메뉴 건너뛰기




Volumn 5, Issue 2, 2006, Pages 262-271

Role of N-terminal hydrophobic region in modulating the subcellular localization and enzyme activity of the bisphosphate nucleotidase from Debaryomyces hansenii

Author keywords

[No Author keywords available]

Indexed keywords

BISPHOSPHOADENYLATE 3' NUCLEOTIDASE; BISPHOSPHOADENYLATE 3'-NUCLEOTIDASE; INORGANIC SALT; INOSITOL 1,4 DIPHOSPHATE 1 PHOSPHATASE; INOSITOL-1,4-BISPHOSPHATE 1-PHOSPHATASE; NUCLEOTIDASE; PHOSPHATASE;

EID: 32944476030     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.5.2.262-271.2006     Document Type: Article
Times cited : (19)

References (40)
  • 1
    • 18944364617 scopus 로고    scopus 로고
    • Molecular cloning and biochemical characterization of a 3′(2′),5′-bisphosphate nucleotidase from Debaryomyces hansenii
    • Aggarwal, M., P. K. Bansal, and A. K. Mondal. 2005. Molecular cloning and biochemical characterization of a 3′(2′),5′-bisphosphate nucleotidase from Debaryomyces hansenii. Yeast 22:457-470.
    • (2005) Yeast , vol.22 , pp. 457-470
    • Aggarwal, M.1    Bansal, P.K.2    Mondal, A.K.3
  • 2
    • 0034723159 scopus 로고    scopus 로고
    • X-ray structure of yeast Hal2p, a major target of lithium and sodium toxicity, and identification of framework interactions determining cation sensitivity
    • Albert, A., L. Yenush, M. R. Gill-Mascarell, P. L. Rodriguez, S. Patel, M. Martinez-Ripell, T. L. Blundell, and R. Serrano. 2000. X-ray structure of yeast Hal2p, a major target of lithium and sodium toxicity, and identification of framework interactions determining cation sensitivity. J. Mol. Biol. 295:927-938.
    • (2000) J. Mol. Biol. , vol.295 , pp. 927-938
    • Albert, A.1    Yenush, L.2    Gill-Mascarell, M.R.3    Rodriguez, P.L.4    Patel, S.5    Martinez-Ripell, M.6    Blundell, T.L.7    Serrano, R.8
  • 3
    • 0032483502 scopus 로고    scopus 로고
    • Expression of the yeast HAL2 gene in tomato increases the in vitro salt tolerance of transgenic progenies
    • Arrillaga, I., R. Gil-Mascarell, C. Gisbert, E. Sales, C. Montesinos, R. Serrano, and V. Moreno. 1998. Expression of the yeast HAL2 gene in tomato increases the in vitro salt tolerance of transgenic progenies. Plant Sci. 136:219-2268.
    • (1998) Plant Sci. , vol.136 , pp. 219-2268
    • Arrillaga, I.1    Gil-Mascarell, R.2    Gisbert, C.3    Sales, E.4    Montesinos, C.5    Serrano, R.6    Moreno, V.7
  • 4
    • 0034650216 scopus 로고    scopus 로고
    • Isolation and sequence of the HOG1 homologue from Debaryomyces hansenii by complementation of the hog1 delta strain of Saccharomyces cerevisiae
    • Bansal, P. K., and A. K. Mondal. 2000. Isolation and sequence of the HOG1 homologue from Debaryomyces hansenii by complementation of the hog1 delta strain of Saccharomyces cerevisiae. Yeast 16:81-88.
    • (2000) Yeast , vol.16 , pp. 81-88
    • Bansal, P.K.1    Mondal, A.K.2
  • 5
    • 0023922758 scopus 로고
    • Inorganic pyrophosphatase as a label in heterogeneous enzyme immunoassay
    • Baykov, A. A., O. A. Evtushenko, and S. M. Avaeva. 1988. Inorganic pyrophosphatase as a label in heterogeneous enzyme immunoassay. Anal. Biochem. 171:266-270.
