메뉴 건너뛰기




Volumn 114, Issue 2, 1997, Pages 643-652

Light regulation of the abundance of mRNA encoding a nucleolin-like protein localized in the nucleoli of pea nuclei

Author keywords

[No Author keywords available]

Indexed keywords

ASSAY; COMPLEMENTARY DNA; ESCHERICHIA COLI; ETIOLATION; GENE EXPRESSION; IMMUNOLOCALIZATION; IRRADIATION; LIGHT REGULATION; MESSENGER RNA; MOLECULAR CLONING; NUCLEOLIN; NUCLEOLUS; PHYTOCHROME; PISUM SATIVUM; POLYCLONAL ANTIBODY; PROTEIN LOCALIZATION; WESTERN BLOTTING; XENOPUS LAEVIS;

EID: 0031153922     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.114.2.643     Document Type: Article
Times cited : (36)

References (51)
  • 1
    • 0025014623 scopus 로고
    • Increased rRNA gene activity during a specific window of early pea development
    • Baerson SR, Kaufman LS (1990) Increased rRNA gene activity during a specific window of early pea development. Mol Cell Biol 10: 842-845
    • (1990) Mol Cell Biol , vol.10 , pp. 842-845
    • Baerson, S.R.1    Kaufman, L.S.2
  • 2
    • 0024655246 scopus 로고
    • RNA-binding proteins as developmental regulators
    • Bandziulis RJ, Swanson MS, Dreyfuss G (1989) RNA-binding proteins as developmental regulators. Genes Dev 3: 431-437
    • (1989) Genes Dev , vol.3 , pp. 431-437
    • Bandziulis, R.J.1    Swanson, M.S.2    Dreyfuss, G.3
  • 5
    • 0024966024 scopus 로고
    • Major nucleolar proteins shuttle between nucleus and cytoplasm
    • Borer RA, Lehner CF, Eppenberger HM, Nigg EA (1989) Major nucleolar proteins shuttle between nucleus and cytoplasm. Cell 56: 379-390
    • (1989) Cell , vol.56 , pp. 379-390
    • Borer, R.A.1    Lehner, C.F.2    Eppenberger, H.M.3    Nigg, E.A.4
  • 6
    • 0021760269 scopus 로고
    • Interrelations between the maturation of a 100 kDa nucleolar protein and pre rRNA synthesis in CHO cells
    • Bouche G, Caizergues-Ferrer M, Bugler B, Amalric F (1984) Interrelations between the maturation of a 100 kDa nucleolar protein and pre rRNA synthesis in CHO cells. Nucleic Acids Res 12: 3025-3035
    • (1984) Nucleic Acids Res , vol.12 , pp. 3025-3035
    • Bouche, G.1    Caizergues-Ferrer, M.2    Bugler, B.3    Amalric, F.4
  • 8
    • 0023914653 scopus 로고
    • Structure of the mouse nucleolin gene: The complete sequence reveals that each RNA binding domain is encoded by two independent exons
    • Bourbon HM, Lapeyre B, Amalric F (1988) Structure of the mouse nucleolin gene: the complete sequence reveals that each RNA binding domain is encoded by two independent exons. J Mol Biol 200: 627-638
    • (1988) J Mol Biol , vol.200 , pp. 627-638
    • Bourbon, H.M.1    Lapeyre, B.2    Amalric, F.3
  • 11
    • 0023645293 scopus 로고
    • Purification and partial characterization of a calmodulin-stimulated nucleoside triphosphatase from pea nuclei
    • Chen Y-R, Datta N, Roux SJ (1986) Purification and partial characterization of a calmodulin-stimulated nucleoside triphosphatase from pea nuclei. J Biol Chem 262: 10689-10694
    • (1986) J Biol Chem , vol.262 , pp. 10689-10694
    • Chen, Y.-R.1    Datta, N.2    Roux, S.J.3
  • 12
    • 0022427409 scopus 로고
    • Phytochrome and calcium stimulation of protein phosphorylation in isolated pea nuclei
