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Volumn 63, Issue 11, 1999, Pages 1871-1881

Involvement of Thioredoxin Peroxidase Type II (Ahp1p) of Saccharomyces cerevisiae in Mn2+ Homeostasis

Author keywords

AHP1; Manganese; Organellar trafficking; Saccharomyces cerevisiae

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATASE (CALCIUM); CALCINEURIN; HYDROGEN PEROXIDE; MANGANESE; PEROXIDASE; PEROXIREDOXIN; PMR1 PROTEIN, S CEREVISIAE; RECOMBINANT PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 0033217253     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.63.1871     Document Type: Article
Times cited : (15)

References (50)
  • 1
    • 0020073664 scopus 로고
    • Free manganese (II) and iron (II) cations can act as cellular controls
    • Wiliams, R. J. P., Free manganese (II) and iron (II) cations can act as cellular controls. FEBS Let., 140, 3-10 (1982).
    • (1982) FEBS Let. , vol.140 , pp. 3-10
    • Wiliams, R.J.P.1
  • 2
    • 0028877431 scopus 로고
    • Manganese effectively supports yeast cell-cycle progression in place of calcium
    • Loukin, S. and Kung, C., Manganese effectively supports yeast cell-cycle progression in place of calcium. J. Cell Biol., 131, 1025-1037 (1995).
    • (1995) J. Cell Biol. , vol.131 , pp. 1025-1037
    • Loukin, S.1    Kung, C.2
  • 4
    • 0019276106 scopus 로고
    • Role of vacuolar ion pool in Saccharomyces carlsbergensis. Potassium efflux from vacuoles is coupled with manganese or magnesium influx
    • Lichko, L. P., Okorokov, L. A., and Kulaev, I. S., Role of vacuolar ion pool in Saccharomyces carlsbergensis. Potassium efflux from vacuoles is coupled with manganese or magnesium influx. J. Bacteriol., 144, 666-671 (1980).
    • (1980) J. Bacteriol. , vol.144 , pp. 666-671
    • Lichko, L.P.1    Okorokov, L.A.2    Kulaev, I.S.3
  • 8
    • 0001904037 scopus 로고
    • Biochemical and nutritional role of manganese: An overview
    • Klimis-Tavantzis D. J., CRC Press, Inc., Boca Raton FL
    • Wedler, F. C., Biochemical and nutritional role of manganese: an overview. In “Manganese in Health and Disease” ed. Klimis-Tavantzis D. J., CRC Press, Inc., Boca Raton FL, pp. 1-38 (1994).
    • (1994) In “Manganese in Health and Disease” , pp. 1-38
    • Wedler, F.C.1
  • 10
    • 0029978512 scopus 로고    scopus 로고
    • A yeast manganese transporter related to the macrophage protein involved in conferring resistance to mycobacteria
    • Supek, F., Supekova, L., Nelson, H., and Nelson, N., A yeast manganese transporter related to the macrophage protein involved in conferring resistance to mycobacteria. Proc. Natl. Acad. Sei. USA, 93, 5105-5110 (1996).
    • (1996) Proc. Natl. Acad. Sei. USA , vol.93 , pp. 5105-5110
    • Supek, F.1    Supekova, L.2    Nelson, H.3    Nelson, N.4
  • 11
    • 0028889152 scopus 로고
    • Mutations in PMR1 suppress oxidative damage in yeast lacking superoxide dismutase
    • Lapinskas, P. J., Cunningham, K. W., Liu, X. F., Fink, G. R., and Culotta, V. C., Mutations in PMR1 suppress oxidative damage in yeast lacking superoxide dismutase. Mol. Cell. Biol., 15, 1382-1388 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1382-1388
    • Lapinskas, P.J.1    Cunningham, K.W.2    Liu, X.F.3    Fink, G.R.4    Culotta, V.C.5
  • 12
    • 0029787345 scopus 로고    scopus 로고
    • The role of the Saccharomyces cerevisiae CCC1 gene in the homeostasis of manganese ions
    • Lapinskas, P. J., Lin, S., and Culotta, V. C., The role of the Saccharomyces cerevisiae CCC1 gene in the homeostasis of manganese ions. Mol. Microbiol., 21, 519-528 (1996).
