메뉴 건너뛰기




Volumn 225, Issue 3, 2007, Pages 625-639

Biochemical and cellular characterization of the plant ortholog of PYM, a protein that interacts with the exon junction complex core proteins Mago and Y14

Author keywords

Arabidopsis; Exon junction complex; Mago Y14; Nonsense mediated decay; Post transcriptional regulation; PYM

Indexed keywords

ARABIDOPSIS PROTEIN; DROSOPHILA PROTEIN; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; MAGO PROTEIN, DROSOPHILA; NUCLEAR PROTEIN; PYM PROTEIN, DROSOPHILA; RNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 33846820435     PISSN: 00320935     EISSN: 14322048     Source Type: Journal    
DOI: 10.1007/s00425-006-0385-y     Document Type: Article
Times cited : (28)

References (44)
  • 1
    • 3543032700 scopus 로고    scopus 로고
    • Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex
    • Bono F, Ebert J, Unterholzner L, Guttler T, Izaurralde E, Conti E (2004) Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex. EMBO Rep 5:304-310
    • (2004) EMBO Rep , vol.5 , pp. 304-310
    • Bono, F.1    Ebert, J.2    Unterholzner, L.3    Guttler, T.4    Izaurralde, E.5    Conti, E.6
  • 2
    • 0025784620 scopus 로고
    • Mutations in a newly identified Drosophila melanogaster gene, mago nashi, disrupt germ cell formation and result in the formation of mirror-image symmetrical double abdomen embryos
    • Boswell RE, Prout ME, Steichen JC (1991) Mutations in a newly identified Drosophila melanogaster gene, mago nashi, disrupt germ cell formation and result in the formation of mirror-image symmetrical double abdomen embryos. Development 113:373-384
    • (1991) Development , vol.113 , pp. 373-384
    • Boswell, R.E.1    Prout, M.E.2    Steichen, J.C.3
  • 3
    • 28344453630 scopus 로고    scopus 로고
    • The peroxisomal multifunctional protein interacts with cortical microtubules in plant cells
    • Chuong SD, Mullen RT, Muench DG (2005) The peroxisomal multifunctional protein interacts with cortical microtubules in plant cells. BMC Cell Biol 6:40
    • (2005) BMC Cell Biol , vol.6 , pp. 40
    • Chuong, S.D.1    Mullen, R.T.2    Muench, D.G.3
  • 4
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough S, Bent A (1998) Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J 16:735-743
    • (1998) Plant J , vol.16 , pp. 735-743
    • Clough, S.1    Bent, A.2
  • 5
    • 19344374029 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay: Molecular insights and mechanistic variations across species
    • Conti E, Izaurralde E (2005) Nonsense-mediated mRNA decay: molecular insights and mechanistic variations across species. Curr Opin Cell Biol 17:316-325
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 316-325
    • Conti, E.1    Izaurralde, E.2
  • 6
    • 0028485367 scopus 로고
    • Light modulation of ferredoxin mRNA abundance requires an open reading frame
    • Dickey LF, Nguyen TT, Allen GC, Thompson WF (1994) Light modulation of ferredoxin mRNA abundance requires an open reading frame. Plant Cell 6:1171-1176
    • (1994) Plant Cell , vol.6 , pp. 1171-1176
    • Dickey, L.F.1    Nguyen, T.T.2    Allen, G.C.3    Thompson, W.F.4
  • 7
    • 0036512117 scopus 로고    scopus 로고
    • Messenger-RNA-binding proteins and the messages they carry
    • Dreyfuss G, Kim VN, Kataoka N (2002) Messenger-RNA-binding proteins and the messages they carry. Nat Rev Mol Cell Biol 3:195-205
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 195-205
    • Dreyfuss, G.1    Kim, V.N.2    Kataoka, N.3
  • 8