    • Datta N, Chen Y-R, Roux SJ (1985) Phytochrome and calcium stimulation of protein phosphorylation in isolated pea nuclei. Biochem Biophys Res Commun 128: 1403-1408
    • (1985) Biochem Biophys Res Commun , vol.128 , pp. 1403-1408
    • Datta, N.1    Chen, Y.-R.2    Roux, S.J.3
  • 13
    • 0028943215 scopus 로고
    • Nucleolin is a matrix attachment region DNA-binding protein that specifically recognizes a region with high base-unpairing potential
    • Dickinson LA, Kohwi-Shigematsu T (1995) Nucleolin is a matrix attachment region DNA-binding protein that specifically recognizes a region with high base-unpairing potential. Mol Cell Biol 15: 456-465
    • (1995) Mol Cell Biol , vol.15 , pp. 456-465
    • Dickinson, L.A.1    Kohwi-Shigematsu, T.2
  • 15
    • 0028884482 scopus 로고
    • A 110-kD nuclear shuttling protein, nucleolin, binds to the neurite-promoting IKVAV site of laminin-1
    • Kibbey MC, Johnson B, Petryshyn R, Jucker M, Kleinman HK (1995) A 110-kD nuclear shuttling protein, nucleolin, binds to the neurite-promoting IKVAV site of laminin-1. J Neurosci Res 42: 314-322
    • (1995) J Neurosci Res , vol.42 , pp. 314-322
    • Kibbey, M.C.1    Johnson, B.2    Petryshyn, R.3    Jucker, M.4    Kleinman, H.K.5
  • 16
    • 0024787667 scopus 로고
    • Phytochrome induces changes in the immunodetectable level of a wall peroxidase that precede growth changes in maize seedlings
    • Kim S-H, Shinkle JR, Roux SJ (1989) Phytochrome induces changes in the immunodetectable level of a wall peroxidase that precede growth changes in maize seedlings. Proc Natl Acad Sci USA 86: 9866-9870
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 9866-9870
    • Kim, S.-H.1    Shinkle, J.R.2    Roux, S.J.3
  • 18
    • 0026742967 scopus 로고
    • Yeast NSR1 protein that has structural similarity to mammalian nucleolin is involved in pre-rRNA processing
    • Kondo K, Inouye M (1992) Yeast NSR1 protein that has structural similarity to mammalian nucleolin is involved in pre-rRNA processing. J Biol Chem 267: 16252-16258
    • (1992) J Biol Chem , vol.267 , pp. 16252-16258
    • Kondo, K.1    Inouye, M.2
  • 19
    • 0026731812 scopus 로고
    • Cold shock induction of yeast NSR1 protein and its role in pre-rRNA processing
    • Kondo K, Kowalski LRZ, Inouye M (1992) Cold shock induction of yeast NSR1 protein and its role in pre-rRNA processing, J Biol Chem 267: 16259-16265
    • (1992) J Biol Chem , vol.267 , pp. 16259-16265
    • Kondo, K.1    Kowalski, L.R.Z.2    Inouye, M.3
  • 20
    • 0342446581 scopus 로고
    • Nucleolin, the major nucleolar protein of growing eukaryotic cells: An unusual protein structure revealed by the nucleotide sequence
    • Lapeyre B, Bourbon H, Amalric F (1987) Nucleolin, the major nucleolar protein of growing eukaryotic cells: an unusual protein structure revealed by the nucleotide sequence. Proc Natl Acad Sci 84: 1472-1476
    • (1987) Proc Natl Acad Sci , vol.84 , pp. 1472-1476
    • Lapeyre, B.1    Bourbon, H.2    Amalric, F.3
  • 21
    • 0025906753 scopus 로고
    • The NSR1 gene encodes a protein that specially binds nuclear localization sequences and has two RNA recognition motifs