    • (1996) Mol. Microbiol. , vol.21 , pp. 519-528
    • Lapinskas, P.J.1    Lin, S.2    Culotta, V.C.3
  • 13
    • 0029806025 scopus 로고    scopus 로고
    • Suppression of oxidative damage by Saccharomyces cerevisiae ATX2, which encodes a manganese-trafficking protein, localizes to Golgi-like vesicle
    • Lin, S. J. and Culotta, V. C. Suppression of oxidative damage by Saccharomyces cerevisiae ATX2, which encodes a manganese-trafficking protein, localizes to Golgi-like vesicle. Mol. Cell. Biol., 16, 6303-6312 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6303-6312
    • Lin, S.J.1    Culotta, V.C.2
  • 16
    • 0029088948 scopus 로고
    • Protein phosphatase 2B of Saccharomyces cerevisiae is required for tolerance to manganese, in blocking the entry of ions into the cells
    • Farcasanu, I. C., Hirata, D., Tsuchiya, E., Nishiyama, F., and Miyakawa, T., Protein phosphatase 2B of Saccharomyces cerevisiae is required for tolerance to manganese, in blocking the entry of ions into the cells. Eur. J. Biochem., 232, 712-717 (1995).
    • (1995) Eur. J. Biochem. , vol.232 , pp. 712-717
    • Farcasanu, I.C.1    Hirata, D.2    Tsuchiya, E.3    Nishiyama, F.4    Miyakawa, T.5
  • 17
    • 0030006878 scopus 로고    scopus 로고
    • The product of HUM1, a novel yeast gene, is required for vacuolar Ca2+/H+ exchange and is related to mammalian Na+/Ca2+ exchangers
    • 2+ exchangers. Mol. Cell. Biol, 16, 3730-3741 (1996).
    • (1996) Mol. Cell. Biol , vol.16 , pp. 3730-3741
    • Pozos, T.C.1    Sekler, I.2    Cyert, M.S.3
  • 18
    • 0025809351 scopus 로고
    • The Saccharomyces cerevisiae genes (CMP1 and CMP2) encoding calmodulin-binding protein homologous to the catalytic subunit of mammalian protein phosphatase 2B
    • Liu, J., Ishii, S., Tokai, M., Tsutsumi, H., Ohki, O., Akada, R., Tanaka, K., Tsuchiya, E., Fukui, S., and Miyakawa, T., The Saccharomyces cerevisiae genes (CMP1 and CMP2) encoding calmodulin-binding protein homologous to the catalytic subunit of mammalian protein phosphatase 2B. Mol. Gen. Genet., 227, 52-59 (1991).
    • (1991) Mol. Gen. Genet. , vol.227 , pp. 52-59
    • Liu, J.1    Ishii, S.2    Tokai, M.3    Tsutsumi, H.4    Ohki, O.5    Akada, R.6    Tanaka, K.7    Tsuchiya, E.8    Fukui, S.9    Miyakawa, T.10
  • 19
    • 0025913953 scopus 로고
    • Yeast has homologs (CNA1 and CNA2 gene products) of mammalian calcineurin, a calmodulin-regulated phosphoprotein phosphatase
    • Cyert, M. S., Kunisawa, R., Kaim, D., and Thorner, J., Yeast has homologs (CNA1 and CNA2 gene products) of mammalian calcineurin, a calmodulin-regulated phosphoprotein phosphatase. Proc. Natl. Acad. Sci. USA, 88, 7376-7380 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7376-7380
    • Cyert, M.S.1    Kunisawa, R.2    Kaim, D.3    Thorner, J.4
  • 21
    • 0026637095 scopus 로고
    • Regulatory subunit (CNB1 gene product) of yeast Ca2+/calmodulin-dependent phosphoprotein phosphatases is required for adaptation to pheromone
    • 2+/calmodulin-dependent phosphoprotein phosphatases is required for adaptation to pheromone. Mol. Cell. Biol., 12, 3460-3469 (1992).
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3460-3469
    • Cyert, M.S.1    Thorner, J.2
  • 22
    • 0029862619 scopus 로고    scopus 로고
    • Calcineurin inhibits FCX7-dependent H+/Ca2+ exchange and induces Ca2+ AT-Pases in yeast
    • 2+ AT-Pases in yeast. Mol. Cell. Biol., 16, 2226-2237 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2226-2237
    • Cunningham, K.W.1    Fink, G.R.2
  • 23
    • 0031451194 scopus 로고    scopus 로고
    • Tcnlp/Crzlp, a calcineurin-dependent transcription factor that differentially regulates gene expression in
    • Matheos, D. P., Kingsbury, T. J., Salma Ahsan, U., and Cunningham, K. W., Tcnlp/Crzlp, a calcineurin-dependent transcription factor that differentially regulates gene expression in Saccharomyces cerevisiae. Genes & Dev., 11, 3445-3458 (1997).
