund S, Skogman E, Thelander L: An S-phase specific release from a transcriptional block regulates the expression of mouse ribonucleotide reductase R2 subunit. EMBO J 11: 4953-4959 (1992).
    • (1992) EMBO J , vol.11 , pp. 4953-4959
    • Björklund, S.1    Skogman, E.2    Thelander, L.3
  • 4
    • 0029774568 scopus 로고    scopus 로고
    • Deoxyribonucleotide synthesis in green algae: Cell cycle fluctuation of ribonucleotide reductase is only moderate in the unicellular, exsymbiotic green algae, Chlorella sp. pbi
    • Bornemann C, Drude K, Follmann H: Deoxyribonucleotide synthesis in green algae: cell cycle fluctuation of ribonucleotide reductase is only moderate in the unicellular, exsymbiotic green algae, Chlorella sp. pbi. J Plant Physiol 148: 657-661 (1996).
    • (1996) J Plant Physiol , vol.148 , pp. 657-661
    • Bornemann, C.1    Drude, K.2    Follmann, H.3
  • 5
    • 0027146287 scopus 로고
    • Cloning and characterization of subunit genes of ribonucleotide reductase, a cell-cycle-regulated enzyme from Plasmodium falciparum
    • Chakbrabarti D, Schuster SM, Chakbrabarti R: Cloning and characterization of subunit genes of ribonucleotide reductase, a cell-cycle-regulated enzyme from Plasmodium falciparum. Proc Natl Acad Sci USA 90: 12020-12024 (1993).
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 12020-12024
    • Chakbrabarti, D.1    Schuster, S.M.2    Chakbrabarti, R.3
  • 6
    • 0027990745 scopus 로고
    • Regulation of mammalian ribonucleotide reductase R1 mRNA stability is mediated by a ribonucleotide reductase R1 mRNA 3′-untranslated region cis-trans interaction through a protein kinase C-controlled pathway
    • Chen FY, Amara FM, Wright JA: Regulation of mammalian ribonucleotide reductase R1 mRNA stability is mediated by a ribonucleotide reductase R1 mRNA 3′-untranslated region cis-trans interaction through a protein kinase C-controlled pathway. Biochem J 302: 125-132 (1994).
    • (1994) Biochem J , vol.302 , pp. 125-132
    • Chen, F.Y.1    Amara, F.M.2    Wright, J.A.3
  • 7
    • 0028110330 scopus 로고
    • Mimosine inhibits viral DNA synthesis through ribonucleotide reductase
    • Dai Y, Gold B, Vishwanatha JK, Rhode SL: Mimosine inhibits viral DNA synthesis through ribonucleotide reductase. Virology 205: 210-216 (1994).
    • (1994) Virology , vol.205 , pp. 210-216
    • Dai, Y.1    Gold, B.2    Vishwanatha, J.K.3    Rhode, S.L.4
  • 8
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux JPH, Smithies O: A comprehensive set of sequence analysis programs for the VAX. Nucl Acids Res 12: 387-396 (1984).
    • (1984) Nucl Acids Res , vol.12 , pp. 387-396
    • Devereux, J.P.H.1    Smithies, O.2
  • 9
    • 0023395932 scopus 로고
    • Identification and isolation of the gene encoding the small subunit of ribonucleotide reductase from Saccharomyces cerevisiae: DNA damage-inducible gene required for mitotic viability
    • Elledge SJ, Davis RW: Identification and isolation of the gene encoding the small subunit of ribonucleotide reductase from Saccharomyces cerevisiae: DNA damage-inducible gene required for mitotic viability. Mol Cell Biol 7: 2783-2793 (1987).
    • (1987) Mol Cell Biol , vol.7 , pp. 2783-2793
    • Elledge, S.J.1    Davis, R.W.2
  • 10
    • 0025350420 scopus 로고
    • Two genes, differentially regulated in the cell cycle and by DNA-damaging agents encode alternative regulatory subunits of ribonucleotide reductase
    • Elledge SJ, Davis RW: Two genes, differentially regulated in the cell cycle and by DNA-damaging agents encode alternative regulatory subunits of ribonucleotide reductase. Genes Devel 4: 740-751 (1990).