    • 0037227959 scopus 로고    scopus 로고
    • An efficient protein complex purification method for functional proteomics in higher eukaryotes
    • Forler D, Kocher T, Rode M, Gentzel M, Izaurralde E, Wilm M (2003) An efficient protein complex purification method for functional proteomics in higher eukaryotes. Nat Biotechnol 21:89-92
    • (2003) Nat Biotechnol , vol.21 , pp. 89-92
    • Forler, D.1    Kocher, T.2    Rode, M.3    Gentzel, M.4    Izaurralde, E.5    Wilm, M.6
  • 9
    • 0037766047 scopus 로고    scopus 로고
    • A novel mode of RBD-protein recognition in the Y14-Mago complex
    • Fribourg S, Gatfield D, Izaurralde E, Conti E (2003) A novel mode of RBD-protein recognition in the Y14-Mago complex. Nat Struct Biol 10:433-439
    • (2003) Nat Struct Biol , vol.10 , pp. 433-439
    • Fribourg, S.1    Gatfield, D.2    Izaurralde, E.3    Conti, E.4
  • 10
    • 25844512736 scopus 로고    scopus 로고
    • Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements
    • Gehring NH, Kunz JB, Neu-Yilik G, Breit S, Viegas MH, Hentze MW, Kulozik AE (2005) Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements. Mol Cell 20:65-75
    • (2005) Mol Cell , vol.20 , pp. 65-75
    • Gehring, N.H.1    Kunz, J.B.2    Neu-Yilik, G.3    Breit, S.4    Viegas, M.H.5    Hentze, M.W.6    Kulozik, A.E.7
  • 11
    • 0035787713 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay in Saccharomyces cerevisiae: A quality control mechanism that degrades transcripts harboring premature termination codons
    • Gonzalez CI, Wang W, Peltz SW (2001) Nonsense-mediated mRNA decay in Saccharomyces cerevisiae: a quality control mechanism that degrades transcripts harboring premature termination codons. Cold Spring Harb Symp Quant Biol 66:321-328
    • (2001) Cold Spring Harb Symp Quant Biol , vol.66 , pp. 321-328
    • Gonzalez, C.I.1    Wang, W.2    Peltz, S.W.3
  • 12
    • 0035975970 scopus 로고    scopus 로고
    • Drosophila Y14 shuttles to the posterior of the oocyte and is required for oskar mRNA transport
    • Hachet O, Ephrussi A (2001) Drosophila Y14 shuttles to the posterior of the oocyte and is required for oskar mRNA transport. Curr Biol 11:1666-1674
    • (2001) Curr Biol , vol.11 , pp. 1666-1674
    • Hachet, O.1    Ephrussi, A.2
  • 13
    • 2342439151 scopus 로고    scopus 로고
    • Splicing of oskar RNA in the nucleus is coupled to its cytoplasmic localization
    • Hachet O, Ephrussi A (2004) Splicing of oskar RNA in the nucleus is coupled to its cytoplasmic localization. Nature 428:959-963
    • (2004) Nature , vol.428 , pp. 959-963
    • Hachet, O.1    Ephrussi, A.2
  • 14
    • 0030238338 scopus 로고    scopus 로고
    • Premature nonsense codons decrease the stability of phytohemagglutinin mRNA in a position-dependent manner
    • van Hoof A, Green PJ (1996) Premature nonsense codons decrease the stability of phytohemagglutinin mRNA in a position-dependent manner. Plant J 10:415-424
    • (1996) Plant J , vol.10 , pp. 415-424
    • van Hoof, A.1    Green, P.J.2
  • 15
    • 0024655993 scopus 로고
    • A frameshift mutation prevents Kunitz trypsin inhibitor mRNA accumulation in soybean embryos
    • Jofuku KD, Schipper RD, Goldberg RB (1989) A frameshift mutation prevents Kunitz trypsin inhibitor mRNA accumulation in soybean embryos. Plant Cell 1:567
    • (1989) Plant Cell , vol.1 , pp. 567
    • Jofuku, K.D.1    Schipper, R.D.2    Goldberg, R.B.3
  • 17
    • 0033634824 scopus 로고    scopus 로고
    • Pre-mRNA splicing imprints mRNA in the nucleus with a novel RNA-binding protein that persists in the cytoplasm
