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Volumn 111, Issue 52, 2014, Pages 18619-18624

TDP-43 N terminus encodes a novel ubiquitin-like fold and its unfolded form in equilibrium that can be shifted by binding to ssDNA

Author keywords

Amyotrophic lateral sclerosis; FTLD TDP; NMR spectroscopy; TDP 43; Ubiquitin like fold

Indexed keywords

NUCLEIC ACID; RIBONUCLEOPROTEIN; SINGLE STRANDED DNA; TAR DNA BINDING PROTEIN; UBIQUITIN; DNA BINDING PROTEIN; PROTEIN BINDING; PROTEIN TDP-43;

EID: 84924325934     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1413994112     Document Type: Article
Times cited : (104)

References (38)
  • 1
    • 33750716074 scopus 로고    scopus 로고
    • TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Arai T, et al. (2006) TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem Biophys Res Commun 351(3):602-611.
    • (2006) Biochem Biophys Res Commun , vol.351 , Issue.3 , pp. 602-611
    • Arai, T.1
  • 2
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann M, et al. (2006) Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314(5796):130-133.
    • (2006) Science , vol.314 , Issue.5796 , pp. 130-133
    • Neumann, M.1
  • 3
    • 84881490873 scopus 로고    scopus 로고
    • Converging mechanisms in ALS and FTD: Disrupted RNA and protein homeostasis
    • Ling SC, Polymenidou M, Cleveland DW (2013) Converging mechanisms in ALS and FTD: Disrupted RNA and protein homeostasis. N euron 79(3):416-438.
    • (2013) N euron , vol.79 , Issue.3 , pp. 416-438
    • Ling, S.C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 4
    • 84155167265 scopus 로고    scopus 로고
    • Gains or losses: Molecular mechanisms of TDP43-mediated neurodegeneration
    • Lee EB, Lee VM, Trojanowski JQ (2012) Gains or losses: Molecular mechanisms of TDP43-mediated neurodegeneration. Nat Rev Neurosci 13(1):38-50.
    • (2012) Nat Rev Neurosci , vol.13 , Issue.1 , pp. 38-50
    • Lee, E.B.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 5
    • 44749091997 scopus 로고    scopus 로고
    • Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation
    • Winton MJ, et al. (2008) Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation. J Biol Chem 283(19):13302-13309.
    • (2008) J Biol Chem , vol.283 , Issue.19 , pp. 13302-13309
    • Winton, M.J.1
  • 6
    • 17144426507 scopus 로고    scopus 로고
    • Human, Drosophila, and C.Elegans TDP43: Nucleic acid binding properties and splicing regulatory function
    • Ayala YM, et al. (2005) Human, Drosophila, and C.elegans TDP43: Nucleic acid binding properties and splicing regulatory function. J Mol Biol 348(3):575-588.
    • (2005) J Mol Biol , vol.348 , Issue.3 , pp. 575-588
    • Ayala, Y.M.1
  • 7
    • 0035965309 scopus 로고    scopus 로고
    • Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9
    • Buratti E, Baralle FE (2001) Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9. J Biol Chem 276(39):36337-36343.
    • (2001) J Biol Chem , vol.276 , Issue.39 , pp. 36337-36343
    • Buratti, E.1    Baralle, F.E.2
  • 8
    • 84890134733 scopus 로고    scopus 로고
    • Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43
    • Lukavsky PJ, et al. (2013) Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43. Nat Struct Mol Biol 20(12):1443-1449.
    • (2013) Nat Struct Mol Biol , vol.20 , Issue.12 , pp. 1443-1449
    • Lukavsky, P.J.1
  • 9
    • 27844514227 scopus 로고    scopus 로고
    • TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: An important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing
    • Buratti E, et al. (2005) TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: An important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing. J Biol Chem 280(45):37572-37584.
    • (2005) J Biol Chem , vol.280 , Issue.45 , pp. 37572-37584
    • Buratti, E.1
  • 10
    • 67749133873 scopus 로고    scopus 로고
    • TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity
    • Johnson BS, et al. (2009) TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity. J Biol Chem 284(30):20329-20339.
    • (2009) J Biol Chem , vol.284 , Issue.30 , pp. 20329-20339
    • Johnson, B.S.1
  • 11
    • 77956155794 scopus 로고    scopus 로고
    • Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43
    • Fuentealba RA, et al. (2010) Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43. J Biol Chem 285(34):26304-26314.
    • (2010) J Biol Chem , vol.285 , Issue.34 , pp. 26304-26314
    • Fuentealba, R.A.1
  • 12
    • 84857768992 scopus 로고    scopus 로고
    • Cellular model of TAR DNA-binding protein 43 (TDP-43) aggregation based on its C-terminal Gln/Asn-rich region
    • Budini M, et al. (2012) Cellular model of TAR DNA-binding protein 43 (TDP-43) aggregation based on its C-terminal Gln/Asn-rich region. J Biol Chem 287(10):7512-7525.
