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Volumn 90, Issue 2, 2003, Pages 361-378

A proteomic study of the Arabidopsis nuclear matrix

Author keywords

Arabidopsis; Mass spectrometry; Nuclear matrix; Nucleolus; Proteomics

Indexed keywords

DNA; FIBRILLARIN; HISTONE DEACETYLASE; NUCLEOLIN; NUCLEOPROTEIN; RNA;

EID: 0141529726     PISSN: 07302312     EISSN: None     Source Type: Journal    
DOI: 10.1002/jcb.10624     Document Type: Article
Times cited : (79)

References (67)
  • 3
    • 0034282647 scopus 로고    scopus 로고
    • Fibrillarin genes encode both a conserved nucleolar protein and a novel small nucleolar RNA involved in ribosomal RNA methylation in Arabidopsis thaliana
    • Barneche F, Steinmetz F, Echeverria M. 2000. Fibrillarin genes encode both a conserved nucleolar protein and a novel small nucleolar RNA involved in ribosomal RNA methylation in Arabidopsis thaliana. J Biol Chem 275: 27212-27220.
    • (2000) J Biol Chem , vol.275 , pp. 27212-27220
    • Barneche, F.1    Steinmetz, F.2    Echeverria, M.3
  • 4
    • 0026071401 scopus 로고
    • A comprehensive study on the isolation and characterization of the HeLa S3 nuclear matrix
    • Belgrader P, Siegel AJ, Berezney R. 1991. A comprehensive study on the isolation and characterization of the HeLa S3 nuclear matrix. J Cell Sci 98:281-291.
    • (1991) J Cell Sci , vol.98 , pp. 281-291
    • Belgrader, P.1    Siegel, A.J.2    Berezney, R.3
  • 5
    • 0001532085 scopus 로고
    • Organization and functions of the nuclear matrix
    • Hnilica LS, editor. Boca Raton, FL: CRC Press
    • Berezney R. 1984. Organization and functions of the nuclear matrix. In: Hnilica LS, editor. Chromosomal nonhistone proteins. Vol. IV. Boca Raton, FL: CRC Press. pp 119-180.
    • (1984) Chromosomal Nonhistone Proteins , vol.4 , pp. 119-180
    • Berezney, R.1
  • 7
    • 0017687532 scopus 로고
    • Nuclear matrix. Isolation and characterization of a framework structure from rat liver nuclei
    • Berezney R, Coffey DS. 1977. Nuclear matrix. Isolation and characterization of a framework structure from rat liver nuclei. J Cell Biol 73:616-637.
    • (1977) J Cell Biol , vol.73 , pp. 616-637
    • Berezney, R.1    Coffey, D.S.2
  • 9
    • 0036122494 scopus 로고    scopus 로고
    • Functional divergence between histone deacetylases in fission yeast by distinct cellular localization and in vivo specificity
    • Bjerling P, Silverstein RA, Thon G, Caudy A, Grewal S, Ekwall K. 2002. Functional divergence between histone deacetylases in fission yeast by distinct cellular localization and in vivo specificity. Mol Cell Biol 22:2170-2181.
    • (2002) Mol Cell Biol , vol.22 , pp. 2170-2181
    • Bjerling, P.1    Silverstein, R.A.2    Thon, G.3    Caudy, A.4    Grewal, S.5    Ekwall, K.6
  • 10
    • 0020420866 scopus 로고
    • Fine structure and localization of the nuclear matrix in situ
    • Brasch K. 1982. Fine structure and localization of the nuclear matrix in situ. Exp Cell Res 140:161-171.
    • (1982) Exp Cell Res , vol.140 , pp. 161-171
    • Brasch, K.1
  • 11
    • 0036781068 scopus 로고    scopus 로고
    • Ribosome components are associated with sites of transcription
    • Brogna S, Sato TA, Rosbash M. 2002. Ribosome components are associated with sites of transcription. Mol Cell 10:93-104.
    • (2002) Mol Cell , vol.10 , pp. 93-104
    • Brogna, S.1    Sato, T.A.2    Rosbash, M.3
  • 12
    • 0037264089 scopus 로고    scopus 로고
    • Plant snoRNAs: Functional evolution and new modes of gene expression
    • Brown JW, Echeverria M, Qu LH. 2003. Plant snoRNAs: Functional evolution and new modes of gene expression. Trends Plant Sci 8:42-49.
