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Volumn 6, Issue 5, 2011, Pages

Calpain-catalyzed proteolysis of human dutpase specifically removes the nuclear localization signal peptide

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CALPAIN; DEOXYURIDINE TRIPHOSPHATE DERIVATIVE; DEOXYURIDINE TRIPHOSPHATE PYROPHOSPHATASE; PEPTIDE;

EID: 79956295897     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0019546     Document Type: Article
Times cited : (8)

References (47)
  • 1
    • 73649114570 scopus 로고    scopus 로고
    • Calcium-activated calpain-2 is a mediator of beta cell dysfunction and apoptosis in type 2 diabetes
    • Huang CJ, Gurlo T, Haataja L, Costes S, Daval M, et al. (2010) Calcium-activated calpain-2 is a mediator of beta cell dysfunction and apoptosis in type 2 diabetes. J Biol Chem 285: 339-348.
    • (2010) J Biol Chem , vol.285 , pp. 339-348
    • Huang, C.J.1    Gurlo, T.2    Haataja, L.3    Costes, S.4    Daval, M.5
  • 2
    • 67349170024 scopus 로고    scopus 로고
    • Calpain-1 induces apoptosis in pulmonary microvascular endothelial cells under septic conditions
    • Hu H, Li X, Li Y, Wang L, Mehta S, et al. (2009) Calpain-1 induces apoptosis in pulmonary microvascular endothelial cells under septic conditions. Microvasc Res 78: 33-39.
    • (2009) Microvasc Res , vol.78 , pp. 33-39
    • Hu, H.1    Li, X.2    Li, Y.3    Wang, L.4    Mehta, S.5
  • 3
    • 33845972578 scopus 로고    scopus 로고
    • Calpain inhibition stimulates caspase-dependent apoptosis induced by taxol in NIH3T3 cells
    • Pineiro D, Martin ME, Guerra N, Salinas M, Gonzalez VM, (2007) Calpain inhibition stimulates caspase-dependent apoptosis induced by taxol in NIH3T3 cells. Exp Cell Res 313: 369-379.
    • (2007) Exp Cell Res , vol.313 , pp. 369-379
    • Pineiro, D.1    Martin, M.E.2    Guerra, N.3    Salinas, M.4    Gonzalez, V.M.5
  • 4
    • 34247472173 scopus 로고    scopus 로고
    • Cross-talk between calpain and caspase-3/-7 in cisplatin-induced apoptosis of melanoma cells: a major role of calpain inhibition in cell death protection and p53 status
    • Del Bello B, Moretti D, Gamberucci A, Maellaro E, (2007) Cross-talk between calpain and caspase-3/-7 in cisplatin-induced apoptosis of melanoma cells: a major role of calpain inhibition in cell death protection and p53 status. Oncogene 26: 2717-2726.
    • (2007) Oncogene , vol.26 , pp. 2717-2726
    • Del Bello, B.1    Moretti, D.2    Gamberucci, A.3    Maellaro, E.4
  • 6
    • 33746126134 scopus 로고    scopus 로고
    • Implication of calpain in neuronal apoptosis. A possible regulation of Alzheimer's disease
    • Raynaud F, Marcilhac A, (2006) Implication of calpain in neuronal apoptosis. A possible regulation of Alzheimer's disease. FEBS J 273: 3437-3443.
    • (2006) FEBS J , vol.273 , pp. 3437-3443
    • Raynaud, F.1    Marcilhac, A.2
  • 7
    • 2642520594 scopus 로고    scopus 로고
    • RyR2 and calpain-10 delineate a novel apoptosis pathway in pancreatic islets
    • Johnson JD, Han Z, Otani K, Ye H, Zhang Y, et al. (2004) RyR2 and calpain-10 delineate a novel apoptosis pathway in pancreatic islets. J Biol Chem 279: 24794-24802.
    • (2004) J Biol Chem , vol.279 , pp. 24794-24802
    • Johnson, J.D.1    Han, Z.2    Otani, K.3    Ye, H.4    Zhang, Y.5
  • 9
    • 61849128423 scopus 로고    scopus 로고
    • Keeping uracil out of DNA: physiological role, structure and catalytic mechanism of dUTPases
    • Vertessy BG, Toth J, (2009) Keeping uracil out of DNA: physiological role, structure and catalytic mechanism of dUTPases. Acc Chem Res 42: 97-106.