    • (1997) Saccharomyces Cerevisiae. Genes & Dev. , vol.11 , pp. 3445-3458
    • Matheos, D.P.1    Kingsbury, T.J.2    Salma Ahsan, U.3    Cunningham, K.W.4
  • 25
    • 0027097849 scopus 로고    scopus 로고
    • The yeast Ca2+-ATPase homo-logue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution
    • 2+-ATPase homo-logue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution. Mol. Biol. Cell, 3, 633-654 (1997).
    • (1997) Mol. Biol. Cell , vol.3 , pp. 633-654
    • Antebi, A.1    Fink, G.R.2
  • 26
    • 0028079476 scopus 로고
    • Calcineurin-dependent growth control in Saccharomyces cerevisiae mutants lacking PMC1, a homolog of plasma membrane Ca2+ ATPases
    • 2+ ATPases. J. Cell Biol, 124, 351-363 (1994).
    • (1994) J. Cell Biol , vol.124 , pp. 351-363
    • Cunningham, K.W.1    Fink, G.R.2
  • 27
    • 0000300772 scopus 로고    scopus 로고
    • Purification and characterization of a second type thioredoxin peroxidase (Type II TPx) from
    • (1999)
    • Jeong, J. S., Kwon, S. J., Kang, S. W., Rhee, S. G., and Kim, K., (1999) Purification and characterization of a second type thioredoxin peroxidase (type II TPx) from Saccharomyces cerevisiae. Biochemistry, 38, 776-83 (1999).
    • (1999) Saccharomyces Cerevisiae. Biochemistry , pp. 38
    • Jeong, J.S.1    Kwon, S.J.2    Kang, S.W.3    Rhee, S.G.4    Kim, K.5
  • 28
    • 0033582416 scopus 로고    scopus 로고
    • A new antioxidant with alkyl hydroperoxide defense properties in yeast
    • Lee, J., Spector, D., Godon, C., Labarre, J., and Toledano, M. B., A new antioxidant with alkyl hydroperoxide defense properties in yeast. J. Biol. Chem., 274, 4537-4544 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 4537-4544
    • Lee, J.1    Spector, D.2    Godon, C.3    Labarre, J.4    Toledano, M.B.5
  • 29
    • 0024076281 scopus 로고
    • Identification of peroxisomal targeting signals located at the carboxi terminus of four peroxisomal proteins
    • Gould, S. J., Keller, G.-A., and Subramani, S., Identification of peroxisomal targeting signals located at the carboxi terminus of four peroxisomal proteins. J. Cell Biol, 107, 897-905 (1994).
    • (1994) J. Cell Biol , vol.107 , pp. 897-905
    • Gould, S.J.1    Keller, G.-A.2    Subramani, S.3
  • 30
    • 0028149887 scopus 로고
    • Peroxisomal biogenesis: Multiple pathways of protein import
    • Purdue, P. E. and Lazarow, P. B., Peroxisomal biogenesis: multiple pathways of protein import. J. Biol. Chem., 269, 30065-30068 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 30065-30068
    • Purdue, P.E.1    Lazarow, P.B.2
  • 32
    • 0003529274 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor New York
    • Sherman, F., Fink, G. R., and Hicks, J. B., “Methods in yeast genetics,” Cold Spring Harbor Laboratory Press, Cold Spring Harbor New York (1986).
    • (1986) Methods in Yeast Genetics
    • Sherman, F.1    Fink, G.R.2    Hicks, J.B.3
  • 33
    • 0026073301 scopus 로고
    • Classical Mutagenesis Techniques
    • Lawrence, C. W., Classical Mutagenesis Techniques. Meth. En-zymol., 194, 273-281 (1986).
    • (1986) Meth. En-Zymol. , vol.194 , pp. 273-281
    • Lawrence, C.W.1
  • 35
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Fukuda, I., Murata, K., and Kimura, A., Transformation of intact yeast cells treated with alkali cations. J. Bacteriol., 153, 163-168 (1983).
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, I.2    Murata, K.3    Kimura, A.4
  • 36
    • 0041773753 scopus 로고
    • Cycle sequencing
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Kretz, K., Callen, W., and Hedden, V., Cycle sequencing. In “PCR primer: a laboratory manual,” Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, pp. 527-537 (1995).
