메뉴 건너뛰기




Volumn 182, Issue 13, 2000, Pages 3619-3625

Tol1, a fission yeast phosphomonoesterase, is an in vivo target of lithium, and its deletion leads to sulfite auxotrophy

Author keywords

[No Author keywords available]

Indexed keywords

INOSITOL POLYPHOSPHATE; LITHIUM; PHOSPHATASE; SULFITE;

EID: 0034086732     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.13.3619-3625.2000     Document Type: Article
Times cited : (16)

References (37)
  • 1
    • 0031438616 scopus 로고    scopus 로고
    • Regulation of salt tolerance in fission yeast by a protein-phosphatase-Z-like Ser/ Thr protein phosphatase
    • Balcells, L., N. Gomez, A. Casamayor, J. Clotet, and J. Arino. 1997. Regulation of salt tolerance in fission yeast by a protein-phosphatase-Z-like Ser/ Thr protein phosphatase. Eur. J. Biochem. 250:476-483.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 476-483
    • Balcells, L.1    Gomez, N.2    Casamayor, A.3    Clotet, J.4    Arino, J.5
  • 2
    • 0027441494 scopus 로고
    • TATA box mutations in the Schizosaccharomyces pombe nmtl promoter affect transcription efficiency hut not the transcription start point or thiamine repressibility
    • Basi, G., E. Schmid, and K. Maundrell. 1993. TATA box mutations in the Schizosaccharomyces pombe nmtl promoter affect transcription efficiency hut not the transcription start point or thiamine repressibility. Gene 123:131-136.
    • (1993) Gene , vol.123 , pp. 131-136
    • Basi, G.1    Schmid, E.2    Maundrell, K.3
  • 3
    • 0020410160 scopus 로고
    • Construction of a Schizosaccharomyces pombe gene bank in a yeast bacterial shuttle vector and its use to isolate genes by complementation
    • Beach, D., M. Piper, and P. Nurse. 1982. Construction of a Schizosaccharomyces pombe gene bank in a yeast bacterial shuttle vector and its use to isolate genes by complementation. Mol. Gen. Genet. 187:326-329.
    • (1982) Mol. Gen. Genet. , vol.187 , pp. 326-329
    • Beach, D.1    Piper, M.2    Nurse, P.3
  • 4
    • 0024341795 scopus 로고
    • Neural and developmental actions of lithium: A unifying hypothesis
    • Berridge, M. J., C. P. Downes, and M. R. Hanley. 1989. Neural and developmental actions of lithium: a unifying hypothesis. Cell 59:411-419.
    • (1989) Cell , vol.59 , pp. 411-419
    • Berridge, M.J.1    Downes, C.P.2    Hanley, M.R.3
  • 5
    • 0028136974 scopus 로고
    • Sulfur amino acid metabolism in Schizosaccharomyces pombe: Occurrence of two O-acetylhomoserine sulfhydrylases and the lack of the reverse transsulfuration pathway
    • Brzywczy, J., and A. Paszewski. 1994. Sulfur amino acid metabolism in Schizosaccharomyces pombe: occurrence of two O-acetylhomoserine sulfhydrylases and the lack of the reverse transsulfuration pathway. FEMS Microbiol. Lett. 121:171-174.
    • (1994) FEMS Microbiol. Lett. , vol.121 , pp. 171-174
    • Brzywczy, J.1    Paszewski, A.2
  • 6
    • 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
  • 7
    • 0026006263 scopus 로고
    • A novel P-type ATPase from yeast involved in sodium transport
    • Haro, R., B. Garciadeblas, and N. A. Rodriguez. 1991. A novel P-type ATPase from yeast involved in sodium transport. FEBS Lett. 291:189-191.
    • (1991) FEBS Lett. , vol.291 , pp. 189-191
    • Haro, R.1    Garciadeblas, B.2    Rodriguez, N.A.3
  • 8
    • 0017409146 scopus 로고
    • Control of arylsulfatase in a serine auxotroph of Neurospora