    • (1988) Anal. Biochem. , vol.171 , pp. 266-270
    • Baykov, A.A.1    Evtushenko, O.A.2    Avaeva, S.M.3
  • 6
    • 0022972326 scopus 로고
    • Structure of yeast LEU4. The 5′ flanking region contains features that predict two modes of control and two productive translation starts
    • Beltzer, J. P., L. F. L. Chang, A. E. Hinkkanen, and G. B. Kohlhaw. 1986. Structure of yeast LEU4. The 5′ flanking region contains features that predict two modes of control and two productive translation starts. J. Biol. Chem. 261:5160-5167.
    • (1986) J. Biol. Chem. , vol.261 , pp. 5160-5167
    • Beltzer, J.P.1    Chang, L.F.L.2    Hinkkanen, A.E.3    Kohlhaw, G.B.4
  • 7
    • 0023902156 scopus 로고
    • The yeast VAS1 gene encodes both mitochondrial and cytoplasmic valyl-tRNA synthetases
    • Chatton, B., P. Walter, J. P. Ebel, F. Lacroute, and F. Fasiolo. 1988. The yeast VAS1 gene encodes both mitochondrial and cytoplasmic valyl-tRNA synthetases. J. Biol. Chem. 263:52-57.
    • (1988) J. Biol. Chem. , vol.263 , pp. 52-57
    • Chatton, B.1    Walter, P.2    Ebel, J.P.3    Lacroute, F.4    Fasiolo, F.5
  • 9
    • 0026471632 scopus 로고
    • HTS1 encodes both the cytoplasmic and mitochondrial histidyl-tRNA synthetase of Saccharomyces cerevisiae: Mutations alter the specificity of compartmentation
    • Chui, M. I., T. L. Mason, and G. R. Fink. 1992. HTS1 encodes both the cytoplasmic and mitochondrial histidyl-tRNA synthetase of Saccharomyces cerevisiae: mutations alter the specificity of compartmentation. Genetics 132:987-1001.
    • (1992) Genetics , vol.132 , pp. 987-1001
    • Chui, M.I.1    Mason, T.L.2    Fink, G.R.3
  • 10
    • 0032488032 scopus 로고    scopus 로고
    • The stress-activated phosphatidylinositol 3-phosphate 5-kinase Fab1p is essential for vacuole function in S. cerevisiae
    • Cooke, F. T., S. K. Dove, R. K. McEwen, G. Painter, A. B. Holmes, M. N. Hall, R. H. Michell, and P. J. Parker. 1998. The stress-activated phosphatidylinositol 3-phosphate 5-kinase Fab1p is essential for vacuole function in S. cerevisiae. Curr. Biol. 8:1219-1222.
    • (1998) Curr. Biol. , vol.8 , pp. 1219-1222
    • Cooke, F.T.1    Dove, S.K.2    McEwen, R.K.3    Painter, G.4    Holmes, A.B.5    Hall, M.N.6    Michell, R.H.7    Parker, P.J.8
  • 11
    • 0029561101 scopus 로고
    • A second osmosensing signal transduction pathway in yeast
    • Davenport, K. R., M. Sohaskey, Y. Kamada, and D. E. Levin. 1995. A second osmosensing signal transduction pathway in yeast. J. Biol. Chem. 270:30157-30161.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30157-30161
    • Davenport, K.R.1    Sohaskey, M.2    Kamada, Y.3    Levin, D.E.4
  • 12
    • 0030726285 scopus 로고    scopus 로고
    • Lithium toxicity in yeast is due to the inhibition of RNA processing enzymes
    • Dichtl, B., A. Stevens, and D. Tollervey. 1997. Lithium toxicity in yeast is due to the inhibition of RNA processing enzymes. EMBO J. 16:7184-7195.
