메뉴 건너뛰기




Volumn 8, Issue 1, 2013, Pages

Plant Coilin: Structural Characteristics and RNA-Binding Properties

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN ATCOILIN; PROTEIN COILIN; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 84872177572     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0053571     Document Type: Article
Times cited : (31)

References (46)
  • 1
    • 77951023685 scopus 로고    scopus 로고
    • Phosphorylation and the Cajal body: modification in search of function
    • Hebert MD, (2010) Phosphorylation and the Cajal body: modification in search of function. Arch Biochem Biophys 496(2): 69-76.
    • (2010) Arch Biochem Biophys , vol.496 , Issue.2 , pp. 69-76
    • Hebert, M.D.1
  • 2
    • 0031804377 scopus 로고    scopus 로고
    • Of coiled bodies, gems, and salmon
    • Matera AG, (1998) Of coiled bodies, gems, and salmon. J Cell Biochem 70(2): 181-192.
    • (1998) J Cell Biochem , vol.70 , Issue.2 , pp. 181-192
    • Matera, A.G.1
  • 3
    • 0031667189 scopus 로고    scopus 로고
    • Coilin can form a complex with the U7 small nuclear ribonucleoprotein
    • Bellini M, Gall JG, (1998) Coilin can form a complex with the U7 small nuclear ribonucleoprotein. Mol Biol Cell 9: 2987-3001.
    • (1998) Mol Biol Cell , vol.9 , pp. 2987-3001
    • Bellini, M.1    Gall, J.G.2
  • 4
    • 0036323673 scopus 로고    scopus 로고
    • Large-scale isolation of Cajal bodies from HeLa cells
    • Lam YW, Lyon CE, Lamond AI, (2002) Large-scale isolation of Cajal bodies from HeLa cells. Mol Biol Cell 13: 2461-2473.
    • (2002) Mol Biol Cell , vol.13 , pp. 2461-2473
    • Lam, Y.W.1    Lyon, C.E.2    Lamond, A.I.3
  • 5
    • 0027324153 scopus 로고
    • Identification and characterization of a sphere organelle protein
    • Tuma RS, Stolk JA, Roth MB, (1993) Identification and characterization of a sphere organelle protein. J Cell Biol 122: 767-773.
    • (1993) J Cell Biol , vol.122 , pp. 767-773
    • Tuma, R.S.1    Stolk, J.A.2    Roth, M.B.3
  • 7
    • 33745590149 scopus 로고    scopus 로고
    • A distant coilin homologue is required for the formation of Cajal bodies in Arabidopsis
    • Collier S, Pendle A, Boudonck K, van Rij T, Dolan L, et al. (2006) A distant coilin homologue is required for the formation of Cajal bodies in Arabidopsis. Mol Biol Cell 17: 2942-2951.
    • (2006) Mol Biol Cell , vol.17 , pp. 2942-2951
    • Collier, S.1    Pendle, A.2    Boudonck, K.3    van Rij, T.4    Dolan, L.5
  • 8
    • 61449169212 scopus 로고    scopus 로고
    • Coilin is essential for Cajal body organization in Drosophila melanogaster
    • Liu JL, Wu Z, Nizami Z, Deryusheva S, Rajendra TK, et al. (2009) Coilin is essential for Cajal body organization in Drosophila melanogaster. Mol. Biol. Cell 20: 1661-1670.
    • (2009) Mol.Biol. Cell , vol.20 , pp. 1661-1670
    • Liu, J.L.1    Wu, Z.2    Nizami, Z.3    Deryusheva, S.4    Rajendra, T.K.5
  • 9
    • 0025852299 scopus 로고
    • Human autoantibody to a novel protein of the nuclear coiled body: Immunological characterization and cDNA cloning of p80-coilin
    • Andrade LEC, Chan EKL, Raska I, Peebles CL, Roos G, et al. (1991) Human autoantibody to a novel protein of the nuclear coiled body: Immunological characterization and cDNA cloning of p80-coilin. J Exp Med 173: 1407-1419.