    • (2009) Acc Chem Res , vol.42 , pp. 97-106
    • Vertessy, B.G.1    Toth, J.2
  • 10
    • 54049140420 scopus 로고    scopus 로고
    • Novel opportunities for thymidylate metabolism as a therapeutic target
    • Wilson PM, Fazzone W, LaBonte MJ, Deng J, Neamati N, et al. (2008) Novel opportunities for thymidylate metabolism as a therapeutic target. Mol Cancer Ther 7: 3029-3037.
    • (2008) Mol Cancer Ther , vol.7 , pp. 3029-3037
    • Wilson, P.M.1    Fazzone, W.2    LaBonte, M.J.3    Deng, J.4    Neamati, N.5
  • 11
    • 0017866954 scopus 로고
    • Deoxyuridine triphosphatase of Escherichia coli. Purification, properties, and use as a reagent to reduce uracil incorporation into DNA
    • Shlomai J, Kornberg A, (1978) Deoxyuridine triphosphatase of Escherichia coli. Purification, properties, and use as a reagent to reduce uracil incorporation into DNA. J Biol Chem 253: 3305-3312.
    • (1978) J Biol Chem , vol.253 , pp. 3305-3312
    • Shlomai, J.1    Kornberg, A.2
  • 12
    • 0034694904 scopus 로고    scopus 로고
    • Altered Subunit Communication in Subfamilies of Trimeric dUTPases
    • Fiser A, Vertessy BG, (2000) Altered Subunit Communication in Subfamilies of Trimeric dUTPases. Biochem Biophys Res Commun 279: 534-542.
    • (2000) Biochem Biophys Res Commun , vol.279 , pp. 534-542
    • Fiser, A.1    Vertessy, B.G.2
  • 13
    • 45849136329 scopus 로고    scopus 로고
    • Active site of mycobacterial dUTPase: structural characteristics and a built-in sensor
    • Varga B, Barabas O, Takacs E, Nagy N, Nagy P, et al. (2008) Active site of mycobacterial dUTPase: structural characteristics and a built-in sensor. Biochem Biophys Res Commun 373: 8-13.
    • (2008) Biochem Biophys Res Commun , vol.373 , pp. 8-13
    • Varga, B.1    Barabas, O.2    Takacs, E.3    Nagy, N.4    Nagy, P.5
  • 14
    • 33750935665 scopus 로고    scopus 로고
    • Quantitative determination of uracil residues in Escherichia coli DNA: Contribution of ung, dug, and dut genes to uracil avoidance
    • Lari SU, Chen CY, Vertessy BG, Morre J, Bennett SE, (2006) Quantitative determination of uracil residues in Escherichia coli DNA: Contribution of ung, dug, and dut genes to uracil avoidance. DNA Repair (Amst) 5: 1407-1420.
    • (2006) DNA Repair (Amst) , vol.5 , pp. 1407-1420
    • Lari, S.U.1    Chen, C.Y.2    Vertessy, B.G.3    Morre, J.4    Bennett, S.E.5
  • 15
    • 84855639293 scopus 로고    scopus 로고
    • A one-step method for quantitative determination of uracil in DNA by real-time PCR
    • Horvath A, Vertessy BG, (2010) A one-step method for quantitative determination of uracil in DNA by real-time PCR. Nucleic Acids Res 38: e196.
    • (2010) Nucleic Acids Res , vol.38
    • Horvath, A.1    Vertessy, B.G.2
  • 16
    • 0023967987 scopus 로고
    • Lethality of a dut (deoxyuridine triphosphatase) mutation in Escherichia coli
    • el-Hajj HH, Zhang H, Weiss B, (1988) Lethality of a dut (deoxyuridine triphosphatase) mutation in Escherichia coli. J Bacteriol 170: 1069-1075.
    • (1988) J Bacteriol , vol.170 , pp. 1069-1075
    • El-Hajj, H.H.1    Zhang, H.2    Weiss, B.3
  • 17
    • 0027426749 scopus 로고
    • DUtp pyrophosphatase is an essential enzyme in Saccharomyces cerevisiae
    • Gadsden MH, McIntosh EM, Game JC, Wilson PJ, Haynes RH, (1993) dUtp pyrophosphatase is an essential enzyme in Saccharomyces cerevisiae. Embo J 12: 4425-4431.
    • (1993) Embo J , vol.12 , pp. 4425-4431
    • Gadsden, M.H.1    McIntosh, E.M.2    Game, J.C.3    Wilson, P.J.4    Haynes, R.H.5
  • 19
    • 0029882967 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli dUTPase in complex with a substrate analogue (dUDP)
    • Larsson G, Svensson LA, Nyman PO, (1996) Crystal structure of the Escherichia coli dUTPase in complex with a substrate analogue (dUDP). Nat Struct Biol 3: 532-538.