    • (1990) Genes Devel , vol.4 , pp. 740-751
    • Elledge, S.J.1    Davis, R.W.2
  • 11
    • 0027605113 scopus 로고
    • DNA damage and cell cycle regulation of ribonucleotide reductase
    • Elledge SJ, Zhou Z, Allen JB, Navas TA: DNA damage and cell cycle regulation of ribonucleotide reductase. BioEssays 15: 333-339 (1993).
    • (1993) BioEssays , vol.15 , pp. 333-339
    • Elledge, S.J.1    Zhou, Z.2    Allen, J.B.3    Navas, T.A.4
  • 12
    • 0017133579 scopus 로고
    • Ribonucleotide reductase activity in green algae
    • Feller W, Follmann H: Ribonucleotide reductase activity in green algae. Biochem Biophys Res Commun 70: 752-758 (1976).
    • (1976) Biochem Biophys Res Commun , vol.70 , pp. 752-758
    • Feller, W.1    Follmann, H.2
  • 13
    • 0025336798 scopus 로고
    • Analysis of premRNA processing in transfected protoplasts
    • Goodall G, Wiebauer K, Filipowicz W: Analysis of premRNA processing in transfected protoplasts. Meth Enzymol 181: 148-161 (1990).
    • (1990) Meth Enzymol , vol.181 , pp. 148-161
    • Goodall, G.1    Wiebauer, K.2    Filipowicz, W.3
  • 14
    • 0029684610 scopus 로고    scopus 로고
    • Regulation of synthesis of ribonucleotide reductase and relationship to DNA replication in various systems
    • Greenberg GR, Hilfinger JM: Regulation of synthesis of ribonucleotide reductase and relationship to DNA replication in various systems. Prog Nucl Acid Res Mol Biol 53: 345-392 (1996).
    • (1996) Prog Nucl Acid Res Mol Biol , vol.53 , pp. 345-392
    • Greenberg, G.R.1    Hilfinger, J.M.2
  • 15
    • 84995062994 scopus 로고
    • Okadaid acid as a probe to analyse the cell cycle progression in plant cells
    • Hasezawa S, Nagata T: Okadaid acid as a probe to analyse the cell cycle progression in plant cells. Bot Acta 105: 63-69 (1992).
    • (1992) Bot Acta , vol.105 , pp. 63-69
    • Hasezawa, S.1    Nagata, T.2
  • 16
    • 0023426281 scopus 로고
    • Identification of the gene for the yeast ribonucleotide reductase small subunit and its inducibility by methyl methanesulfonate
    • Hurd HK, Roberts CW, Roberts JW: Identification of the gene for the yeast ribonucleotide reductase small subunit and its inducibility by methyl methanesulfonate. Mol Cell Biol 7: 3673-3677 (1987).
    • (1987) Mol Cell Biol , vol.7 , pp. 3673-3677
    • Hurd, H.K.1    Roberts, C.W.2    Roberts, J.W.3
  • 17
    • 0029585370 scopus 로고
    • The TATA-less promoter of mouse ribonucleotide reductase R1 gene contains a TFII-I binding initiator element essential for cell cycle- Regulated transcription
    • Johansson E, Skogman E, Thelander L: The TATA-less promoter of mouse ribonucleotide reductase R1 gene contains a TFII-I binding initiator element essential for cell cycle- regulated transcription. J Biol Chem 270: 30162-30167 (1995).
    • (1995) J Biol Chem , vol.270 , pp. 30162-30167
    • Johansson, E.1    Skogman, E.2    Thelander, L.3
  • 18
    • 0030580112 scopus 로고    scopus 로고
    • The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2
    • Kauppi B, Nielsen BB, Ramaswamy S, Kjoller Larsen I, Thelander M, L. T., Eklund H: The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2. J Mol Biol 262: 706-720 (1996).
    • (1996) J Mol Biol , vol.262 , pp. 706-720
    • Kauppi, B.1    Nielsen, B.B.2    Ramaswamy, S.3    Kjoller Larsen, I.4    Thelander, M.5    L., T.6    Eklund, H.7
  • 19
    • 0027589196 scopus 로고
    • Mammalian proliferating cell nuclear antigen1 stimulates the processivity of two wheat embryo DNA polymerases
    • Laquel P, Litvak S, Castroviejo M: Mammalian proliferating cell nuclear antigen1 stimulates the processivity of two wheat embryo DNA polymerases. Plant Physiol 102: 107-114 (1993).