    • (1991) J Exp Med , vol.173 , pp. 1407-1419
    • Andrade, L.E.C.1    Chan, E.K.L.2    Raska, I.3    Peebles, C.L.4    Roos, G.5
  • 10
    • 0032483028 scopus 로고    scopus 로고
    • Evolutionary parameters of the transcribed mammalian genome: an analysis of 2,820 orthologous rodent and human sequences
    • Makalowski W, Boguski MS, (1998) Evolutionary parameters of the transcribed mammalian genome: an analysis of 2,820 orthologous rodent and human sequences. Proc Natl Acad Sci USA 95(16): 9407-9412.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.16 , pp. 9407-9412
    • Makalowski, W.1    Boguski, M.S.2
  • 12
    • 0035939674 scopus 로고    scopus 로고
    • Residual Cajal bodies in coilin knockout mice fail to recruit Sm snRNPs and SMN, the spinal muscular atrophy determining gene product
    • Tucker KE, Berciano MT, Jacobs EY, LePage D, Shpargel KB, et al. (2001) Residual Cajal bodies in coilin knockout mice fail to recruit Sm snRNPs and SMN, the spinal muscular atrophy determining gene product. J. Cell Biol 154: 293-307.
    • (2001) J. Cell Biol , vol.154 , pp. 293-307
    • Tucker, K.E.1    Berciano, M.T.2    Jacobs, E.Y.3    LePage, D.4    Shpargel, K.B.5
  • 13
    • 67650337072 scopus 로고    scopus 로고
    • Reduced viability, fertility and fecundity in mice lacking the Cajal body marker protein, coilin
    • Walker MP, Tian L, Matera AG (2009) Reduced viability, fertility and fecundity in mice lacking the Cajal body marker protein, coilin. PLoS One: 4, e6171.
    • (2009) PLoS One , vol.4
    • Walker, M.P.1    Tian, L.2    Matera, A.G.3
  • 14
    • 77950462004 scopus 로고    scopus 로고
    • Dynamic control of Cajal body number in zebrafish embryogenesis
    • Strzelecka M, Oates AC, Neugebauer KM, (2010) Dynamic control of Cajal body number in zebrafish embryogenesis. Nucleus 1: 96-108.
    • (2010) Nucleus , vol.1 , pp. 96-108
    • Strzelecka, M.1    Oates, A.C.2    Neugebauer, K.M.3
  • 15
    • 33745594313 scopus 로고    scopus 로고
    • Ongoing U snRNP biogenesis is required for the integrity of Cajal bodies
    • Lemm I, Girard C, Kuhn AN, Watkins NJ, Schneider M, et al. (2006) Ongoing U snRNP biogenesis is required for the integrity of Cajal bodies. Mol Biol Cell 17(7): 3221-31.
    • (2006) Mol Biol Cell , vol.17 , Issue.7 , pp. 3221-3231
    • Lemm, I.1    Girard, C.2    Kuhn, A.N.3    Watkins, N.J.4    Schneider, M.5
  • 16
    • 42449118380 scopus 로고    scopus 로고
    • Coilin levels and modifications influence artificial reporter splicing
    • Whittom AA, Xu H, Hebert MD, (2008) Coilin levels and modifications influence artificial reporter splicing. Cell Mol Life Sci 65: 1256-1271.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1256-1271
    • Whittom, A.A.1    Xu, H.2    Hebert, M.D.3
  • 18
    • 0033638658 scopus 로고    scopus 로고
    • Self-association of coilin reveals a common theme in nuclear body localization
    • Hebert MD, Matera AG, (2000) Self-association of coilin reveals a common theme in nuclear body localization. Mol Biol Cell 11: 4159-4171.
    • (2000) Mol Biol Cell , vol.11 , pp. 4159-4171
    • Hebert, M.D.1    Matera, A.G.2
  • 19
    • 77957794698 scopus 로고    scopus 로고
    • Solution structure of the carboxy-terminal Tudor domain from human Coilin
    • Shanbhag R, Kurabi A, Kwan JJ, Donaldson LW, (2010) Solution structure of the carboxy-terminal Tudor domain from human Coilin. FEBS Lett 584: 4351-4356.