    • (1996) Nat Struct Biol , vol.3 , pp. 532-538
    • Larsson, G.1    Svensson, L.A.2    Nyman, P.O.3
  • 20
    • 13844296398 scopus 로고    scopus 로고
    • DUTPase as a platform for antimalarial drug design: structural basis for the selectivity of a class of nucleoside inhibitors
    • Whittingham JL, Leal I, Nguyen C, Kasinathan G, Bell E, et al. (2005) dUTPase as a platform for antimalarial drug design: structural basis for the selectivity of a class of nucleoside inhibitors. Structure 13: 329-338.
    • (2005) Structure , vol.13 , pp. 329-338
    • Whittingham, J.L.1    Leal, I.2    Nguyen, C.3    Kasinathan, G.4    Bell, E.5
  • 21
    • 34548702237 scopus 로고    scopus 로고
    • Active site closure facilitates juxtaposition of reactant atoms for initiation of catalysis by human dUTPase
    • Varga B, Barabas O, Kovari J, Toth J, Hunyadi-Gulyas E, et al. (2007) Active site closure facilitates juxtaposition of reactant atoms for initiation of catalysis by human dUTPase. FEBS Lett 581: 4783-4788.
    • (2007) FEBS Lett , vol.581 , pp. 4783-4788
    • Varga, B.1    Barabas, O.2    Kovari, J.3    Toth, J.4    Hunyadi-Gulyas, E.5
  • 22
    • 2342441633 scopus 로고    scopus 로고
    • Altered active site flexibility and a structural metal-binding site in eukaryotic dUTPase: kinetic characterization, folding, and crystallographic studies of the homotrimeric Drosophila enzyme
    • Kovari J, Barabas O, Takacs E, Bekesi A, Dubrovay Z, et al. (2004) Altered active site flexibility and a structural metal-binding site in eukaryotic dUTPase: kinetic characterization, folding, and crystallographic studies of the homotrimeric Drosophila enzyme. J Biol Chem 279: 17932-17944.
    • (2004) J Biol Chem , vol.279 , pp. 17932-17944
    • Kovari, J.1    Barabas, O.2    Takacs, E.3    Bekesi, A.4    Dubrovay, Z.5
  • 23
    • 0030791450 scopus 로고    scopus 로고
    • The human dUTPase gene encodes both nuclear and mitochondrial isoforms. Differential expression of the isoforms and characterization of a cDNA encoding the mitochondrial species
    • Ladner RD, Caradonna SJ, (1997) The human dUTPase gene encodes both nuclear and mitochondrial isoforms. Differential expression of the isoforms and characterization of a cDNA encoding the mitochondrial species. J Biol Chem 272: 19072-19080.
    • (1997) J Biol Chem , vol.272 , pp. 19072-19080
    • Ladner, R.D.1    Caradonna, S.J.2
  • 24
    • 0037530083 scopus 로고    scopus 로고
    • Identification of sequence determinants of human nuclear dUTPase isoform localization
    • Tinkelenberg BA, Fazzone W, Lynch FJ, Ladner RD, (2003) Identification of sequence determinants of human nuclear dUTPase isoform localization. Exp Cell Res 287: 39-46.
    • (2003) Exp Cell Res , vol.287 , pp. 39-46
    • Tinkelenberg, B.A.1    Fazzone, W.2    Lynch, F.J.3    Ladner, R.D.4
  • 25
    • 60749125716 scopus 로고    scopus 로고
    • Molecular shape and prominent role of beta-strand swapping in organization of dUTPase oligomers
    • Takacs E, Barabas O, Petoukhov MV, Svergun DI, Vertessy BG, (2009) Molecular shape and prominent role of beta-strand swapping in organization of dUTPase oligomers. FEBS Lett 583: 865-871.
    • (2009) FEBS Lett , vol.583 , pp. 865-871
    • Takacs, E.1    Barabas, O.2    Petoukhov, M.V.3    Svergun, D.I.4    Vertessy, B.G.5
  • 26
    • 77951247293 scopus 로고    scopus 로고
    • Drosophila proteins involved in metabolism of uracil-DNA possess different types of nuclear localization signals
    • Merényi G, Kónya E, Vertessy BG, (2010) Drosophila proteins involved in metabolism of uracil-DNA possess different types of nuclear localization signals. FEBS Journal 277: 2142-2156.