    • Jacobson, E. S., and R. L. Metzenberg. 1977. Control of arylsulfatase in a serine auxotroph of Neurospora. J. Bacteriol. 130:1397-1398.
    • (1977) J. Bacteriol. , vol.130 , pp. 1397-1398
    • Jacobson, E.S.1    Metzenberg, R.L.2
  • 9
    • 0026533592 scopus 로고
    • Gene amplification at a locus encoding a putative Na+/H+ antiporter confers sodium and lithium tolerance in fission yeast
    • Jia, Z. P., N. McCullough, R. Martel, S. Hemmingsen, and P. G. Young. 1992. Gene amplification at a locus encoding a putative Na+/H+ antiporter confers sodium and lithium tolerance in fission yeast. EMBO J. 11:1631-1640.
    • (1992) EMBO J. , vol.11 , pp. 1631-1640
    • Jia, Z.P.1    McCullough, N.2    Martel, R.3    Hemmingsen, S.4    Young, P.G.5
  • 10
    • 0029776032 scopus 로고    scopus 로고
    • A molecular mechanism for the effect of lithium on development
    • Klein, P. S., and D. A. Melton. 1996. A molecular mechanism for the effect of lithium on development. Proc. Natl. Acad. Sci. USA 93:8455-8459.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8455-8459
    • Klein, P.S.1    Melton, D.A.2
  • 11
    • 0027722019 scopus 로고
    • Ziskind-Somerfeld Research Award 1993. Biochemical, behavioral, and clinical studies of the role of inositol in lithium treatment and depression
    • Kofman, O., and R. H. Belmaker. 1993. Ziskind-Somerfeld Research Award 1993. Biochemical, behavioral, and clinical studies of the role of inositol in lithium treatment and depression. Biol. Psychiatry 34:839-852.
    • (1993) Biol. Psychiatry , vol.34 , pp. 839-852
    • Kofman, O.1    Belmaker, R.H.2
  • 12
    • 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, C. J., 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, C.J.1    Belles, J.M.2    Lesage, F.3    Serrano, R.4    Rodriguez, P.L.5
  • 13
    • 0033067784 scopus 로고    scopus 로고
    • The yeast inositol monophosphatase is a lithium-and sodium-sensitive enzyme encoded by a non-essential gene pair
    • Lopez, F., M. Leube, M. R. Gil, A. J. Navarro, and R. Serrano. 1999. The yeast inositol monophosphatase is a lithium-and sodium-sensitive enzyme encoded by a non-essential gene pair. Mol. Microbiol. 31:1255-1264.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1255-1264
    • Lopez, F.1    Leube, M.2    Gil, M.R.3    Navarro, A.J.4    Serrano, R.5
  • 14
    • 0026659202 scopus 로고
    • Inositol phosphate biochemistry
    • Majerus, P. W. 1992. Inositol phosphate biochemistry. Annu. Rev. Biochem. 61:225-250.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 225-250
    • Majerus, P.W.1
  • 15
    • 0030845895 scopus 로고    scopus 로고
    • Molecular genetics of sulfur assimilation in filamentous fungi and yeast
    • Marzluf, G. A. 1997. Molecular genetics of sulfur assimilation in filamentous fungi and yeast. Annu. Rev. Microbiol. 51:73-96.
    • (1997) Annu. Rev. Microbiol. , vol.51 , pp. 73-96
    • Marzluf, G.A.1
  • 16
    • 0016823338 scopus 로고
    • Methionine biosynthesis in Saccharomyces cerevisiae. I. Genetical analysis of auxotrophic mutants
    • Masselot, M., and S. H. De-Robichon. 1975. Methionine biosynthesis in Saccharomyces cerevisiae. I. Genetical analysis of auxotrophic mutants. Mol. Gen. Genet. 139:121-132.
    • (1975) Mol. Gen. Genet. , vol.139 , pp. 121-132
    • Masselot, M.1    De-Robichon, S.H.2
  • 17
    • 0028800519 scopus 로고