    • (1997) EMBO J. , vol.16 , pp. 7184-7195
    • Dichtl, B.1    Stevens, A.2    Tollervey, D.3
  • 13
    • 0037189551 scopus 로고    scopus 로고
    • In Saccharomyces cerevisiae, the inositol polyphosphate kinase activity of Kcslp is required for resistance to salt stress, cell wall integrity, and vacuolar morphogenesis
    • Dubois, E., B. Scherens, F. Vierendeels, M. M. Ho, F. Messenguy, and S. B. Shears. 2002. In Saccharomyces cerevisiae, the inositol polyphosphate kinase activity of Kcslp is required for resistance to salt stress, cell wall integrity, and vacuolar morphogenesis. J. Biol. Chem. 277:23755-23763.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23755-23763
    • Dubois, E.1    Scherens, B.2    Vierendeels, F.3    Ho, M.M.4    Messenguy, F.5    Shears, S.B.6
  • 15
    • 0024602506 scopus 로고
    • Amino-terminal extension generated from an upstream AUG codon increases the efficiency of mitochondrial import of yeast N2,N2-dimethylguanosine-specific tRNA methyltransferases
    • Ellis, S. R., A. K. Hopper, and N. C. Martin. 1989. Amino-terminal extension generated from an upstream AUG codon increases the efficiency of mitochondrial import of yeast N2,N2-dimethylguanosine-specific tRNA methyltransferases. Mol. Cell. Biol. 9:1611-1620.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1611-1620
    • Ellis, S.R.1    Hopper, A.K.2    Martin, N.C.3
  • 16
    • 0032189837 scopus 로고    scopus 로고
    • Regulated nucleo/cytoplasmic exchange of HOG1 MAPK requires the importin beta homologs NMD5 and XPO1
    • Ferrigno, P., F. Posas, D. Koepp, H. Saito, and P. A. Silver. 1998. Regulated nucleo/cytoplasmic exchange of HOG1 MAPK requires the importin beta homologs NMD5 and XPO1. EMBO J. 17:5606-5614.
    • (1998) EMBO J. , vol.17 , pp. 5606-5614
    • Ferrigno, P.1    Posas, F.2    Koepp, D.3    Saito, H.4    Silver, P.A.5
  • 17
    • 0026731477 scopus 로고
    • A novel and conserved salt induced protein is an important determinant of salt tolerance in yeast
    • Gaxiola, R., I. F. de Larrinoa, J. M. Villalba, and R. Serrano. 1992. A novel and conserved salt induced protein is an important determinant of salt tolerance in yeast. EMBO J. 11:3157-3164.
    • (1992) EMBO J. , vol.11 , pp. 3157-3164
    • Gaxiola, R.1    De Larrinoa, I.F.2    Villalba, J.M.3    Serrano, R.4
  • 18
    • 0040888719 scopus 로고    scopus 로고
    • The Arabidopsis thaliana HAL2-like gene family includes a novel sodium-sensitive phosphatase
    • Gil-Mascarell, R., J. M. Lopez-Coronado, J. M. Belles, R. Serrano, and P. L. Rodriguez. 1999. The Arabidopsis thaliana HAL2-like gene family includes a novel sodium-sensitive phosphatase. Plant J. 17:373-383.
    • (1999) Plant J. , vol.17 , pp. 373-383
    • Gil-Mascarell, R.1    Lopez-Coronado, J.M.2    Belles, J.M.3    Serrano, R.4    Rodriguez, P.L.5
  • 19
    • 0027328991 scopus 로고
    • Salt tolerance and methionine biosynthesis in Saccharomyces cerevisiae involves a putative phosphatase gene
    • Glaser, H. V., D. Thomas, H. Gaxiola, F. Montrichard, Y. Surdin-Kerjan, and R. Serrano. 1993. Salt tolerance and methionine biosynthesis in Saccharomyces cerevisiae involves a putative phosphatase gene. EMBO J. 12:3105-3110.
    • (1993) EMBO J. , vol.12 , pp. 3105-3110
    • Glaser, H.V.1    Thomas, D.2    Gaxiola, H.3    Montrichard, F.4    Surdin-Kerjan, Y.5    Serrano, R.6
  • 20
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 21
    • 0039772523 scopus 로고    scopus 로고
    • A novel mammalian lithium-sensitive enzyme with a dual enzymatic activity, 3′-phosphoadenosine 5′-phosphate phosphatase and inositol-polyphosphate 1-phosphatase
    • Lopez-Coronado, J. M., J. M. Belles, F. Lesage, R. Serrano, and P. L. Rodriguez. 1999. A novel mammalian lithium-sensitive enzyme with a dual enzymatic activity, 3′-phosphoadenosine 5′-phosphate phosphatase and inositol-polyphosphate 1-phosphatase. J. Biol. Chem. 274:16034-16039.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16034-16039
    • Lopez-Coronado, J.M.1    Belles, J.M.2    Lesage, F.3    Serrano, R.4    Rodriguez, P.L.5
  • 22
    • 0028953840 scopus 로고
    • Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds
    • Mumberg, D., R. Muller, and M. Funk. 1995. Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds. Gene 156:119-122.