    • (2003) Trends Plant Sci , vol.8 , pp. 42-49
    • Brown, J.W.1    Echeverria, M.2    Qu, L.H.3
  • 13
    • 0035795422 scopus 로고    scopus 로고
    • Nucleolar components involved in ribosome biogenesis cycle between the nucleolus and nucleoplasm in interphase cells
    • Chen D, Huang S. 2001. Nucleolar components involved in ribosome biogenesis cycle between the nucleolus and nucleoplasm in interphase cells. J Cell Biol 153:169-176.
    • (2001) J Cell Biol , vol.153 , pp. 169-176
    • Chen, D.1    Huang, S.2
  • 14
    • 0033499709 scopus 로고    scopus 로고
    • Human Nopp140, which interacts with RNA polymerase I: Implications for rRNA gene transcription and nucleolar structural organization
    • Chen HK, Pai CY, Huang JY, Yeh NH. 1999. Human Nopp140, which interacts with RNA polymerase I: Implications for rRNA gene transcription and nucleolar structural organization. Mol Cell Biol 19:8536-8546.
    • (1999) Mol Cell Biol , vol.19 , pp. 8536-8546
    • Chen, H.K.1    Pai, C.Y.2    Huang, J.Y.3    Yeh, N.H.4
  • 15
    • 0035984183 scopus 로고    scopus 로고
    • The DNA-compacting protein DCP68 from soybean chloroplasts is ferrodoxin:sulfite reductase and co-localizes with the organellar nucleoid
    • Chi-Ham CL, Keaton MA, Cannon GC, And Heinhorst S. 2002. The DNA-compacting protein DCP68 from soybean chloroplasts is ferrodoxin:sulfite reductase and co-localizes with the organellar nucleoid. Plant Mol Biol 49: 621-631.
    • (2002) Plant Mol Biol , vol.49 , pp. 621-631
    • Chi-Ham, C.L.1    Keaton, M.A.2    Cannon, G.C.3    And Heinhorst, S.4
  • 16
    • 0034331073 scopus 로고    scopus 로고
    • Finding nuclear localization signals
    • Cokol M, Nair R, Rost B. 2000. Finding nuclear localization signals. EMBO Rep 1:411-415.
    • (2000) EMBO Rep , vol.1 , pp. 411-415
    • Cokol, M.1    Nair, R.2    Rost, B.3
  • 17
    • 0029848521 scopus 로고    scopus 로고
    • Histone modifications, chromatin structure, and the nuclear matrix
    • Davie JR. 1996. Histone modifications, chromatin structure, and the nuclear matrix. J Cell Biochem 62:149-157.
    • (1996) J Cell Biochem , vol.62 , pp. 149-157
    • Davie, J.R.1
  • 18
    • 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
  • 19
    • 0035834037 scopus 로고    scopus 로고
    • Nuclear envelope proteomics: Novel integral membrane proteins of the inner nuclear membrane
    • Dreger M, Bengtsson L, Schoneberg T, Otto H, Hucho F. 2001. Nuclear envelope proteomics: Novel integral membrane proteins of the inner nuclear membrane. Proc Natl Acad Sci USA 98:11943-11948.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11943-11948
    • Dreger, M.1    Bengtsson, L.2    Schoneberg, T.3    Otto, H.4    Hucho, F.5
  • 22
    • 0036591884 scopus 로고    scopus 로고
    • Biogenesis of small nucleolar ribonucleoproteins
    • Filipowicz W, Pogacic V. 2000. Biogenesis of small nucleolar ribonucleoproteins. Curr Opin Cell Biol 14:319-327.
    • (2000) Curr Opin Cell Biol , vol.14 , pp. 319-327
    • Filipowicz, W.1    Pogacic, V.2
  • 23
    • 0032401696 scopus 로고    scopus 로고
    • Similarity between nuclear matrix proteins of various cells revealed by an improved isolation method
    • Gerner C, Holzmann K, Grimm R, Sauermann G. 1998. Similarity between nuclear matrix proteins of various cells revealed by an improved isolation method. J Cell Biochem 71:363-374.
    • (1998) J Cell Biochem , vol.71 , pp. 363-374
    • Gerner, C.1    Holzmann, K.2    Grimm, R.3    Sauermann, G.4
  • 26
    • 0033150016 scopus 로고    scopus 로고
    • Matrix attachment region binding protein MFP1 is located in discrete domains at the nuclear envelope
    • Gindullis F, Meier I. 1999. Matrix attachment region binding protein MFP1 is located in discrete domains at the nuclear envelope. Plant Cell 11:1117-1128.