    • Lee W-C, Xue Z, Melese T (1991) The NSR1 gene encodes a protein that specially binds nuclear localization sequences and has two RNA recognition motifs. J Cell Biol 113: 1-12
    • (1991) J Cell Biol , vol.113 , pp. 1-12
    • Lee, W.-C.1    Xue, Z.2    Melese, T.3
  • 22
    • 0026776083 scopus 로고
    • NSR1 is required for pre-rRNA processing and for the proper maintenance of steadystate levels of ribosomal subunits
    • Lee W-C, Zabetakis D, Melese T (1992) NSR1 is required for pre-rRNA processing and for the proper maintenance of steadystate levels of ribosomal subunits. Mol Cell Biol 12: 3865-3871
    • (1992) Mol Cell Biol , vol.12 , pp. 3865-3871
    • Lee, W.-C.1    Zabetakis, D.2    Melese, T.3
  • 24
    • 0026884030 scopus 로고
    • Purification and characterization of a casein kinase 2-type protein kinase from pea nuclei
    • Li H, Roux SJ (1992) Purification and characterization of a casein kinase 2-type protein kinase from pea nuclei. Plant Physiol 99: 686-692
    • (1992) Plant Physiol , vol.99 , pp. 686-692
    • Li, H.1    Roux, S.J.2
  • 25
    • 0019801350 scopus 로고
    • Localization of phosphoprotein C23 to nucleolar structures and to the nucleolus organizer regions
    • Lischwe MA, Richards RL, Busch RK, Busch H (1981) Localization of phosphoprotein C23 to nucleolar structures and to the nucleolus organizer regions. Exp Cell Res 136: 101-109
    • (1981) Exp Cell Res , vol.136 , pp. 101-109
    • Lischwe, M.A.1    Richards, R.L.2    Busch, R.K.3    Busch, H.4
  • 26
    • 0017722842 scopus 로고
    • Bismuth staining for light and electron microscopy
    • Locke M, Huie P (1977) Bismuth staining for light and electron microscopy. Tissue & Cell 9: 347-371
    • (1977) Tissue & Cell , vol.9 , pp. 347-371
    • Locke, M.1    Huie, P.2
  • 27
    • 0025253546 scopus 로고
    • CDNA sequences of chicken nucleolin/C23 and NO38/B23, two major nucleolar proteins
    • Maridor G, Nigg EA (1990) cDNA sequences of chicken nucleolin/C23 and NO38/B23, two major nucleolar proteins. Nucleic Acids Res 18: 1286
    • (1990) Nucleic Acids Res , vol.18 , pp. 1286
    • Maridor, G.1    Nigg, E.A.2
  • 28
    • 0019971808 scopus 로고
    • Separation of guinea pig IgG subclasses by affinity chromatography on protein A-sepharose
    • Martin LN (1982) Separation of guinea pig IgG subclasses by affinity chromatography on protein A-sepharose. J Immunol Methods 52: 205-212
    • (1982) J Immunol Methods , vol.52 , pp. 205-212
    • Martin, L.N.1
  • 30
    • 0026773097 scopus 로고
    • Nopp140 shuttles on tracks between nucleolus and cytoplasm
    • Meier UT, Blobel G (1992) Nopp140 shuttles on tracks between nucleolus and cytoplasm. Cell 70: 127-138
    • (1992) Cell , vol.70 , pp. 127-138
    • Meier, U.T.1    Blobel, G.2
  • 31
    • 0030020912 scopus 로고    scopus 로고
    • In situ localization of nucieolin in the plant nucleolar matrix
    • Minguez A, Moreno Diaz de la Espina S (1996) In situ localization of nucieolin in the plant nucleolar matrix. Exp Cell Res 222: 171-178
    • (1996) Exp Cell Res , vol.222 , pp. 171-178
    • Minguez, A.1    De la Moreno Diaz Espina, S.2
  • 32