    • (1993) Plant Physiol , vol.102 , pp. 107-114
    • Laquel, P.1    Litvak, S.2    Castroviejo, M.3
  • 20
    • 0026503081 scopus 로고
    • A plant histone promoter can direct both replication-dependent and -independent gene expression in transgenic plants
    • Lepetit M, Ehling M, Atanassova R, Chaubet N, Gigot C: A plant histone promoter can direct both replication-dependent and -independent gene expression in transgenic plants. Mol Gen Genet 231: 276-285 (1992).
    • (1992) Mol Gen Genet , vol.231 , pp. 276-285
    • Lepetit, M.1    Ehling, M.2    Atanassova, R.3    Chaubet, N.4    Gigot, C.5
  • 22
    • 0030271304 scopus 로고    scopus 로고
    • Chemical inhibitors of cyclin-dependent kinases
    • Meijer L: Chemical inhibitors of cyclin-dependent kinases. Trends Cell Biol 6: 393-397 (1996).
    • (1996) Trends Cell Biol , vol.6 , pp. 393-397
    • Meijer, L.1
  • 24
    • 0026568783 scopus 로고
    • Tobacco BY2 cell line as the 'Hela' cell in the cell biology of higher plants
    • Nagata T, Nemoto Y, Hazezawa S: Tobacco BY2 cell line as the 'Hela' cell in the cell biology of higher plants. Int Rev Cytol 132: 1-30 (1992).
    • (1992) Int Rev Cytol , vol.132 , pp. 1-30
    • Nagata, T.1    Nemoto, Y.2    Hazezawa, S.3
  • 25
    • 0027380398 scopus 로고
    • Reduction and loss of the iron center in the reaction of the small subunit of mouse ribonucleotide reductase with hydroxyurea
    • Nyholm S, Thelander L, Gräslund A: Reduction and loss of the iron center in the reaction of the small subunit of mouse ribonucleotide reductase with hydroxyurea. Biochemistry 32: 11569-11574 (1993).
    • (1993) Biochemistry , vol.32 , pp. 11569-11574
    • Nyholm, S.1    Thelander, L.2    Gräslund, A.3
  • 26
    • 0028917867 scopus 로고
    • Molecular characterization and cell cycle-regulated expression of a cDNA clone from Arabidopsis thaliana homologous to the small subunit of ribonucleotide reductase
    • Philipps G, Clement B, Gigot C: Molecular characterization and cell cycle-regulated expression of a cDNA clone from Arabidopsis thaliana homologous to the small subunit of ribonucleotide reductase. FEBS Lett 358: 67-70 (1995).
    • (1995) FEBS Lett , vol.358 , pp. 67-70
    • Philipps, G.1    Clement, B.2    Gigot, C.3
  • 27
    • 0028822845 scopus 로고
    • The tef1 box, a ubiquitous cis-acting element involved in the activation of plant genes that are highly expressed in cycling cells
    • Regad F, Herve C, Marinx O, Bergounioux C, Tremoussaygue D, Lescure B: The tef1 box, a ubiquitous cis-acting element involved in the activation of plant genes that are highly expressed in cycling cells. Mol Gen Genet 248: 703-711 (1995).
    • (1995) Mol Gen Genet , vol.248 , pp. 703-711
    • Regad, F.1    Herve, C.2    Marinx, O.3    Bergounioux, C.4    Tremoussaygue, D.5    Lescure, B.6
  • 28
    • 0023925454 scopus 로고
    • Interactions between deoxyribonucleotide and DNA synthesis
    • Reichard P: Interactions between deoxyribonucleotide and DNA synthesis. Annu Rev Biochem 57: 349-374 (1988).
    • (1988) Annu Rev Biochem , vol.57 , pp. 349-374
    • Reichard, P.1
  • 29
    • 0030447082 scopus 로고    scopus 로고
    • Multiple A-type cyclins express sequentially during the cell cycle in Nicotiana tabacum BY2 cells
    • Reichheld J-P, Chaubet N, Shen WH, Renaudin J-P, Gigot C: Multiple A-type cyclins express sequentially during the cell cycle in Nicotiana tabacum BY2 cells. Proc Natl Acad Sci USA 93: 13819-13824 (1996).