    • (1999) Plant Cell , vol.11 , pp. 1117-1128
    • Gindullis, F.1    Meier, I.2
  • 27
    • 0032473356 scopus 로고    scopus 로고
    • Nucleolin functions in the first step of ribosomal RNA processing
    • Ginisty H, Amalric F, Bouvet P. 1998. Nucleolin functions in the first step of ribosomal RNA processing. EMBO J 17:1476-1486.
    • (1998) EMBO J , vol.17 , pp. 1476-1486
    • Ginisty, H.1    Amalric, F.2    Bouvet, P.3
  • 30
    • 0033930577 scopus 로고    scopus 로고
    • A new look at the nuclear matrix
    • Hancock R. 2000. A new look at the nuclear matrix. Chromosoma 109:219-225.
    • (2000) Chromosoma , vol.109 , pp. 219-225
    • Hancock, R.1
  • 31
    • 0033136650 scopus 로고    scopus 로고
    • Two MAR DNA-binding proteins of the pea nuclear matrix identify a new class of DNA-binding proteins
    • Hatton D, Gray JC. 1999. Two MAR DNA-binding proteins of the pea nuclear matrix identify a new class of DNA-binding proteins. Plant J 18:417-429.
    • (1999) Plant J , vol.18 , pp. 417-429
    • Hatton, D.1    Gray, J.C.2
  • 34
    • 0035839002 scopus 로고    scopus 로고
    • Coupled transcription and translation within nuclei of mammalian cells
    • Iborra FJ, Jackson DA, Cook PR. 2001. Coupled transcription and translation within nuclei of mammalian cells. Science 293:1139-1142.
    • (2001) Science , vol.293 , pp. 1139-1142
    • Iborra, F.J.1    Jackson, D.A.2    Cook, P.R.3
  • 37
    • 0030771898 scopus 로고    scopus 로고
    • Identification of maize histone deacetylase HD2 as an acidic nucleolar phosphoprotein
    • Lusser A, Brosch G, Loidl A, Haas H, Loidl P. 1997. Identification of maize histone deacetylase HD2 as an acidic nucleolar phosphoprotein. Science 277:88-91.
    • (1997) Science , vol.277 , pp. 88-91
    • Lusser, A.1    Brosch, G.2    Loidl, A.3    Haas, H.4    Loidl, P.5
  • 38
    • 0019132556 scopus 로고
    • Human-specific nuclear protein that associates with the polar region of the mitotic apparatus: Distribution in a human/hamster hybrid cells
    • Lydersen BK, Petijohn DE. 1980. Human-specific nuclear protein that associates with the polar region of the mitotic apparatus: Distribution in a human/hamster hybrid cells. Cell 22:489-499.
    • (1980) Cell , vol.22 , pp. 489-499
    • Lydersen, B.K.1    Petijohn, D.E.2
  • 39
    • 0029024197 scopus 로고
    • The protein composition of Friend cell nuclear matrix stabilized by various treatments. Different recovery of nucleolar proteins B23 and C23 and nuclear lamins
    • Martelli AM, Manzoli L, Rubbini S, Billi AM, Bareggi R, Cocco L. 1995. The protein composition of Friend cell nuclear matrix stabilized by various treatments. Different recovery of nucleolar proteins B23 and C23 and nuclear lamins. Biol Cell 83:15-22.
    • (1995) Biol Cell , vol.83 , pp. 15-22
    • Martelli, A.M.1    Manzoli, L.2    Rubbini, S.3    Billi, A.M.4    Bareggi, R.5    Cocco, L.6
  • 42
    • 0030020912 scopus 로고    scopus 로고
    • In situ localization of nucleolin in the plant nucleolar matrix
    • Minguez A, Moreno Diaz de la Espina S. 1996. In situ localization of nucleolin in the plant nucleolar matrix. Exp Cell Res 222:171-178.
    • (1996) Exp Cell Res , vol.222 , pp. 171-178
    • Minguez, A.1    Moreno Diaz de la Espina, S.2
  • 43
    • 0021675784 scopus 로고
    • Organization of the higher-order chromatin loop: Specific DNA attachment sites on nuclear scaffold
    • Mirkovitch J, Mirault ME, Laemmli UK. 1984. Organization of the higher-order chromatin loop: Specific DNA attachment sites on nuclear scaffold. Cell 39:223-232.