    • 0019321718 scopus 로고
    • Rapid isolation of high molecular weight plant DNA
    • Murray MG, Thompson WF (1980) Rapid isolation of high molecular weight plant DNA. Nucleic Acids Res 8: 4321-4325
    • (1980) Nucleic Acids Res , vol.8 , pp. 4321-4325
    • Murray, M.G.1    Thompson, W.F.2
  • 33
    • 0000204855 scopus 로고
    • The role of proteins in nucleolar structure and function
    • PR Strauss, SH Wilson, eds. Telford Press, Caldwell, NJ
    • Olson MOJ (1990) The role of proteins in nucleolar structure and function. In PR Strauss, SH Wilson, eds, The Eukaryotic Nucleus, Vol 2. Telford Press, Caldwell, NJ, pp 519-559
    • (1990) Eukaryotic Nucleus , vol.2 , pp. 519-559
    • Moj, O.1
  • 34
    • 0025265082 scopus 로고
    • Identification of major nucleolar proteins as candidate mitotic substrates of cdc2 kinase
    • Peter M, Kakagawa J, Doree M, Labbe JC, Nigg EA (1990) Identification of major nucleolar proteins as candidate mitotic substrates of cdc2 kinase. Cell 60: 791-801
    • (1990) Cell , vol.60 , pp. 791-801
    • Peter, M.1    Kakagawa, J.2    Doree, M.3    Labbe, J.C.4    Nigg, E.A.5
  • 38
    • 0027299218 scopus 로고
    • Structure, function and assembly of the nucleolus
    • Scheer U, Thiry M, Goessens G (1993) Structure, function and assembly of the nucleolus. Trends Cell Biol 3: 236-241
    • (1993) Trends Cell Biol , vol.3 , pp. 236-241
    • Scheer, U.1    Thiry, M.2    Goessens, G.3
  • 39
    • 0002475987 scopus 로고
    • A simple and efficient method for amplification of cDNA ends using 5′ RACE
    • Schuster DM, Buchman GW, Rashtchian A (1992) A simple and efficient method for amplification of cDNA ends using 5′ RACE. Focus 14: 46-52
    • (1992) Focus , vol.14 , pp. 46-52
    • Schuster, D.M.1    Buchman, G.W.2    Rashtchian, A.3
  • 40
    • 0025123543 scopus 로고
    • A protein partially expressed on the surface of HepG2 cells that binds lipoproteins specifically is nucleolin
    • Scmenkovich CF, Ostlund RE, Olson MOJ, Yang JW (1990) A protein partially expressed on the surface of HepG2 cells that binds lipoproteins specifically is nucleolin. Biochemistry 29: 9708-9713
    • (1990) Biochemistry , vol.29 , pp. 9708-9713
    • Scmenkovich, C.F.1    Ostlund, R.E.2    Olson, M.O.J.3    Yang, J.W.4
  • 42
    • 0022391350 scopus 로고
    • Effects of androgen and polyamines on the phosphorylation of nucleolar proteins from rat ventral prostates with particular reference to 110-kDa phosphoprotein
    • Suzuki N, Matsui H, Hosoya T (1985) Effects of androgen and polyamines on the phosphorylation of nucleolar proteins from rat ventral prostates with particular reference to 110-kDa phosphoprotein. J Biol Chem 260: 8050-8085
    • (1985) J Biol Chem , vol.260 , pp. 8050-8085
    • Suzuki, N.1    Matsui, H.2    Hosoya, T.3
  • 43
    • 3543012782 scopus 로고
    • Control by phytochrome of cytoplas- Mic and plastid rRNA accumulation in cotyledons of mustard seedlings in the absence of photosynthesis
    • Thien W, Schopfer P (1975) Control by phytochrome of cytoplas- mic and plastid rRNA accumulation in cotyledons of mustard seedlings in the absence of photosynthesis. Plant Physiol 56: 660-664