    • (1995) PCR Primer: A Laboratory Manual , pp. 527-537
    • Kretz, K.1    Callen, W.2    Hedden, V.3
  • 37
    • 0020645054 scopus 로고
    • One-step gene disruption in yeast
    • Rothstein, R. J., One-step gene disruption in yeast. Meth. Enzymol, 101, 202-211 (1995).
    • (1995) Meth. Enzymol , vol.101 , pp. 202-211
    • Rothstein, R.J.1
  • 39
    • 0025975314 scopus 로고
    • Analysis of mitochondrial function and assembly
    • Yaffe, M. P., Analysis of mitochondrial function and assembly. Methods Enzymol., 194, 627-643 (1991).
    • (1991) Methods Enzymol. , vol.194 , pp. 627-643
    • Yaffe, M.P.1
  • 40
    • 0027254848 scopus 로고
    • Assay of succinate dehydrogenase activity by a colorimetric-continuous method using iodonitrotetrazolium chloride as electron acceptor
    • Munujos, P., Coll-Canti, J., Gonzales-Sastre, F., and Gella, F. J., Assay of succinate dehydrogenase activity by a colorimetric-continuous method using iodonitrotetrazolium chloride as electron acceptor. Anal. Biochem., 212, 506-509 (1993).
    • (1993) Anal. Biochem. , vol.212 , pp. 506-509
    • Munujos, P.1    Coll-Canti, J.2    Gonzales-Sastre, F.3    Gella, F.J.4
  • 41
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford, M. M., 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).
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 42
    • 0020803681 scopus 로고
    • The nature of the electron spin resonance signal during aerobic uptake of Mn2+ in mitochondria from rat liver
    • 2+ in mitochondria from rat liver. Eur. J. Biochem., 134, 385-390 (1983).
    • (1983) Eur. J. Biochem. , vol.134 , pp. 385-390
    • Bragadin, M.1    Pozzan, T.2    Azzone, G.F.3
  • 43
  • 44
    • 0027249006 scopus 로고
    • Kinetic analysis of manganese peroxidase
    • Kuan, I. C., Johnson, K. A., and Tien, M., Kinetic analysis of manganese peroxidase. J. Biol. Chem., 268, 20064-20070 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 20064-20070
    • Kuan, I.C.1    Johnson, K.A.2    Tien, M.3
  • 45
    • 0020118402 scopus 로고
    • The scavenging of superoxide radical by manganous complexes
    • Archibald, F. S. and Fridovich, I., The scavenging of superoxide radical by manganous complexes in vitro. Arch. Biochem Biophys., 214, 452-463 (1982).
    • (1982) In Vitro. Arch. Biochem Biophys. , vol.214 , pp. 452-463
    • Archibald, F.S.1    Fridovich, I.2
  • 46
    • 0029152774 scopus 로고
    • Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions
    • Chen, L., Keramati, L., and Helmann, J. D., Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions. Proc. Natl. Acad. Sci. USA, 92, 8190-8194 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8190-8194
    • Chen, L.1    Keramati, L.2    Helmann, J.D.3
  • 49
    • 0032483373 scopus 로고    scopus 로고
    • The cytoplasmic Cu, Zn superoxide dismutase of Saccharomyces cerevisiae is required for resistance to freeze-thaw stress. Generation of free radicals during freezing and thawing
    • Park, J. I., Grant, C. M., Davies, M. J., and Dawes, I. W., The cytoplasmic Cu, Zn superoxide dismutase of Saccharomyces cerevisiae is required for resistance to freeze-thaw stress. Generation of free radicals during freezing and thawing. J. Biol. Chem., 273, 22921-22928 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 22921-22928
    • Park, J.I.1    Grant, C.M.2    Davies, M.J.3    Dawes, I.W.4
  • 50
    • 0030323039 scopus 로고    scopus 로고
    • Enhancement of yeast ethanol tolerance by calcium and magnesium
    • Ciesarova, Z., Smogrovicova, D., and Domeny, Z., Enhancement of yeast ethanol tolerance by calcium and magnesium. Folia Microbiol. (Praha), 41, 485-488 (1996).
    • (1996) Folia Microbiol. (Praha) , vol.41 , pp. 485-488
    • Ciesarova, Z.1    Smogrovicova, D.2    Domeny, Z.3


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