    • Kataoka N, Yong J, Kim VN, Velazquez F, Perkinson RA, Wang F, Dreyfuss G (2000) Pre-mRNA splicing imprints mRNA in the nucleus with a novel RNA-binding protein that persists in the cytoplasm. Mol Cell 6:673-682
    • (2000) Mol Cell , vol.6 , pp. 673-682
    • Kataoka, N.1    Yong, J.2    Kim, V.N.3    Velazquez, F.4    Perkinson, R.A.5    Wang, F.6    Dreyfuss, G.7
  • 18
    • 0037850982 scopus 로고    scopus 로고
    • Structure of the Y14-Magoh core of the exon junction complex
    • Lau CK, Diem MD, Dreyfuss G, Van Duyne GD (2003) Structure of the Y14-Magoh core of the exon junction complex. Curr Biol 13:933-941
    • (2003) Curr Biol , vol.13 , pp. 933-941
    • Lau, C.K.1    Diem, M.D.2    Dreyfuss, G.3    Van Duyne, G.D.4
  • 19
    • 0034672093 scopus 로고    scopus 로고
    • The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions
    • Le Hir H, Izaurralde E, Maquat LE, Moore MJ (2000a) The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions. Embo J 19:6860-6869
    • (2000) Embo J , vol.19 , pp. 6860-6869
    • Le Hir, H.1    Izaurralde, E.2    Maquat, L.E.3    Moore, M.J.4
  • 20
    • 0034193569 scopus 로고    scopus 로고
    • Pre-mRNA splicing alters mRNP composition: Evidence for stable association of proteins at exon-exon junctions
    • Le Hir H, Moore MJ, Maquat LE (2000b) Pre-mRNA splicing alters mRNP composition: evidence for stable association of proteins at exon-exon junctions. Genes Dev 14:1098-1108
    • (2000) Genes Dev , vol.14 , pp. 1098-1108
    • Le Hir, H.1    Moore, M.J.2    Maquat, L.E.3
  • 21
    • 19344366251 scopus 로고    scopus 로고
    • Mechanistic links between nonsense-mediated mRNA decay and pre-mRNA splicing in mammalian cells
    • Lejeune F, Maquat LE (2005) Mechanistic links between nonsense-mediated mRNA decay and pre-mRNA splicing in mammalian cells. Curr Opin Cell Biol 17:309-315
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 309-315
    • Lejeune, F.1    Maquat, L.E.2
  • 22
    • 3042803315 scopus 로고    scopus 로고
    • Use of fluorescent protein tags to study nuclear organization of the spliceosomal machinery in transiently transformed living plant cells
    • Lorkovic ZJ, Hilscher J, Barta A (2004) Use of fluorescent protein tags to study nuclear organization of the spliceosomal machinery in transiently transformed living plant cells. Mol Biol Cell 15:3233-3243
    • (2004) Mol Biol Cell , vol.15 , pp. 3233-3243
    • Lorkovic, Z.J.1    Hilscher, J.2    Barta, A.3
  • 23
    • 9444282150 scopus 로고    scopus 로고
    • Compartmentalization of the splicing machinery in plant cell nuclei
    • Lorkovic ZJ, Barta A (2004) Compartmentalization of the splicing machinery in plant cell nuclei. Trends Plant Sci 9:565-568
    • (2004) Trends Plant Sci , vol.9 , pp. 565-568
    • Lorkovic, Z.J.1    Barta, A.2
  • 24
    • 33644816419 scopus 로고    scopus 로고
    • Localization of the tomato bushy stunt virus replication protein p33 reveals a peroxisome-to-endoplasmic reticulum sorting pathway
    • McCartney AW, Greenwood JS, Fabian MR, White KA, Mullen RT (2005) Localization of the tomato bushy stunt virus replication protein p33 reveals a peroxisome-to-endoplasmic reticulum sorting pathway. Plant Cell 17:3513-3531
    • (2005) Plant Cell , vol.17 , pp. 3513-3531
    • McCartney, A.W.1    Greenwood, J.S.2    Fabian, M.R.3    White, K.A.4    Mullen, R.T.5
  • 25
    • 0035498967 scopus 로고    scopus 로고
