메뉴 건너뛰기




Volumn 8, Issue 5, 2013, Pages

Expression of Bovine Cytosolic 5′-Nucleotidase (cN-II) in Yeast: Nucleotide Pools Disturbance and Its Consequences on Growth and Homologous Recombination

Author keywords

[No Author keywords available]

Indexed keywords

5' NUCLEOTIDASE; CYTOSOLIC 5' NUCLEOTIDASE II; PURINE DERIVATIVE; PYRIMIDINE DERIVATIVE; UNCLASSIFIED DRUG; NUCLEOTIDE; PRIMER DNA;

EID: 84877865749     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0063914     Document Type: Article
Times cited : (14)

References (37)
  • 1
    • 0027274023 scopus 로고
    • IMP-GMP 5′-nucleotidase
    • Itoh R, (1993) IMP-GMP 5′-nucleotidase. Comp Biochem Physiol B 105: 13-19.
    • (1993) Comp Biochem Physiol B , vol.105 , pp. 13-19
    • Itoh, R.1
  • 2
    • 0344443811 scopus 로고    scopus 로고
    • Mammalian 5′-nucleotidases
    • Bianchi V, Spychala J, (2003) Mammalian 5′-nucleotidases. J Biol Chem 278: 46195-46198.
    • (2003) J Biol Chem , vol.278 , pp. 46195-46198
    • Bianchi, V.1    Spychala, J.2
  • 3
    • 0026701617 scopus 로고
    • A comparative study on tissue distribution and metabolic adaptation of IMP-GMP 5′-nucleotidase
    • Itoh R, Echizen H, Higuchi M, Oka J, Yamada K, (1992) A comparative study on tissue distribution and metabolic adaptation of IMP-GMP 5′-nucleotidase. Comp Biochem Physiol B 103: 153-159.
    • (1992) Comp Biochem Physiol B , vol.103 , pp. 153-159
    • Itoh, R.1    Echizen, H.2    Higuchi, M.3    Oka, J.4    Yamada, K.5
  • 4
    • 0031807603 scopus 로고    scopus 로고
    • Identification of multiple forms of the cytosolic 5′-nucleotidase/phosphotransferase in rat tissues
    • Pesi R, Allegrini S, Golfarini S, Baiocchi C, Moretti E, et al. (1998) Identification of multiple forms of the cytosolic 5′-nucleotidase/phosphotransferase in rat tissues. Adv Exp Med Biol 431: 495-499.
    • (1998) Adv Exp Med Biol , vol.431 , pp. 495-499
    • Pesi, R.1    Allegrini, S.2    Golfarini, S.3    Baiocchi, C.4    Moretti, E.5
  • 5
    • 33845218744 scopus 로고    scopus 로고
    • Recent advances in structure and function of cytosolic IMP-GMP specific 5′-nucleotidase II (cN-II)
    • Ipata PL, Tozzi MG, (2006) Recent advances in structure and function of cytosolic IMP-GMP specific 5′-nucleotidase II (cN-II). Purinergic Signal 2: 669-675.
    • (2006) Purinergic Signal , vol.2 , pp. 669-675
    • Ipata, P.L.1    Tozzi, M.G.2
  • 6
    • 34547124338 scopus 로고    scopus 로고
    • Crystal structure of human cytosolic 5′-nucleotidase II: insights into allosteric regulation and substrate recognition
    • Wallden K, Stenmark P, Nyman T, Flodin S, Graslund S, et al. (2007) Crystal structure of human cytosolic 5′-nucleotidase II: insights into allosteric regulation and substrate recognition. J Biol Chem 282: 17828-17836.
    • (2007) J Biol Chem , vol.282 , pp. 17828-17836
    • Wallden, K.1    Stenmark, P.2    Nyman, T.3    Flodin, S.4    Graslund, S.5
  • 7
    • 0033125735 scopus 로고    scopus 로고
    • Human high-Km 5′-nucleotidase effects of overexpression of the cloned cDNA in cultured human cells
    • Rampazzo C, Gazziola C, Ferraro P, Gallinaro L, Johansson M, et al. (1999) Human high-Km 5′-nucleotidase effects of overexpression of the cloned cDNA in cultured human cells. Eur J Biochem 261: 689-697.
    • (1999) Eur J Biochem , vol.261 , pp. 689-697
    • Rampazzo, C.1    Gazziola, C.2    Ferraro, P.3    Gallinaro, L.4    Johansson, M.5
  • 8
    • 46549084491 scopus 로고    scopus 로고
    • Knockdown of cytosolic 5′-nucleotidase II (cN-II) reveals that its activity is essential for survival in astrocytoma cells