    • (2010) FEBS Lett , vol.584 , pp. 4351-4356
    • Shanbhag, R.1    Kurabi, A.2    Kwan, J.J.3    Donaldson, L.W.4
  • 20
    • 0035887042 scopus 로고    scopus 로고
    • Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein
    • Hebert MD, Szymczyk PW, Shpargel KB, Matera AG, (2001) Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein. Genes Dev 15: 2720-2729.
    • (2001) Genes Dev , vol.15 , pp. 2720-2729
    • Hebert, M.D.1    Szymczyk, P.W.2    Shpargel, K.B.3    Matera, A.G.4
  • 21
    • 77953292137 scopus 로고    scopus 로고
    • Coilin phosphorylation mediates interaction with SMN and SmB
    • Toyota CG, Davis MD, Cosman AM, Hebert MD, (2010) Coilin phosphorylation mediates interaction with SMN and SmB'. Chromosoma 119: 205-215.
    • (2010) Chromosoma , vol.119 , pp. 205-215
    • Toyota, C.G.1    Davis, M.D.2    Cosman, A.M.3    Hebert, M.D.4
  • 22
    • 69449096183 scopus 로고    scopus 로고
    • Cajal-body formation correlates with differential coilin phosphorylation in primary and transformed cell lines
    • Hearst SM, Gilder AS, Negi SS, Davis MD, George EM, et al. (2009) Cajal-body formation correlates with differential coilin phosphorylation in primary and transformed cell lines. J Cell Sci 122 (Pt 11): 1872-1881.
    • (2009) J Cell Sci , vol.122 , Issue.Pt 11 , pp. 1872-1881
    • Hearst, S.M.1    Gilder, A.S.2    Negi, S.S.3    Davis, M.D.4    George, E.M.5
  • 23
    • 25144436982 scopus 로고    scopus 로고
    • The C-terminal domain of coilin interacts with Sm proteins and U snRNPs
    • Xu H, Pillai RS, Azzouz TN, Shpargel KB, Kambach C, et al. (2005) The C-terminal domain of coilin interacts with Sm proteins and U snRNPs. Chromosoma 114: 155-166.
    • (2005) Chromosoma , vol.114 , pp. 155-166
    • Xu, H.1    Pillai, R.S.2    Azzouz, T.N.3    Shpargel, K.B.4    Kambach, C.5
  • 25
    • 0027389169 scopus 로고
    • Assembly of snRNP-containing coiled bodies is regulated in interphase and mitosis-evidence that the coiled body is a kinetic nuclear structure
    • Carmo-Fonseca M, Ferreira J, Lamond AI, (1993) Assembly of snRNP-containing coiled bodies is regulated in interphase and mitosis-evidence that the coiled body is a kinetic nuclear structure. J Cell Biol 120: 841-852.
    • (1993) J Cell Biol , vol.120 , pp. 841-852
    • Carmo-Fonseca, M.1    Ferreira, J.2    Lamond, A.I.3
  • 26
    • 78649658701 scopus 로고    scopus 로고
    • Coilin interacts with Ku proteins and inhibits in vitro non-homologous DNA end joining
    • Velma V, Carrero ZI, Cosman AM, Hebert MD, (2010) Coilin interacts with Ku proteins and inhibits in vitro non-homologous DNA end joining. FEBS Lett 584: 4735-4739.
    • (2010) FEBS Lett , vol.584 , pp. 4735-4739
    • Velma, V.1    Carrero, Z.I.2    Cosman, A.M.3    Hebert, M.D.4
  • 27
    • 84860454343 scopus 로고    scopus 로고
    • In vitro RNase and nucleic acid binding activities implicate coilin in U snRNA Processing
    • Broome HJ, Hebert MD, (2012) In vitro RNase and nucleic acid binding activities implicate coilin in U snRNA Processing. PLoS One 7(4): e36300.