    • (1984) Cell , vol.39 , pp. 223-232
    • Mirkovitch, J.1    Mirault, M.E.2    Laemmli, U.K.3
  • 44
    • 0027105007 scopus 로고
    • A knowledge base for predicting protein localization sites in eukaryotic cells
    • Nakai K, Kanehisa M. 1992. A knowledge base for predicting protein localization sites in eukaryotic cells. Genomics 14:897-911.
    • (1992) Genomics , vol.14 , pp. 897-911
    • Nakai, K.1    Kanehisa, M.2
  • 45
    • 0035110880 scopus 로고    scopus 로고
    • Experimental observations of a nuclear matrix
    • Nickerson JA. 2001. Experimental observations of a nuclear matrix. J Cell Sci 114:463-474.
    • (2001) J Cell Sci , vol.114 , pp. 463-474
    • Nickerson, J.A.1
  • 46
    • 0025261920 scopus 로고
    • Immunolocalization in three dimensions: Immunogold staining of cytoskeletal and nuclear matrix proteins in resinless electron microscopy sections
    • Nickerson JA, Krockmalnic G, He DC, Penman S. 1990. Immunolocalization in three dimensions: Immunogold staining of cytoskeletal and nuclear matrix proteins in resinless electron microscopy sections. Proc Natl Acad Sci USA 87:2259-2263.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 2259-2263
    • Nickerson, J.A.1    Krockmalnic, G.2    He, D.C.3    Penman, S.4
  • 47
    • 0030956629 scopus 로고    scopus 로고
    • The nuclear matrix revealed by eluting chromatin from a cross-linked nucleus
    • Nickerson JA, Krockmalnic G, Wan KM, Penman S. 1997. The nuclear matrix revealed by eluting chromatin from a cross-linked nucleus. Proc Natl Acad Sci USA 94:4446-4450.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4446-4450
    • Nickerson, J.A.1    Krockmalnic, G.2    Wan, K.M.3    Penman, S.4
  • 48
    • 0033534476 scopus 로고    scopus 로고
    • S-adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein argininemethyltransferase
    • Niewmierzycka A, Clarke S. 1999. S-adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein argininemethyltransferase. J Biol Chem 274:814-824.
    • (1999) J Biol Chem , vol.274 , pp. 814-824
    • Niewmierzycka, A.1    Clarke, S.2
  • 49
    • 0029050553 scopus 로고
    • Cell-cycle-dependent alterations of a highly phosphorylated nucleolar protein p130 are associated with nucleologenesis
    • Pai CY, Chen HK, Shen HL, Yeh NH. 1995. Cell-cycle-dependent alterations of a highly phosphorylated nucleolar protein p130 are associated with nucleologenesis. J Cell Sci 108:1911-1920.
    • (1995) J Cell Sci , vol.108 , pp. 1911-1920
    • Pai, C.Y.1    Chen, H.K.2    Shen, H.L.3    Yeh, N.H.4
  • 50
    • 0032571368 scopus 로고    scopus 로고
    • Thinking about a nuclear matrix
    • Pederson T. 1998. Thinking about a nuclear matrix. J Mol Biol 277:147-159.
    • (1998) J Mol Biol , vol.277 , pp. 147-159
    • Pederson, T.1
  • 51
    • 0034100040 scopus 로고    scopus 로고
    • Half a century of "the nuclear matrix"
    • Pederson T. 2000. Half a century of "the nuclear matrix." Mol Biol Cell 11:799-805.
    • (2000) Mol Biol Cell , vol.11 , pp. 799-805
    • Pederson, T.1
  • 52
    • 0029078045 scopus 로고
    • Rethinking cell structure
    • Penman S. 1995. Rethinking cell structure. Proc Natl Acad Sci USA 92:525-527.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 525-527
    • Penman, S.1
  • 54
    • 0021068615 scopus 로고
    • Localization of the 70,000 dalton heat-induced protein in the nuclear matrix of BHK cells
    • Pouchelet M, St-Pierre E, Bibor-Hardy V, Simard R. 1983. Localization of the 70,000 dalton heat-induced protein in the nuclear matrix of BHK cells. Exp Cell Res 149:451-459.