    • Inositol monophosphatase activity from the Escherichia coli suhB gene product
    • Matsuhisa, A., N. Suzuki, T. Noda, and K. Shiba. 1995. Inositol monophosphatase activity from the Escherichia coli suhB gene product. J. Bacteriol. 177:200-205.
    • (1995) J. Bacteriol. , vol.177 , pp. 200-205
    • Matsuhisa, A.1    Suzuki, N.2    Noda, T.3    Shiba, K.4
  • 18
    • 0027390036 scopus 로고
    • Thiamine-repressible expression vectors pREP and pRIP for fission yeast
    • Maundrell, K. 1993. Thiamine-repressible expression vectors pREP and pRIP for fission yeast. Gene 123:127-130.
    • (1993) Gene , vol.123 , pp. 127-130
    • Maundrell, K.1
  • 19
    • 0028286249 scopus 로고
    • The protein phosphatase calcineurin is essential for NaCl tolerance of Saccharomyces cerevisiae
    • Mendoza, I., F. Rubio, N. A. Rodriguez, and J. M. Pardo. 1994. The protein phosphatase calcineurin is essential for NaCl tolerance of Saccharomyces cerevisiae. J. Biol. Chem. 269:8792-8796.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8792-8796
    • Mendoza, I.1    Rubio, F.2    Rodriguez, N.A.3    Pardo, J.M.4
  • 20
    • 0026025891 scopus 로고
    • Molecular genetic analysis of fission yeast Schizosaccharomyces pombe
    • Moreno, S., A. Klar, and P. Nurse. 1991. Molecular genetic analysis of fission yeast Schizosaccharomyces pombe. Methods Enzymol. 194:795-823.
    • (1991) Methods Enzymol. , vol.194 , pp. 795-823
    • Moreno, S.1    Klar, A.2    Nurse, P.3
  • 21
    • 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
  • 22
    • 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
  • 23
    • 0027385382 scopus 로고
    • Protein phosphatase type 2B (calcineurin)-mediated, FK506-sensitive regulation of intracellular ions in yeast is an important determinant for adaptation to high salt stress conditions
    • Nakamura, T., Y. Liu, D. Hirata, H. Namba, S. Harada, T. Hirokawa, and T. Miyakawa. 1993. Protein phosphatase type 2B (calcineurin)-mediated, FK506-sensitive regulation of intracellular ions in yeast is an important determinant for adaptation to high salt stress conditions. EMBO J. 12: 4063-4071.
    • (1993) EMBO J. , vol.12 , pp. 4063-4071
    • Nakamura, T.1    Liu, Y.2    Hirata, D.3    Namba, H.4    Harada, S.5    Hirokawa, T.6    Miyakawa, T.7
  • 25
    • 0027327985 scopus 로고
    • Lithium. Current status in psychiatric disorders
    • Peet, M., and J. P. Pratt 1993. Lithium. Current status in psychiatric disorders. Drugs 46:7-17.
    • (1993) Drugs , vol.46 , pp. 7-17
    • Peet, M.1    Pratt, J.P.2
  • 26
    • 0028858093 scopus 로고
    • 2+-sensitive 3′(2′),5′-diphosphonucleoside 3′(2′)-phosphohydrolase and complements yeast met22 and Escherichia coli cysQ mutations
    • 2+-sensitive 3′(2′),5′-diphosphonucleoside 3′(2′)-phosphohydrolase and complements yeast met22 and Escherichia coli cysQ mutations. J. Biol. Chem. 270:29105-29110.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29105-29110
    • Peng, Z.1    Verma, D.P.2
  • 27
    • 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 N. A. Rodriguez. 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, N.A.3
  • 28
    • 0020023938 scopus 로고
    • The role of the lithium ion in medicine
    • Rosenthal, N. E., and F. K. Goodwin. 1982. The role of the lithium ion in medicine. Annu. Rev. Med. 33:555-568.
    • (1982) Annu. Rev. Med. , vol.33 , pp. 555-568