    • (2012) PLoS One , vol.7 , Issue.4
    • Broome, H.J.1    Hebert, M.D.2
  • 28
    • 24044515001 scopus 로고    scopus 로고
    • FoldIndex: a simple tool to predict whether a given protein sequence is intrinsically unfolded
    • Prilusky J, Felder CE, Zeev-Ben-Mordehai T, Rydberg EH, Man O, et al. (2005) FoldIndex: a simple tool to predict whether a given protein sequence is intrinsically unfolded. Bioinformatics 21: 3435-3438.
    • (2005) Bioinformatics , vol.21 , pp. 3435-3438
    • Prilusky, J.1    Felder, C.E.2    Zeev-Ben-Mordehai, T.3    Rydberg, E.H.4    Man, O.5
  • 30
    • 1642546383 scopus 로고    scopus 로고
    • Computation and analysis of protein circular dichroism spectra
    • Sreerama N, Woody RW, (2004) Computation and analysis of protein circular dichroism spectra. Methods Enzymol 383: 318-351.
    • (2004) Methods Enzymol , vol.383 , pp. 318-351
    • Sreerama, N.1    Woody, R.W.2
  • 31
    • 44349189806 scopus 로고    scopus 로고
    • K2D2: estimation of protein secondary structure from circular dichroism spectra
    • Perez-Iratxeta C, Andrade-Navarro M, (2008) K2D2: estimation of protein secondary structure from circular dichroism spectra. BMC Struct Biol 8: 25.
    • (2008) BMC Struct Biol , vol.8 , pp. 25
    • Perez-Iratxeta, C.1    Andrade-Navarro, M.2
  • 32
    • 0023785593 scopus 로고
    • Secondary structure of proteins through circular dichroism spectroscopy
    • Johnson WC Jr, (1988) Secondary structure of proteins through circular dichroism spectroscopy. Annu Rev Biophys Biophys Chem 17: 145-166.
    • (1988) Annu Rev Biophys Biophys Chem , vol.17 , pp. 145-166
    • Johnson Jr., W.C.1
  • 33
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: a point where biology waits for physics
    • Uversky VN, (2002) Natively unfolded proteins: a point where biology waits for physics. Protein Sci 11: 739-756.
    • (2002) Protein Sci , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 34
    • 0029180525 scopus 로고
    • Fluorescence spectroscopic studies of proteins
    • Roy S, Bhattacharyya B, (1995) Fluorescence spectroscopic studies of proteins. Subcell Biochem 24: 101-114.
    • (1995) Subcell Biochem , vol.24 , pp. 101-114
    • Roy, S.1    Bhattacharyya, B.2
  • 35
    • 33646918845 scopus 로고    scopus 로고
    • Probing protein folding and conformational transitions with fluorescence
    • Royer CA, (2006) Probing protein folding and conformational transitions with fluorescence. Chem Rev 106: 1769-1784.
    • (2006) Chem Rev , vol.106 , pp. 1769-1784
    • Royer, C.A.1
  • 37
    • 17844403033 scopus 로고    scopus 로고
    • Bacterial DNA segregation dynamics mediated by the polymerizing protein ParF
    • Barilla D, Rosenberg MF, Nobbmann U, Hayes F, (2005) Bacterial DNA segregation dynamics mediated by the polymerizing protein ParF. EMBO J 24: 1453-1464.
    • (2005) EMBO J , vol.24 , pp. 1453-1464
    • Barilla, D.1    Rosenberg, M.F.2    Nobbmann, U.3    Hayes, F.4
  • 38
    • 84862225232 scopus 로고    scopus 로고
    • Ab initio protein structure assembly using continuous structure fragments and optimized knowledge-based force field
    • Xu D, Zhang Y, (2012) Ab initio protein structure assembly using continuous structure fragments and optimized knowledge-based force field. Proteins 80(7): 1715-1735.