    • (2010) FEBS Journal , vol.277 , pp. 2142-2156
    • Merényi, G.1    Kónya, E.2    Vertessy, B.G.3
  • 27
    • 26844461079 scopus 로고    scopus 로고
    • Digestive versus regulatory proteases: on calpain action in vivo
    • Friedrich P, Bozoky Z, (2005) Digestive versus regulatory proteases: on calpain action in vivo. Biol Chem 386: 609-612.
    • (2005) Biol Chem , vol.386 , pp. 609-612
    • Friedrich, P.1    Bozoky, Z.2
  • 28
    • 61849114645 scopus 로고    scopus 로고
    • Nuclear localization signal-dependent and -independent movements of Drosophila melanogaster dUTPase isoforms during nuclear cleavage
    • Muha V, Zagyva I, Venkei Z, Szabad J, Vertessy BG, (2009) Nuclear localization signal-dependent and-independent movements of Drosophila melanogaster dUTPase isoforms during nuclear cleavage. Biochem Biophys Res Commun 381: 271-275.
    • (2009) Biochem Biophys Res Commun , vol.381 , pp. 271-275
    • Muha, V.1    Zagyva, I.2    Venkei, Z.3    Szabad, J.4    Vertessy, B.G.5
  • 29
    • 77954244548 scopus 로고    scopus 로고
    • Nuclear-export-signal-dependent protein translocation of dUTPase encoded by Singapore grouper iridovirus
    • Gong J, Huang YH, Huang XH, Zhang R, Qin QW, (2010) Nuclear-export-signal-dependent protein translocation of dUTPase encoded by Singapore grouper iridovirus. Arch Virol 155: 1069-1076.
    • (2010) Arch Virol , vol.155 , pp. 1069-1076
    • Gong, J.1    Huang, Y.H.2    Huang, X.H.3    Zhang, R.4    Qin, Q.W.5
  • 30
    • 0025800039 scopus 로고
    • Proteolysis of nuclear proteins by mu-calpain and m-calpain
    • Mellgren RL, (1991) Proteolysis of nuclear proteins by mu-calpain and m-calpain. J Biol Chem 266: 13920-13924.
    • (1991) J Biol Chem , vol.266 , pp. 13920-13924
    • Mellgren, R.L.1
  • 31
  • 32
  • 34
    • 3042822256 scopus 로고    scopus 로고
    • M-Calpain implication in cell cycle during muscle precursor cell activation
    • Raynaud F, Carnac G, Marcilhac A, Benyamin Y, (2004) m-Calpain implication in cell cycle during muscle precursor cell activation. Exp Cell Res 298: 48-57.
    • (2004) Exp Cell Res , vol.298 , pp. 48-57
    • Raynaud, F.1    Carnac, G.2    Marcilhac, A.3    Benyamin, Y.4
  • 35
    • 0027416049 scopus 로고
    • In vivo inhibition of cyclin B degradation and induction of cell-cycle arrest in mammalian cells by the neutral cysteine protease inhibitor N-acetylleucylleucylnorleucinal
    • Sherwood SW, Kung AL, Roitelman J, Simoni RD, Schimke RT, (1993) In vivo inhibition of cyclin B degradation and induction of cell-cycle arrest in mammalian cells by the neutral cysteine protease inhibitor N-acetylleucylleucylnorleucinal. Proc Natl Acad Sci U S A 90: 3353-3357.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 3353-3357
    • Sherwood, S.W.1    Kung, A.L.2    Roitelman, J.3    Simoni, R.D.4    Schimke, R.T.5
  • 36
    • 33646240050 scopus 로고    scopus 로고
    • Functional proteomics of resveratrol-induced colon cancer cell apoptosis: caspase-6-mediated cleavage of lamin A is a major signaling loop
    • Lee SC, Chan J, Clement MV, Pervaiz S, (2006) Functional proteomics of resveratrol-induced colon cancer cell apoptosis: caspase-6-mediated cleavage of lamin A is a major signaling loop. Proteomics 6: 2386-2394.