    • (1983) Exp Cell Res , vol.149 , pp. 451-459
    • Pouchelet, M.1    St.-Pierre, E.2    Bibor-Hardy, V.3    Simard, R.4
  • 55
    • 0037384776 scopus 로고    scopus 로고
    • A novel alpha-helical protein, specific to and highly conserved in plants, is associated with the nuclear matrix fraction
    • Rose A, Gindullis F, Meier I. 2003. A novel alpha-helical protein, specific to and highly conserved in plants, is associated with the nuclear matrix fraction. J Exp Botany 54:1-9.
    • (2003) J Exp Botany , vol.54 , pp. 1-9
    • Rose, A.1    Gindullis, F.2    Meier, I.3
  • 58
    • 0030021267 scopus 로고    scopus 로고
    • Nuclear matrix attachment regions and transgene expression in plants
    • Spiker S, Thompson WT. 1996. Nuclear matrix attachment regions and transgene expression in plants. Plant Physiol 110:15-21.
    • (1996) Plant Physiol , vol.110 , pp. 15-21
    • Spiker, S.1    Thompson, W.T.2
  • 59
    • 0021314916 scopus 로고
    • Methionine adenosyltransferase (S-adenosylmethionine synthase) and S-adenosylmethione decarboxylase
    • Tabor CW, Tabor H. 1984. Methionine adenosyltransferase (S-adenosylmethionine synthase) and S-adenosylmethione decarboxylase. Adv Enzymol 56:251-282.
    • (1984) Adv Enzymol , vol.56 , pp. 251-282
    • Tabor, C.W.1    Tabor, H.2
  • 60
    • 0034026335 scopus 로고    scopus 로고
    • Nuclear matrix-like filaments and fibrogranular complexes form through the rearrangement of specific nuclear ribonucleoproteins
    • Tan J-H, Wooley JC, LeSturgeon WM. 2000. Nuclear matrix-like filaments and fibrogranular complexes form through the rearrangement of specific nuclear ribonucleoproteins. Mol Biol Cell 11:1547-1554.
    • (2000) Mol Biol Cell , vol.11 , pp. 1547-1554
    • Tan, J.-H.1    Wooley, J.C.2    LeSturgeon, W.M.3
  • 62
    • 0033367325 scopus 로고    scopus 로고
    • Ribosome synthesis in Saccharomyces cerevisiae
    • Venema J, Tollervey D. 1999. Ribosome synthesis in Saccharomyces cerevisiae. Annu Rev Genet 33:261-311.
    • (1999) Annu Rev Genet , vol.33 , pp. 261-311
    • Venema, J.1    Tollervey, D.2
  • 63
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn MP, Wolters D, Yates JR III. 2001. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol 19:242-247.
    • (2001) Nat Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates J.R. III3
  • 65
    • 0035698491 scopus 로고    scopus 로고
    • Small heat shock protein p26 associates with nuclear lamins and HSP70 in nuclei and nuclear matrix fractions from stressed cells
    • Willsie JK, Clegg JS. 2002. Small heat shock protein p26 associates with nuclear lamins and HSP70 in nuclei and nuclear matrix fractions from stressed cells. J Cell Biochem 84:601-614.
    • (2002) J Cell Biochem , vol.84 , pp. 601-614
    • Willsie, J.K.1    Clegg, J.S.2
  • 66
    • 0344631628 scopus 로고    scopus 로고
    • The plant nucleoskeleton: Ultrastructural organization and identification of NuMA homologues in the nuclear matrix and mitotic spindle of plant cells
    • Yu W, Moreno Diaz de la Espina S. 1999. The plant nucleoskeleton: Ultrastructural organization and identification of NuMA homologues in the nuclear matrix and mitotic spindle of plant cells. Exp Cell Res 246:516-526.
    • (1999) Exp Cell Res , vol.246 , pp. 516-526
    • Yu, W.1    Moreno Diaz de la Espina, S.2
  • 67
    • 0035166448 scopus 로고    scopus 로고
    • Analysis of sequence-specific binding of RNA to Hsp70 and its various homologs indicates the involvement of N- and C-terminal interactions
    • Zimmer C, von Gabain A, Henics T. 2001. Analysis of sequence-specific binding of RNA to Hsp70 and its various homologs indicates the involvement of N- and C-terminal interactions. RNA 7:1628-1637.
    • (2001) RNA , vol.7 , pp. 1628-1637
    • Zimmer, C.1    Von Gabain, A.2    Henics, T.3


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