    • (2012) J Biol Chem , vol.287 , Issue.10 , pp. 7512-7525
    • Budini, M.1
  • 13
    • 66149114101 scopus 로고    scopus 로고
    • Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity
    • Zhang YJ, et al. (2009) Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity. Proc Natl Acad Sci USA 106(18):7607-7612.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.18 , pp. 7607-7612
    • Zhang, Y.J.1
  • 14
    • 80855138744 scopus 로고    scopus 로고
    • Molecular dissection of TDP-43 proteinopathies
    • Hasegawa M, et al. (2011) Molecular dissection of TDP-43 proteinopathies. J Mol Neurosci 45(3):480-485.
    • (2011) J Mol Neurosci , vol.45 , Issue.3 , pp. 480-485
    • Hasegawa, M.1
  • 15
    • 84880323707 scopus 로고    scopus 로고
    • The dual functions of the extreme N-terminus of TDP-43 in regulating its biological activity and inclusion formation
    • Zhang YJ, et al. (2013) The dual functions of the extreme N-terminus of TDP-43 in regulating its biological activity and inclusion formation. Hum Mol Genet 22(15):3112-3122.
    • (2013) Hum Mol Genet , vol.22 , Issue.15 , pp. 3112-3122
    • Zhang, Y.J.1
  • 16
    • 84865386915 scopus 로고    scopus 로고
    • The N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity
    • Chang CK, et al. (2012) The N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity. Biochem Biophys Res Commun 425(2):219-224.
    • (2012) Biochem Biophys Res Commun , vol.425 , Issue.2 , pp. 219-224
    • Chang, C.K.1
  • 17
    • 61749096920 scopus 로고    scopus 로고
    • Insight into "insoluble proteins" with pure water
    • Song J (2009) Insight into "insoluble proteins" with pure water. FEBS Lett 583(6):953-959.
    • (2009) FEBS Lett , vol.583 , Issue.6 , pp. 953-959
    • Song, J.1
  • 18
    • 84905451354 scopus 로고    scopus 로고
    • Why do proteins aggregate? "Intrinsically insoluble proteins" and "dark mediators" revealed by studies on "insoluble proteins" solubilized in pure water
    • Song J (2013) Why do proteins aggregate? "Intrinsically insoluble proteins" and "dark mediators" revealed by studies on "insoluble proteins" solubilized in pure water. F1000 Res 2:94.
    • (2013) F1000 Res , vol.2 , pp. 94
    • Song, J.1
  • 19
    • 0028541866 scopus 로고
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J Biomol NMR 4(6):845-858.
    • (1994) J Biomol NMR , vol.4 , Issue.6 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4
  • 20
    • 4344707281 scopus 로고    scopus 로고
    • Unfolded proteins and protein folding studied by NMR
    • Dyson HJ, Wright PE (2004) Unfolded proteins and protein folding studied by NMR. Chem Rev 104(8):3607-3622.
    • (2004) Chem Rev , vol.104 , Issue.8 , pp. 3607-3622
    • Dyson, H.J.1    Wright, P.E.2
  • 21
    • 84858634014 scopus 로고    scopus 로고
    • Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts
    • Camilloni C, De Simone A, Vranken WF, Vendruscolo M (2012) Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts. Biochemistry 51(11):2224-2231.
    • (2012) Biochemistry , vol.51 , Issue.11 , pp. 2224-2231
    • Camilloni, C.1    De Simone, A.2    Vranken, W.F.3    Vendruscolo, M.4
  • 22
    • 33751552347 scopus 로고    scopus 로고
    • Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: Implications for fibrillation
    • Marsh JA, Singh VK, Jia Z, Forman-Kay JD (2006) Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: Implications for fibrillation. Protein Sci 15(12):2795-2804.
    • (2006) Protein Sci , vol.15 , Issue.12 , pp. 2795-2804
    • Marsh, J.A.1    Singh, V.K.2    Jia, Z.3    Forman-Kay, J.D.4
  • 23
    • 0028857598 scopus 로고
    • Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements
    • Altieri AS, Hinton DP, Byrd RA (1995) Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements. J Am Chem Soc 117(28):7566-7567.
    • (1995) J Am Chem Soc , vol.117 , Issue.28 , pp. 7566-7567
    • Altieri, A.S.1    Hinton, D.P.2    Byrd, R.A.3
  • 24
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules
    • Palmer AG III, Kroenke CD, Loria JP (2001) Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods Enzymol 339:204-238.
    • (2001) Methods Enzymol , vol.339 , pp. 204-238
    • Palmer, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 25
    • 42449146665 scopus 로고    scopus 로고
    • Consistent blind protein structure generation from NMR chemical shift data
    • Shen Y, et al. (2008) Consistent blind protein structure generation from NMR chemical shift data. Proc Natl Acad Sci USA 105(12):4685-4690.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.12 , pp. 4685-4690
    • Shen, Y.1
  • 26
    • 84863570589 scopus 로고    scopus 로고
    • Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples
    • Lange OF, et al. (2012) Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples. Proc Natl Acad Sci USA 109(27):10873-10878.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.27 , pp. 10873-10878
    • Lange, O.F.1
  • 27
    • 77149179401 scopus 로고    scopus 로고
    • NMR structure determination for larger proteins using backbone-only data
    • Raman S, et al. (2010) NMR structure determination for larger proteins using backbone-only data. Science 327(5968):1014-1018.
    • (2010) Science , vol.327 , Issue.5968 , pp. 1014-1018
    • Raman, S.1
  • 28
    • 79960698669 scopus 로고    scopus 로고
    • Structure of the BamC two-domain protein obtained by Rosetta with a limited NMR data set
    • Warner LR, et al. (2011) Structure of the BamC two-domain protein obtained by Rosetta with a limited NMR data set. J Mol Biol 411(1):83-95.
    • (2011) J Mol Biol , vol.411 , Issue.1 , pp. 83-95
    • Warner, L.R.1
  • 29
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm L, Rosenström P (2010) Dali server: Conservation mapping in 3D. Nucleic Acids Res 38(Web Server issue):W545-9.
    • (2010) Nucleic Acids Res , vol.38 , Issue.WEB SERVER ISSUE , pp. W545-W549
    • Holm, L.1    Rosenström, P.2
  • 30
    • 56749155588 scopus 로고    scopus 로고
    • Structural probing of Zn(II), Cd(II) and Hg(II) binding to human ubiquitin
    • Falini G, Fermani S, Tosi G, Arnesano F, Natile G (2008) Structural probing of Zn(II), Cd(II) and Hg(II) binding to human ubiquitin. Chem Commun (Camb) 7(45):5960-5962.
    • (2008) Chem Commun (Camb) , vol.7 , Issue.45 , pp. 5960-5962
    • Falini, G.1    Fermani, S.2    Tosi, G.3    Arnesano, F.4    Natile, G.5
  • 31
    • 33846099868 scopus 로고    scopus 로고
    • DisProt: The database of disordered proteins
    • Sickmeier M, et al. (2007) DisProt: The database of disordered proteins. Nucleic Acids Res 35(Database issue):D786-D793.
    • (2007) Nucleic Acids Res , vol.35 , Issue.DATABASE ISSUE , pp. D786-D793
    • Sickmeier, M.1
  • 32
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • Dosztányi Z, Csizmok V, Tompa P, Simon I (2005) IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 21(16):3433-3434.
    • (2005) Bioinformatics , vol.21 , Issue.16 , pp. 3433-3434
    • Dosztányi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 33
    • 84896950092 scopus 로고    scopus 로고
    • Folding of the RNA recognition motif (RRM) domains of the amyotrophic lateral sclerosis (ALS)-linked protein TDP-43 reveals an intermediate state
    • Mackness BC, Tran MT, McClain SP, Matthews CR, Zitzewitz JA (2014) Folding of the RNA recognition motif (RRM) domains of the amyotrophic lateral sclerosis (ALS)-linked protein TDP-43 reveals an intermediate state. J Biol Chem 289(12):8264-8276.
    • (2014) J Biol Chem , vol.289 , Issue.12 , pp. 8264-8276
    • Mackness, B.C.1    Tran, M.T.2    McClain, S.P.3    Matthews, C.R.4    Zitzewitz, J.A.5
  • 34
    • 84878661360 scopus 로고    scopus 로고
    • Stress granules as crucibles of ALS pathogenesis
    • Li YR, King OD, Shorter J, Gitler AD (2013) Stress granules as crucibles of ALS pathogenesis. J Cell Biol 201(3):361-372.
    • (2013) J Cell Biol , vol.201 , Issue.3 , pp. 361-372
    • Li, Y.R.1    King, O.D.2    Shorter, J.3    Gitler, A.D.4
  • 35
    • 84898745559 scopus 로고    scopus 로고
    • Two-way communications between ubiquitin-like modifiers and DNA
    • Ulrich HD (2014) Two-way communications between ubiquitin-like modifiers and DNA. Nat Struct Mol Biol 21(4):317-324.
    • (2014) Nat Struct Mol Biol , vol.21 , Issue.4 , pp. 317-324
    • Ulrich, H.D.1
  • 36
    • 79953180492 scopus 로고    scopus 로고
    • Characterizing the RNA targets and position-dependent splicing regulation by TDP-43
    • Tollervey JR, et al. (2011) Characterizing the RNA targets and position-dependent splicing regulation by TDP-43. Nat Neurosci 14(4):452-458.
    • (2011) Nat Neurosci , vol.14 , Issue.4 , pp. 452-458
    • Tollervey, J.R.1
  • 37
    • 84857124994 scopus 로고    scopus 로고
    • Endogenous TDP-43 localized to stress granules can subsequently form protein aggregates
    • Parker SJ, et al. (2012) Endogenous TDP-43 localized to stress granules can subsequently form protein aggregates. Neurochem Int 60(4):415-424.
    • (2012) Neurochem Int , vol.60 , Issue.4 , pp. 415-424
    • Parker, S.J.1
  • 38
    • 84862151933 scopus 로고    scopus 로고
    • The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease
    • King OD, Gitler AD, Shorter J (2012) The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease. Brain Res 1462:61-80.
    • (2012) Brain Res , vol.1462 , pp. 61-80
    • King, O.D.1    Gitler, A.D.2    Shorter, J.3


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