    • (1995) Gene , vol.156 , pp. 119-122
    • Mumberg, D.1    Muller, R.2    Funk, M.3
  • 23
    • 0028912113 scopus 로고
    • A salt sensitive 3′(2′),5′-bisphosphate nucleotidase involved in sulfate activation
    • Murguia, J. R., J. M. Belles, and R. Serrano. 1995. A salt sensitive 3′(2′),5′-bisphosphate nucleotidase involved in sulfate activation. Science 267:232-234.
    • (1995) Science , vol.267 , pp. 232-234
    • Murguia, J.R.1    Belles, J.M.2    Serrano, R.3
  • 24
    • 0029824147 scopus 로고    scopus 로고
    • The yeast HAL2 nucleotidase is an in vivo target of salt toxicity
    • Murguia, J. R., J. M. Belles, and R. Serrano. 1996. The yeast HAL2 nucleotidase is an in vivo target of salt toxicity. J. Biol. Chem. 271:29029-29033.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29029-29033
    • Murguia, J.R.1    Belles, J.M.2    Serrano, R.3
  • 25
    • 0037470455 scopus 로고    scopus 로고
    • Yeast inositol mono- and trisphosphate levels are modulated by inositol monophosphatase activity and nutrients
    • Navarro-Avino, J. P., J. M. Belles, and R. Serrano. 2003. Yeast inositol mono- and trisphosphate levels are modulated by inositol monophosphatase activity and nutrients. Biochem. Biophys. Res. Comm. 302:41-45.
    • (2003) Biochem. Biophys. Res. Comm. , vol.302 , pp. 41-45
    • Navarro-Avino, J.P.1    Belles, J.M.2    Serrano, R.3
  • 27
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., J. Engelbrecht, S. Brunak, and G. von Heijne. 1997. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 28
    • 0030040689 scopus 로고    scopus 로고
    • Regulation of organelle biogenesis
    • Nunnari, J., and P. Walter. 1996. Regulation of organelle biogenesis. Cell 84:389-394.
    • (1996) Cell , vol.84 , pp. 389-394
    • Nunnari, J.1    Walter, P.2
  • 29
    • 0034677903 scopus 로고    scopus 로고
    • A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control
    • Odom, A. R., A. Stahlberg, S. R. Wente, and J. D. York. 2000. A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control. Science 287:2026-2029.
    • (2000) Science , vol.287 , pp. 2026-2029
    • Odom, A.R.1    Stahlberg, A.2    Wente, S.R.3    York, J.D.4
  • 30
    • 0028858093 scopus 로고
    • +-sensitive 3′(2′)5′-diphosphonucleoside 3′(2′)- phosphohydrolase and complements yeast met22 and Eschenchia coli cysQ mutations
    • +-sensitive 3′(2′)5′-diphosphonucleoside 3′(2′)-phosphohydrolase and complements yeast met22 and Eschenchia coli cysQ mutations. J. Biol. Chem. 270:29105-29110.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29105-29110
    • Peng, Z.1    Verma, D.P.S.2
  • 31
    • 0030099036 scopus 로고    scopus 로고
    • The SAL1 gene of Arabidopsis, encoding an enzyme with 3′(2′),5′-bisphosphate nucleotidase and inositol polyphosphate 1-phosphatase activities, increases salt tolerance in yeast
    • Quintero, F. J., B. Garciadeblas, and A. Rodriguez-Navarro. 1996. The SAL1 gene of Arabidopsis, encoding an enzyme with 3′(2′),5′- bisphosphate nucleotidase and inositol polyphosphate 1-phosphatase activities, increases salt tolerance in yeast. Plant Cell 8:529-537.
    • (1996) Plant Cell , vol.8 , pp. 529-537
    • Quintero, F.J.1    Garciadeblas, B.2    Rodriguez-Navarro, A.3
  • 32
    • 0024338964 scopus 로고
    • KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene
    • Rose, M. D., L. M. Misra, and J. P. Vogel. 1989. KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene. Cell 57:1121-1221.