    • The RNA-binding protein Tsunagi interacts with Mago nashi to establish polarity and localize oskar mRNA during Drosophila oogenesis
    • Mohr SE, Dillon ST, Boswell RE (2001) The RNA-binding protein Tsunagi interacts with Mago nashi to establish polarity and localize oskar mRNA during Drosophila oogenesis. Genes Dev 15:2886-2899
    • (2001) Genes Dev , vol.15 , pp. 2886-2899
    • Mohr, S.E.1    Dillon, S.T.2    Boswell, R.E.3
  • 26
    • 33748204183 scopus 로고    scopus 로고
    • Messages on the move: The role of the cytoskeleton in mRNA localization and translation in plant cells
    • Muench DG, Park NI (2006) Messages on the move: the role of the cytoskeleton in mRNA localization and translation in plant cells. Can J Bot 84:572-580
    • (2006) Can J Bot , vol.84 , pp. 572-580
    • Muench, D.G.1    Park, N.I.2
  • 27
    • 0028354293 scopus 로고
    • The mago nashi locus encodes an essential product required for germ plasm assembly in Drosophila
    • Newmark PA, Boswell RE (1994) The mago nashi locus encodes an essential product required for germ plasm assembly in Drosophila. Development 120:1303-1313
    • (1994) Development , vol.120 , pp. 1303-1313
    • Newmark, P.A.1    Boswell, R.E.2
  • 28
    • 0942268832 scopus 로고    scopus 로고
    • Splicing enhances translation in mammalian cells: An additional function of the exon junction complex
    • Nott A, Le Hir H, Moore MJ (2004) Splicing enhances translation in mammalian cells: an additional function of the exon junction complex. Genes Dev 18:210-222
    • (2004) Genes Dev , vol.18 , pp. 210-222
    • Nott, A.1    Le Hir, H.2    Moore, M.J.3
  • 29
    • 0037154982 scopus 로고    scopus 로고
    • A unified theory of gene expression
    • Orphanides G, Reinberg D (2002) A unified theory of gene expression. Cell 108:439-451
    • (2002) Cell , vol.108 , pp. 439-451
    • Orphanides, G.1    Reinberg, D.2
  • 30
    • 1442354190 scopus 로고    scopus 로고
    • An eIF4AIII-containing complex required for mRNA localization and nonsense-mediated mRNA decay
    • Palacios IM, Gatfield D, St Johnston D, Izaurralde E (2004) An eIF4AIII-containing complex required for mRNA localization and nonsense-mediated mRNA decay. Nature 427:753-757
    • (2004) Nature , vol.427 , pp. 753-757
    • Palacios, I.M.1    Gatfield, D.2    St Johnston, D.3    Izaurralde, E.4
  • 32
    • 0033996462 scopus 로고    scopus 로고
    • Premature termination codons destabilize ferredoxin-1 mRNA when ferredoxin-1 is translated
    • Petracek ME, Nuygen T, Thompson WF, Dickey LF (2000) Premature termination codons destabilize ferredoxin-1 mRNA when ferredoxin-1 is translated. Plant J 21:563-569
    • (2000) Plant J , vol.21 , pp. 563-569
    • Petracek, M.E.1    Nuygen, T.2    Thompson, W.F.3    Dickey, L.F.4
  • 33
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut G, Shevchenko A, Rutz B, Wilm M, Mann M, Seraphin B (1999) A generic protein purification method for protein complex characterization and proteome exploration. Nat Biotechnol 17:1030-1032
    • (1999) Nat Biotechnol , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6
  • 34
    • 1842430185 scopus 로고    scopus 로고
    • Improved tandem affinity purification tag and methods for isolation of protein heterocomplexes from plants
    • Rohila JS, Chen M, Cerny R, Fromm ME (2004) Improved tandem affinity purification tag and methods for isolation of protein heterocomplexes from plants. Plant J 38:172-181
    • (2004) Plant J , vol.38 , pp. 172-181
    • Rohila, J.S.1    Chen, M.2    Cerny, R.3    Fromm, M.E.4