    • (2006) Proteomics , vol.6 , pp. 2386-2394
    • Lee, S.C.1    Chan, J.2    Clement, M.V.3    Pervaiz, S.4
  • 37
    • 0032561365 scopus 로고    scopus 로고
    • Identification of apoptosis-associated proteins in a human Burkitt lymphoma cell line. Cleavage of heterogeneous nuclear ribonucleoprotein A1 by caspase 3
    • Brockstedt E, Rickers A, Kostka S, Laubersheimer A, Dorken B, et al. (1998) Identification of apoptosis-associated proteins in a human Burkitt lymphoma cell line. Cleavage of heterogeneous nuclear ribonucleoprotein A1 by caspase 3. J Biol Chem 273: 28057-28064.
    • (1998) J Biol Chem , vol.273 , pp. 28057-28064
    • Brockstedt, E.1    Rickers, A.2    Kostka, S.3    Laubersheimer, A.4    Dorken, B.5
  • 38
    • 55149092516 scopus 로고    scopus 로고
    • Proteomic analysis of anti-tumor effects by Rhizoma Paridis total saponin treatment in HepG2 cells
    • Cheng ZX, Liu BR, Qian XP, Ding YT, Hu WJ, et al. (2008) Proteomic analysis of anti-tumor effects by Rhizoma Paridis total saponin treatment in HepG2 cells. J Ethnopharmacol 120: 129-137.
    • (2008) J Ethnopharmacol , vol.120 , pp. 129-137
    • Cheng, Z.X.1    Liu, B.R.2    Qian, X.P.3    Ding, Y.T.4    Hu, W.J.5
  • 39
    • 78650956818 scopus 로고    scopus 로고
    • Evidence for a second messenger function of dUTP during Bax mediated apoptosis of yeast and mammalian cells
    • Williams D, Norman G, Khoury C, Metcalfe N, Briard J, et al. (2011) Evidence for a second messenger function of dUTP during Bax mediated apoptosis of yeast and mammalian cells. Biochim Biophys Acta 1813: 315-321.
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 315-321
    • Williams, D.1    Norman, G.2    Khoury, C.3    Metcalfe, N.4    Briard, J.5
  • 40
    • 2442576938 scopus 로고    scopus 로고
    • Contribution of distinct structural elements to activation of calpain by Ca2+ ions
    • Alexa A, Bozoky Z, Farkas A, Tompa P, Friedrich P, (2004) Contribution of distinct structural elements to activation of calpain by Ca2+ ions. J Biol Chem 279: 20118-20126.
    • (2004) J Biol Chem , vol.279 , pp. 20118-20126
    • Alexa, A.1    Bozoky, Z.2    Farkas, A.3    Tompa, P.4    Friedrich, P.5
  • 41
    • 36349007726 scopus 로고    scopus 로고
    • Kinetic mechanism of human dUTPase, an essential nucleotide pyrophosphatase enzyme
    • Toth J, Varga B, Kovacs M, Malnasi-Csizmadia A, Vertessy BG, (2007) Kinetic mechanism of human dUTPase, an essential nucleotide pyrophosphatase enzyme. J Biol Chem 282: 33572-33582.
    • (2007) J Biol Chem , vol.282 , pp. 33572-33582
    • Toth, J.1    Varga, B.2    Kovacs, M.3    Malnasi-Csizmadia, A.4    Vertessy, B.G.5
  • 42
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM, (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 44
    • 0029874744 scopus 로고    scopus 로고
    • Specific derivatization of the active site tyrosine in dUTPase perturbs ligand binding to the active site
    • Vertessy BG, Persson R, Rosengren AM, Zeppezauer M, Nyman PO, (1996) Specific derivatization of the active site tyrosine in dUTPase perturbs ligand binding to the active site. Biochem Biophys Res Commun 219: 294-300.
    • (1996) Biochem Biophys Res Commun , vol.219 , pp. 294-300
    • Vertessy, B.G.1    Persson, R.2    Rosengren, A.M.3    Zeppezauer, M.4    Nyman, P.O.5
  • 45
    • 0141755212 scopus 로고    scopus 로고
    • dUTPase and nucleocapsid polypeptides of the Mason-Pfizer monkey virus form a fusion protein in the virion with homotrimeric organization and low catalytic efficiency
    • Barabas O, Rumlova M, Erdei A, Pongracz V, Pichova I, et al. (2003) dUTPase and nucleocapsid polypeptides of the Mason-Pfizer monkey virus form a fusion protein in the virion with homotrimeric organization and low catalytic efficiency. J Biol Chem 278: 38803-38812.
    • (2003) J Biol Chem , vol.278 , pp. 38803-38812
    • Barabas, O.1    Rumlova, M.2    Erdei, A.3    Pongracz, V.4    Pichova, I.5
  • 46


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