    • (1989) Cell , vol.57 , pp. 1121-1221
    • Rose, M.D.1    Misra, L.M.2    Vogel, J.P.3
  • 33
    • 15144348732 scopus 로고    scopus 로고
    • 3′-Phosphorylated nucleotides are tight binding inhibitors of nucleoside diphosphate kinase activity
    • Schneider, B., Y. W. Xu, J. Janin, M. Veron, and D. Deville-Bonne. 1998. 3′-Phosphorylated nucleotides are tight binding inhibitors of nucleoside diphosphate kinase activity. J. Biol. Chem. 273:28773-28778.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28773-28778
    • Schneider, B.1    Xu, Y.W.2    Janin, J.3    Veron, M.4    Deville-Bonne, D.5
  • 34
    • 0029922104 scopus 로고    scopus 로고
    • Salt tolerance in plants and microorganisms: Toxicity targets and defense responses
    • Serrano, R. 1996. Salt tolerance in plants and microorganisms: toxicity targets and defense responses. Int. Rev. Cytol. 165:1-52.
    • (1996) Int. Rev. Cytol. , vol.165 , pp. 1-52
    • Serrano, R.1
  • 35
    • 0033532046 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian lithium sensitive bisphosphate 3′-nucleotidase inhibited by Inosiotol-1,4-bisphosphate
    • Spiegelberg, B. D., J. P. Xiong, J. J. Smith, R. F. Gu, and J. D. York. 1999. Cloning and characterization of a mammalian lithium sensitive bisphosphate 3′-nucleotidase inhibited by Inosiotol-1,4-bisphosphate. J. Biol. Chem. 274:13619-13628.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13619-13628
    • Spiegelberg, B.D.1    Xiong, J.P.2    Smith, J.J.3    Gu, R.F.4    York, J.D.5
  • 36
    • 0031457095 scopus 로고    scopus 로고
    • Metabolism of sulfur amino acids in Saccharomyces cerevisiae
    • Thomas, D., and Y. Surdin-Kerjan. 1997. Metabolism of sulfur amino acids in Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 61:503-532.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 503-532
    • Thomas, D.1    Surdin-Kerjan, Y.2
  • 37
    • 0023645433 scopus 로고
    • Mitochondrial and cytoplasmic fumarases in Saccharomyces cerevisiae are encoded by a single nuclear gene FUM1
    • Wu, M., and A. Tzagoloff. 1987. Mitochondrial and cytoplasmic fumarases in Saccharomyces cerevisiae are encoded by a single nuclear gene FUM1. J. Biol. Chem. 262:12275-12282.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12275-12282
    • Wu, M.1    Tzagoloff, A.2
  • 38
    • 0035423770 scopus 로고    scopus 로고
    • FIERY1 encoding an inositol polyphosphate 1-phosphatase is a negative regulator of abscisic acid and stress signaling in Arabidopsis
    • Xiong, L., B. Lee, M. Ishitani, H. Lee, C. Zhang, and J. K. Zhu. 2001. FIERY1 encoding an inositol polyphosphate 1-phosphatase is a negative regulator of abscisic acid and stress signaling in Arabidopsis. Genes Dev. 15:1971-1984.
    • (2001) Genes Dev. , vol.15 , pp. 1971-1984
    • Xiong, L.1    Lee, B.2    Ishitani, M.3    Lee, H.4    Zhang, C.5    Zhu, J.K.6
  • 40
    • 0346668323 scopus 로고    scopus 로고
    • Erf4p and Erf2p form an endoplasmic reticulum-associated complex involved in the plasma membrane localization of yeast Ras proteins
    • Zhao, L., S. Lobo, X. Dong, A. D. Ault, and R. Deschenes. 2002. Erf4p and Erf2p form an endoplasmic reticulum-associated complex involved in the plasma membrane localization of yeast Ras proteins. J. Biol. Chem. 277:49352-49359.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49352-49359
    • Zhao, L.1    Lobo, S.2    Dong, X.3    Ault, A.D.4    Deschenes, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.