    • Rosenthal, N.E.1    Goodwin, F.K.2
  • 29
    • 0020645054 scopus 로고
    • One-step gene disruption in yeast
    • Rothstein, R. J. 1983. One-step gene disruption in yeast. Methods Enzymol. 101:202-211.
    • (1983) Methods Enzymol. , vol.101 , pp. 202-211
    • Rothstein, R.J.1
  • 30
    • 0033532046 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian lithium-sensitive hisphosphate 3′-nudeotidase inhibited by inositol 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 hisphosphate 3′-nudeotidase inhibited by inositol 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
  • 32
    • 0032472327 scopus 로고    scopus 로고
    • +, a suppressor of calcineurin deficiency, encodes a novel MAP kinase phosphatase in fission yeast
    • +, a suppressor of calcineurin deficiency, encodes a novel MAP kinase phosphatase in fission yeast. EMBO J. 17:140-148.
    • (1998) EMBO J. , vol.17 , pp. 140-148
    • Sugiura, R.1    Toda, T.2    Shuntoh, H.3    Yanagida, M.4    Kuno, T.5
  • 33
    • 0025078941 scopus 로고
    • Gene-enzyme relationship in the sulfate assimilation pathway of Saccharomyces cerevisiae. Study of the 3′-phosphoadenylylsulfate reductase structural gene
    • Thomas, D., R. Barbey, and K. Y. Surdin. 1990. Gene-enzyme relationship in the sulfate assimilation pathway of Saccharomyces cerevisiae. Study of the 3′-phosphoadenylylsulfate reductase structural gene. J. Biol. Chem. 265: 15518-15524.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15518-15524
    • Thomas, D.1    Barbey, R.2    Surdin, K.Y.3
  • 34
    • 0024267104 scopus 로고
    • SAM2 encodes the second methionine S-adenosyl transferase in Saccharomyces cerevisiae: Physiology and regulation of both enzymes
    • Thomas, D., R. Rothstein, N. Rosenberg, and K. Y. Surdin. 1988. SAM2 encodes the second methionine S-adenosyl transferase in Saccharomyces cerevisiae: physiology and regulation of both enzymes. Mol. Cell. Biol. 8: 5132-5139.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 5132-5139
    • Thomas, D.1    Rothstein, R.2    Rosenberg, N.3    Surdin, K.Y.4
  • 35
    • 0029923979 scopus 로고    scopus 로고
    • + gene encodes a novel mitogen-activated protein kinase homolog which regulates cell integrity and functions coordinately with the protein kinase C pathway
    • + gene encodes a novel mitogen-activated protein kinase homolog which regulates cell integrity and functions coordinately with the protein kinase C pathway. Mol. Cell. Biol. 16:6752-6764.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6752-6764
    • Toda, T.1    Dhut, S.2    Superti, F.G.3    Gotoh, Y.4    Nishida, E.5    Sugiura, R.6    Kuno, T.7
  • 36
    • 0031748055 scopus 로고    scopus 로고
    • 2+/CaM-dependent phosphatase (calcineurin) is improved by mutations in URE2 or PMA1
    • 2+/CaM-dependent phosphatase (calcineurin) is improved by mutations in URE2 or PMA1. Genetics 149:865-878.
    • (1998) Genetics , vol.149 , pp. 865-878
    • Wilhee, J.L.1    Sen, R.2    Cyert, M.S.3
  • 37
    • 0029036695 scopus 로고
    • +-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure
    • +-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure. Proc. Natl. Acad. Sci. USA 92: 5149-5153.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5149-5153
    • York, J.D.1    Ponder, J.W.2    Majems, P.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.