    • Careddu MG, Allegrini S, Pesi R, Camici M, Garcia-Gil M, et al. (2008) Knockdown of cytosolic 5′-nucleotidase II (cN-II) reveals that its activity is essential for survival in astrocytoma cells. Biochim Biophys Acta 1783: 1529-1535.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 1529-1535
    • Careddu, M.G.1    Allegrini, S.2    Pesi, R.3    Camici, M.4    Garcia-Gil, M.5
  • 9
    • 0242485936 scopus 로고    scopus 로고
    • ATP and phosphate reciprocally affect subunit association of human recombinant High Km 5′-nucleotidase. Role for the C-terminal polyglutamic acid tract in subunit association and catalytic activity
    • Spychala J, Chen V, Oka J, Mitchell BS, (1999) ATP and phosphate reciprocally affect subunit association of human recombinant High Km 5′-nucleotidase. Role for the C-terminal polyglutamic acid tract in subunit association and catalytic activity. Eur J Biochem 259: 851-858.
    • (1999) Eur J Biochem , vol.259 , pp. 851-858
    • Spychala, J.1    Chen, V.2    Oka, J.3    Mitchell, B.S.4
  • 10
    • 0030724497 scopus 로고    scopus 로고
    • Bovine cytosolic IMP/GMP-specific 5′-nucleotidase: cloning and expression of active enzyme in Escherichia coli
    • Allegrini S, Pesi R, Tozzi MG, Fiol CJ, Johnson RB, et al. (1997) Bovine cytosolic IMP/GMP-specific 5′-nucleotidase: cloning and expression of active enzyme in Escherichia coli. Biochem J 328 (Pt 2): 483-487.
    • (1997) Biochem J , vol.328 , Issue.Pt 2 , pp. 483-487
    • Allegrini, S.1    Pesi, R.2    Tozzi, M.G.3    Fiol, C.J.4    Johnson, R.B.5
  • 11
    • 0028219935 scopus 로고
    • Purification and some properties of an IMP-specific 5′-nucleotidase from yeast
    • Itoh R, (1994) Purification and some properties of an IMP-specific 5′-nucleotidase from yeast. Biochem J 298 Pt 3: 593-598.
    • (1994) Biochem J , vol.298 , Issue.Pt 3 , pp. 593-598
    • Itoh, R.1
  • 12
  • 13
    • 34548356520 scopus 로고    scopus 로고
    • ISN1 nucleotidases and HAD superfamily protein fold: in silico sequence and structure analysis
    • Srinivasan B, Balaram H, (2007) ISN1 nucleotidases and HAD superfamily protein fold: in silico sequence and structure analysis. In Silico Biol 7: 0019.
    • (2007) In Silico Biol , vol.7 , pp. 0019
    • Srinivasan, B.1    Balaram, H.2
  • 14
    • 11244341002 scopus 로고    scopus 로고
    • Mechanistic studies on bovine cytosolic 5′-nucleotidase II, an enzyme belonging to the HAD superfamily
    • Allegrini S, Scaloni A, Careddu MG, Cuccu G, D'Ambrosio C, et al. (2004) Mechanistic studies on bovine cytosolic 5′-nucleotidase II, an enzyme belonging to the HAD superfamily. Eur J Biochem 271: 4881-4891.
    • (2004) Eur J Biochem , vol.271 , pp. 4881-4891
    • Allegrini, S.1    Scaloni, A.2    Careddu, M.G.3    Cuccu, G.4    D'Ambrosio, C.5
  • 15
    • 0037077298 scopus 로고    scopus 로고
    • SDT1/SSM1, a multicopy suppressor of S-II null mutant, encodes a novel pyrimidine 5′-nucleotidase
    • Nakanishi T, Sekimizu K, (2002) SDT1/SSM1, a multicopy suppressor of S-II null mutant, encodes a novel pyrimidine 5′-nucleotidase. J Biol Chem 277: 22103-22106.
    • (2002) J Biol Chem , vol.277 , pp. 22103-22106
    • Nakanishi, T.1    Sekimizu, K.2
  • 16
    • 0023665902 scopus 로고
    • An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs
    • Kozak M, (1987) An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res 15: 8125-8148.
    • (1987) Nucleic Acids Res , vol.15 , pp. 8125-8148
    • Kozak, M.1
  • 17
    • 0028978607 scopus 로고
    • On the mechanism of UV and gamma-ray-induced intrachromosomal recombination in yeast cells synchronized in different stages of the cell cycle