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13819-13824
    • Reichheld, J.-P.1    Chaubet, N.2    Shen, W.H.3    Renaudin, J.-P.4    Gigot, C.5
  • 30
    • 0029168432 scopus 로고
    • Cell cycle-regulated histone gene expression in synchronized plant cells
    • Reichheld JP, Sonobe S, Clement B, Chaubet N, Gigot C: Cell cycle-regulated histone gene expression in synchronized plant cells. Plant J 7: 245-252 (1995).
    • (1995) Plant J , vol.7 , pp. 245-252
    • Reichheld, J.P.1    Sonobe, S.2    Clement, B.3    Chaubet, N.4    Gigot, C.5
  • 32
    • 0030784963 scopus 로고    scopus 로고
    • Ribonucleotide reductase from the higher plant Arabidopsis thaliana: Expression of the R2 component and characterization of its iron-radical center
    • Sauge-Merle S, Laulhere JP, Coves J, Le Pape L, Menage S, Fontecave M: Ribonucleotide reductase from the higher plant Arabidopsis thaliana: expression of the R2 component and characterization of its iron-radical center. J Biol Inorg Chem 2: 586-594 (1997).
    • (1997) J Biol Inorg Chem , vol.2 , pp. 586-594
    • Sauge-Merle, S.1    Laulhere, J.P.2    Coves, J.3    Le Pape, L.4    Menage, S.5    Fontecave, M.6
  • 33
    • 0019321430 scopus 로고
    • Ribonucleotide reductase of calf thymus
    • Thelander L, Erikson L, Akerman M: Ribonucleotide reductase of calf thymus. J Biol Chem 255: 7426-7432 (1980).
    • (1980) J Biol Chem , vol.255 , pp. 7426-7432
    • Thelander, L.1    Erikson, L.2    Akerman, M.3
  • 34
    • 0021908232 scopus 로고
    • Subunit M2 of mammalian ribonucleotide reductase. Characterization of a homologous protein isolated from M2-overproducing mouse cells
    • Thelander M, Gräslund A, Thelander L: Subunit M2 of mammalian ribonucleotide reductase. Characterization of a homologous protein isolated from M2-overproducing mouse cells. J Biol Chem 260: 2737-2741 (1985).
    • (1985) J Biol Chem , vol.260 , pp. 2737-2741
    • Thelander, M.1    Gräslund, A.2    Thelander, L.3
  • 35
    • 0027968068 scopus 로고
    • Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thomson JD, Higgins DG, Gibson TJ: Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl Acids Res 22: 4673-4680 (1994).
    • (1994) Nucl Acids Res , vol.22 , pp. 4673-4680
    • Thomson, J.D.1    Higgins, D.G.2    Gibson, T.J.3    Clustal, W.4
  • 36
    • 0028486194 scopus 로고
    • Structure of ribonucleotide reductase protein R1
    • Uhlin U, Eklund H: Structure of ribonucleotide reductase protein R1. Nature 370: 533-539 (1994).
    • (1994) Nature , vol.370 , pp. 533-539
    • Uhlin, U.1    Eklund, H.2
  • 37
    • 0026651652 scopus 로고
    • Analysis of the DNA damage sensory pathway through the isolation and characterization of the CRT mutants, constitutive for RNR3 transcription
    • Zhou Z, Elledge SJ: Analysis of the DNA damage sensory pathway through the isolation and characterization of the CRT mutants, constitutive for RNR3 transcription. Genetics 131: 851-866 (1992).
    • (1992) Genetics , vol.131 , pp. 851-866
    • Zhou, Z.1    Elledge, S.J.2
  • 38
    • 0017595790 scopus 로고
    • DNA sequence organization in the genome of Nicotiana tabacum
    • Zimmermann JI, Goldberg RB: DNA sequence organization in the genome of Nicotiana tabacum. Chromosoma 59: 227-252 (1977).
    • (1977) Chromosoma , vol.59 , pp. 227-252
    • Zimmermann, J.I.1    Goldberg, R.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.