  • 35
    • 0033063596 scopus 로고    scopus 로고
    • Model system for plant cell biology: GFP imaging in living onion epidermal cells
    • Scott A, Wyatt S, Tsou PL, Robertson D, Allen NS (1999) Model system for plant cell biology: GFP imaging in living onion epidermal cells. Biotechniques 26:1125, 1128-1132
    • (1999) Biotechniques , vol.26 , Issue.1125 , pp. 1128-1132
    • Scott, A.1    Wyatt, S.2    Tsou, P.L.3    Robertson, D.4    Allen, N.S.5
  • 36
    • 0032170495 scopus 로고    scopus 로고
    • High-efficiency cloning of Arabidopsis full-length cDNA by biotinylated CAP trapper
    • Seki M, Carninci P, Nishiyama Y, Hayashizaki Y, Shinozaki K (1998) High-efficiency cloning of Arabidopsis full-length cDNA by biotinylated CAP trapper. Plant J 15:707-720
    • (1998) Plant J , vol.15 , pp. 707-720
    • Seki, M.1    Carninci, P.2    Nishiyama, Y.3    Hayashizaki, Y.4    Shinozaki, K.5
  • 38
    • 0037447151 scopus 로고    scopus 로고
    • Crystal structure of the Drosophila Mago nashi-Y14 complex
    • Shi H, Xu RM (2003) Crystal structure of the Drosophila Mago nashi-Y14 complex. Genes Dev 17:971-976
    • (2003) Genes Dev , vol.17 , pp. 971-976
    • Shi, H.1    Xu, R.M.2
  • 39
    • 0034913423 scopus 로고    scopus 로고
    • Strom AC, Weis K (2001) Importin-beta-like nuclear transport receptors. Genome Biol 2: REVIEWS3008
    • Strom AC, Weis K (2001) Importin-beta-like nuclear transport receptors. Genome Biol 2: REVIEWS3008
  • 40
    • 0034888461 scopus 로고    scopus 로고
    • Molecular characterization and expression analysis of a highly conserved rice mago nashi homolog
    • Swidzinski J, Zaplachinski S, Chuong SDX, Wong J, Muench DG (2001) Molecular characterization and expression analysis of a highly conserved rice mago nashi homolog. Genome 44:394-400
    • (2001) Genome , vol.44 , pp. 394-400
    • Swidzinski, J.1    Zaplachinski, S.2    Chuong, S.D.X.3    Wong, J.4    Muench, D.G.5
  • 41
    • 28344456363 scopus 로고    scopus 로고
    • Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core
    • Tange TO, Shibuya T, Jurica MS, Moore MJ (2005) Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core. Rna 11:1869-1883
    • (2005) Rna , vol.11 , pp. 1869-1883
    • Tange, T.O.1    Shibuya, T.2    Jurica, M.S.3    Moore, M.J.4
  • 42
    • 0025388973 scopus 로고
    • Expression analysis of a pseudogene in transgenic tobacco: A frameshift mutation prevents mRNA accumulation
    • Voelker TA, Moreno J, Chrispeels MJ (1990) Expression analysis of a pseudogene in transgenic tobacco: a frameshift mutation prevents mRNA accumulation. Plant Cell 2:255-261
    • (1990) Plant Cell , vol.2 , pp. 255-261
    • Voelker, T.A.1    Moreno, J.2    Chrispeels, M.J.3
  • 43
    • 0033997355 scopus 로고    scopus 로고
    • MAGOH interacts with a novel RNA-binding protein
    • Zhao X-F, Nowak N, Shows T, Aplan P (2000) MAGOH interacts with a novel RNA-binding protein. Genomics 63:145-148
    • (2000) Genomics , vol.63 , pp. 145-148
    • Zhao, X.-F.1    Nowak, N.2    Shows, T.3    Aplan, P.4
  • 44
    • 13444264729 scopus 로고    scopus 로고
    • GENEVESTIGATOR. Arabidopsis microarray database and analysis toolbox
    • Zimmermann P, Hirsch-Hoffmann M, Hennig L, Gruissem W (2004) GENEVESTIGATOR. Arabidopsis microarray database and analysis toolbox. Plant Physiol 136:2621-2632
    • (2004) Plant Physiol , vol.136 , pp. 2621-2632
    • Zimmermann, P.1    Hirsch-Hoffmann, M.2    Hennig, L.3    Gruissem, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.