    • Galli A, Schiestl RH, (1995) On the mechanism of UV and gamma-ray-induced intrachromosomal recombination in yeast cells synchronized in different stages of the cell cycle. Mol Gen Genet 248: 301-310.
    • (1995) Mol Gen Genet , vol.248 , pp. 301-310
    • Galli, A.1    Schiestl, R.H.2
  • 19
    • 34347206860 scopus 로고    scopus 로고
    • High-efficiency yeast transformation using the LiAc/SS carrier DNA/PEG method
    • Gietz RD, Schiestl RH, (2007) High-efficiency yeast transformation using the LiAc/SS carrier DNA/PEG method. Nat Protoc 2: 31-34.
    • (2007) Nat Protoc , vol.2 , pp. 31-34
    • Gietz, R.D.1    Schiestl, R.H.2
  • 20
    • 0027934847 scopus 로고
    • The bifunctional cytosolic 5′-nucleotidase: regulation of the phosphotransferase and nucleotidase activities
    • Pesi R, Turriani M, Allegrini S, Scolozzi C, Camici M, et al. (1994) The bifunctional cytosolic 5′-nucleotidase: regulation of the phosphotransferase and nucleotidase activities. Arch Biochem Biophys 312: 75-80.
    • (1994) Arch Biochem Biophys , vol.312 , pp. 75-80
    • Pesi, R.1    Turriani, M.2    Allegrini, S.3    Scolozzi, C.4    Camici, M.5
  • 21
    • 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
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0032856295 scopus 로고    scopus 로고
    • Cell division transforms mutagenic lesions into deletion-recombinagenic lesions in yeast cells
    • Galli A, Schiestl RH, (1999) Cell division transforms mutagenic lesions into deletion-recombinagenic lesions in yeast cells. Mutat Res 429: 13-26.
    • (1999) Mutat Res , vol.429 , pp. 13-26
    • Galli, A.1    Schiestl, R.H.2
  • 24
    • 69749110125 scopus 로고    scopus 로고
    • Quantitative evaluation of intracellular metabolite extraction techniques for yeast metabolomics
    • Canelas AB, ten Pierick A, Ras C, Seifar RM, van Dam JC, et al. (2009) Quantitative evaluation of intracellular metabolite extraction techniques for yeast metabolomics. Anal Chem 81: 7379-7389.
    • (2009) Anal Chem , vol.81 , pp. 7379-7389
    • Canelas, A.B.1    ten Pierick, A.2    Ras, C.3    Seifar, R.M.4    van Dam, J.C.5
  • 25
    • 0020669405 scopus 로고
    • Determination of total Protein (Lowry Modified)
    • 1983/01/01 ed
    • Peterson GL (1983) Determination of total Protein (Lowry Modified). Methods Enzymol- Enzyme structure Part I. 1983/01/01 ed. 95-104.
    • (1983) Methods Enzymol - Enzyme structure , pp. 95-104
    • Peterson, G.L.1
  • 26
    • 33846944332 scopus 로고    scopus 로고
    • Capillary electrophoretic method for nucleotide analysis in cells: application on inherited metabolic disorders
    • Friedecky D, Tomkova J, Maier V, Janost'akova A, Prochazka M, et al. (2007) Capillary electrophoretic method for nucleotide analysis in cells: application on inherited metabolic disorders. Electrophoresis 28: 373-380.
    • (2007) Electrophoresis , vol.28 , pp. 373-380
    • Friedecky, D.1    Tomkova, J.2    Maier, V.3    Janost'akova, A.4    Prochazka, M.5
  • 27
    • 0035823603 scopus 로고    scopus 로고
    • Bovine cytosolic 5′-nucleotidase acts through the formation of an aspartate 52-phosphoenzyme intermediate
    • Allegrini S, Scaloni A, Ferrara L, Pesi R, Pinna P, et al. (2001) Bovine cytosolic 5′-nucleotidase acts through the formation of an aspartate 52-phosphoenzyme intermediate. J Biol Chem 276: 33526-33532.
    • (2001) J Biol Chem , vol.276 , pp. 33526-33532
    • Allegrini, S.1    Scaloni, A.2    Ferrara, L.3    Pesi, R.4    Pinna, P.5
  • 28
    • 36949000462 scopus 로고    scopus 로고
    • Identification of the nucleotidase responsible for the AMP hydrolysing hyperactivity associated with neurological and developmental disorders