    • (2012) Proteins , vol.80 , Issue.7 , pp. 1715-1735
    • Xu, D.1    Zhang, Y.2
  • 39
    • 34250851687 scopus 로고    scopus 로고
    • LOMETS: A local meta-threading-server for protein structure prediction
    • Wu S, Zhang Y, (2007) LOMETS: A local meta-threading-server for protein structure prediction. Nucleic Acids Res 35: 3375-3382.
    • (2007) Nucleic Acids Res , vol.35 , pp. 3375-3382
    • Wu, S.1    Zhang, Y.2
  • 40
    • 0028004607 scopus 로고
    • Crystal structure at 1.92 angstrom resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin
    • Oubridge C, Ito N, Evans PR, Teo C, Nagai K, (1994) Crystal structure at 1.92 angstrom resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature 372: 432-438.
    • (1994) Nature , vol.372 , pp. 432-438
    • Oubridge, C.1    Ito, N.2    Evans, P.R.3    Teo, C.4    Nagai, K.5
  • 41
    • 35648993490 scopus 로고    scopus 로고
    • Multiple tryptophan probes reveal that ubiquitin folds via a late misfolded intermediate.J.Mol
    • Vallee-Belisle A, Michnick SW, (2007) Multiple tryptophan probes reveal that ubiquitin folds via a late misfolded intermediate. J. Mol. Biol 374: 791-805.
    • (2007) Biol , vol.374 , pp. 791-805
    • Vallee-Belisle, A.1    Michnick, S.W.2
  • 42
    • 48649105144 scopus 로고    scopus 로고
    • Helix mutations stabilize a late productive intermediate on the folding pathway of ubiquitin
    • Rea AM, Simpson ER, Crespo MD, Searle MS, (2008) Helix mutations stabilize a late productive intermediate on the folding pathway of ubiquitin. Biochemistry 47: 8225-8236.
    • (2008) Biochemistry , vol.47 , pp. 8225-8236
    • Rea, A.M.1    Simpson, E.R.2    Crespo, M.D.3    Searle, M.S.4
  • 43
    • 80053457099 scopus 로고    scopus 로고
    • Coilin phosphomutants disrupt Cajal body formation, reduce cell proliferation and produce a distinct coilin degradation product
    • Carrero ZI, Velma V, Douglas HE, Hebert MD, (2011) Coilin phosphomutants disrupt Cajal body formation, reduce cell proliferation and produce a distinct coilin degradation product. PLoS One 6(10): e25743.
    • (2011) PLoS One , vol.6 , Issue.10
    • Carrero, Z.I.1    Velma, V.2    Douglas, H.E.3    Hebert, M.D.4
  • 44
    • 52649145895 scopus 로고    scopus 로고
    • GPS 2.0, a tool to predict kinase-specific phosphorylation sites in hierarchy.Mol Cell Proteomics
    • Xue Y, Ren J, Gao X, Jin C, Wen L, et al. (2008) GPS 2.0, a tool to predict kinase-specific phosphorylation sites in hierarchy. Mol Cell Proteomics. 7: 1598-1608.
    • (2008) , vol.7 , pp. 1598-1608
    • Xue, Y.1    Ren, J.2    Gao, X.3    Jin, C.4    Wen, L.5
  • 45
    • 33644894371 scopus 로고    scopus 로고
    • The Cajal body: a meeting place for spliceosomal snRNPs in the nuclear maze
    • Stanek D, Neugebauer KM, (2006) The Cajal body: a meeting place for spliceosomal snRNPs in the nuclear maze. Chromosoma 115: 343-354.
    • (2006) Chromosoma , vol.115 , pp. 343-354
    • Stanek, D.1    Neugebauer, K.M.2
  • 46
    • 58149259990 scopus 로고    scopus 로고
    • De novo formation of a subnuclear body
    • Kaiser TE, Intine RV, Dundr M, (2008) De novo formation of a subnuclear body. Science 322(5908): 1713-1717.
    • (2008) Science , vol.322 , Issue.5908 , pp. 1713-1717
    • Kaiser, T.E.1    Intine, R.V.2    Dundr, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.