    • (1975) Plant Physiol , vol.56 , pp. 660-664
    • Thien, W.1    Schopfer, P.2
  • 44
    • 3543015182 scopus 로고
    • Control by phytochrome of cytoplasmic precursor rRNA synthesis in the cotyledons of mustard seedlings
    • Thien W, Schopfer P (1982) Control by phytochrome of cytoplasmic precursor rRNA synthesis in the cotyledons of mustard seedlings. Plant Physiol 69: 1156-1160
    • (1982) Plant Physiol , vol.69 , pp. 1156-1160
    • Thien, W.1    Schopfer, P.2
  • 45
    • 0344376914 scopus 로고
    • Far red reversal of internode-stimulating effect of red light on peas
    • Thompson BF (1959) Far red reversal of internode-stimulating effect of red light on peas. Am J Bot 48: 256-261
    • (1959) Am J Bot , vol.48 , pp. 256-261
    • Thompson, B.F.1
  • 46
    • 0028798912 scopus 로고
    • Specific aspartic acid-rich sequences are responsible for silver staining of nucleolar proteins
    • Valdez BC, Hennig D, Le TV, Busch H (1995) Specific aspartic acid-rich sequences are responsible for silver staining of nucleolar proteins. Biochem Biophys Res Commun 207: 485-491
    • (1995) Biochem Biophys Res Commun , vol.207 , pp. 485-491
    • Valdez, B.C.1    Hennig, D.2    Le, T.V.3    Busch, H.4
  • 47
    • 0024043307 scopus 로고
    • A procedure for the small-scale isolation of plant RNA blot analysis
    • Wadsworth GJ, Redinbaugh MG, Scandalios LG (1988) A procedure for the small-scale isolation of plant RNA blot analysis. Anal Biochem 172: 279-283
    • (1988) Anal Biochem , vol.172 , pp. 279-283
    • Wadsworth, G.J.1    Redinbaugh, M.G.2    Scandalios, L.G.3
  • 48
    • 0025748010 scopus 로고
    • Phosphorylation and proteolytic degradation of nucleolin from 3T3-F442A cells
    • Warrener P, Petryshyn R (1991) Phosphorylation and proteolytic degradation of nucleolin from 3T3-F442A cells. Biochem Biophys Res Commun 180: 716-723
    • (1991) Biochem Biophys Res Commun , vol.180 , pp. 716-723
    • Warrener, P.1    Petryshyn, R.2
  • 49
    • 0028109602 scopus 로고
    • Nucleolar proteins that bind NLSs: A role in nuclear import or ribosome biogenesis?
    • Xue Z, Melese T (1994) Nucleolar proteins that bind NLSs: a role in nuclear import or ribosome biogenesis? Trends Cell Biol 4: 414-417
    • (1994) Trends Cell Biol , vol.4 , pp. 414-417
    • Xue, Z.1    Melese, T.2
  • 50
    • 0027358668 scopus 로고
    • The amino terminus of mammalian nucleolin specifically recognizes SV40 T-antigen type nuclear localization sequences
    • Xue Z, Shan X, tapeyre B, Melese T (1993) The amino terminus of mammalian nucleolin specifically recognizes SV40 T-antigen type nuclear localization sequences. Eur J Cell Biol 62: 13-21
    • (1993) Eur J Cell Biol , vol.62 , pp. 13-21
    • Xue, Z.1    Shan, X.2    Tapeyre, B.3    Melese, T.4
  • 51
    • 0027380639 scopus 로고
    • Multiple regions of NSR1 are for accumulation of a fusion protein within the nucleolus
    • Van C, Melese T (1993) Multiple regions of NSR1 are for accumulation of a fusion protein within the nucleolus. J Cell Biol 123: 1081-1091
    • (1993) J Cell Biol , vol.123 , pp. 1081-1091
    • Van, C.1    Melese, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.