    • Pesi R, Camici M, Micheli V, Notarantonio L, Jacomelli G, et al. (2008) Identification of the nucleotidase responsible for the AMP hydrolysing hyperactivity associated with neurological and developmental disorders. Neurochem Res 33: 59-65.
    • (2008) Neurochem Res , vol.33 , pp. 59-65
    • Pesi, R.1    Camici, M.2    Micheli, V.3    Notarantonio, L.4    Jacomelli, G.5
  • 29
    • 18244376808 scopus 로고    scopus 로고
    • Homeostatic adjustment and metabolic remodeling in glucose-limited yeast cultures
    • Brauer MJ, Saldanha AJ, Dolinski K, Botstein D, (2005) Homeostatic adjustment and metabolic remodeling in glucose-limited yeast cultures. Mol Biol Cell 16: 2503-2517.
    • (2005) Mol Biol Cell , vol.16 , pp. 2503-2517
    • Brauer, M.J.1    Saldanha, A.J.2    Dolinski, K.3    Botstein, D.4
  • 30
    • 0033857139 scopus 로고    scopus 로고
    • Can yeast glycolysis be understood in terms of in vitro kinetics of the constituent enzymes? Testing biochemistry
    • Teusink B, Passarge J, Reijenga CA, Esgalhado E, van der Weijden CC, et al. (2000) Can yeast glycolysis be understood in terms of in vitro kinetics of the constituent enzymes? Testing biochemistry. Eur J Biochem 267: 5313-5329.
    • (2000) Eur J Biochem , vol.267 , pp. 5313-5329
    • Teusink, B.1    Passarge, J.2    Reijenga, C.A.3    Esgalhado, E.4    van der Weijden, C.C.5
  • 31
    • 38449110592 scopus 로고    scopus 로고
    • SNF1/AMPK pathways in yeast
    • Hedbacker K, Carlson M, (2008) SNF1/AMPK pathways in yeast. Front Biosci 13: 2408-2420.
    • (2008) Front Biosci , vol.13 , pp. 2408-2420
    • Hedbacker, K.1    Carlson, M.2
  • 33
    • 0038026009 scopus 로고    scopus 로고
    • The purine nucleoside cycle in cell-free extracts of rat brain: evidence for the occurrence of an inosine and a guanosine cycle with distinct metabolic roles
    • Barsotti C, Pesi R, Felice F, Ipata PL, (2003) The purine nucleoside cycle in cell-free extracts of rat brain: evidence for the occurrence of an inosine and a guanosine cycle with distinct metabolic roles. Cell Mol Life Sci 60: 786-793.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 786-793
    • Barsotti, C.1    Pesi, R.2    Felice, F.3    Ipata, P.L.4
  • 34
    • 76149092853 scopus 로고    scopus 로고
    • Control of ATP homeostasis during the respiro-fermentative transition in yeast
    • Walther T, Novo M, Rossger K, Letisse F, Loret MO, et al. (2010) Control of ATP homeostasis during the respiro-fermentative transition in yeast. Mol Syst Biol 6: 344.
    • (2010) Mol Syst Biol , vol.6 , pp. 344
    • Walther, T.1    Novo, M.2    Rossger, K.3    Letisse, F.4    Loret, M.O.5
  • 35
    • 0033572753 scopus 로고    scopus 로고
    • Induction of human high KM 5′-nucleotidase in cultured 293 cells
    • Gazziola C, Moras M, Ferraro P, Gallinaro L, Verin R, et al. (1999) Induction of human high KM 5′-nucleotidase in cultured 293 cells. Exp Cell Res 253: 474-482.
    • (1999) Exp Cell Res , vol.253 , pp. 474-482
    • Gazziola, C.1    Moras, M.2    Ferraro, P.3    Gallinaro, L.4    Verin, R.5
  • 36
    • 0031810672 scopus 로고    scopus 로고
    • Yeast carbon catabolite repression
    • Gancedo JM, (1998) Yeast carbon catabolite repression. Microbiol Mol Biol Rev 62: 334-361.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 334-361
    • Gancedo, J.M.1
  • 37
    • 3242892765 scopus 로고    scopus 로고
    • DSB repair: the yeast paradigm
    • Aylon Y, Kupiec M, (2004) DSB repair: the yeast paradigm. DNA Repair (Amst) 3: 797-815.
    • (2004) DNA Repair (Amst) , vol.3 , pp. 797-815
    • Aylon, Y.1    Kupiec, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.