메뉴 건너뛰기




Volumn 119, Issue 1-2, 1996, Pages 93-101

Mutants impaired in derepressible alkaline phosphatase activity in Chlamydomonas reinhardtii

Author keywords

Alkaline phosphatase; Chlamydomonas; Derepressible phosphatases; Mutants

Indexed keywords

ALKALINE PHOSPHATASE;

EID: 0030596853     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/0168-9452(96)04447-0     Document Type: Article
Times cited : (7)

References (29)
  • 1
    • 0004145840 scopus 로고
    • McGraw-Hill Inc., New York
    • [1] A.J. Horne and C.R. Goldman, Limnology, McGraw-Hill Inc., New York, 1994, pp. 1-576.
    • (1994) Limnology , pp. 1-576
    • Horne, A.J.1    Goldman, C.R.2
  • 2
    • 0025354922 scopus 로고
    • Functional domains of a positive regulatory protein, PHO4, for transcriptional control of the phosphatase regulon in Saccharomyces cerevisiae
    • [2] N. Ogawa and Y. Oshima, Functional domains of a positive regulatory protein, PHO4, for transcriptional control of the phosphatase regulon in Saccharomyces cerevisiae. Mol. Cell. Biol., 10 (1990) 2224-2236.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2224-2236
    • Ogawa, N.1    Oshima, Y.2
  • 3
    • 0025992263 scopus 로고
    • Impact of the Douglas-Hawthorne model as a paradigm for elucidating cellular regulatory mechanisms in fungi
    • [3] Y. Oshima, Impact of the Douglas-Hawthorne model as a paradigm for elucidating cellular regulatory mechanisms in fungi. Genetics, 128 (1991) 195-201.
    • (1991) Genetics , vol.128 , pp. 195-201
    • Oshima, Y.1
  • 4
    • 0023137257 scopus 로고
    • The yeast PHO5 promoter: Phosphate-control elements and sequences mediating mRNA start site selection
    • [4] H. Rudolph and A. Hinnen, The yeast PHO5 promoter: phosphate-control elements and sequences mediating mRNA start site selection. Genetics, 84 (1987) 1340-1344.
    • (1987) Genetics , vol.84 , pp. 1340-1344
    • Rudolph, H.1    Hinnen, A.2
  • 5
    • 0023929102 scopus 로고
    • Studies on the structure, expression and function of the yeast regulatory gene PHO2
    • [5] G. Berben, M. Legrain and F. Hilger, Studies on the structure, expression and function of the yeast regulatory gene PHO2. Gene, 66 (1988) 307-312.
    • (1988) Gene , vol.66 , pp. 307-312
    • Berben, G.1    Legrain, M.2    Hilger, F.3
  • 6
    • 0024319348 scopus 로고
    • Function of the PHO regulatory genes for repressible acid phosphatase synthesis in Saccharomyces cerevisiae
    • [6] K. Yoshida, N. Ogawa and Y. Oshima, Function of the PHO regulatory genes for repressible acid phosphatase synthesis in Saccharomyces cerevisiae. Mol. Gen. Genet., 217 (1989) 40-46.
    • (1989) Mol. Gen. Genet. , vol.217 , pp. 40-46
    • Yoshida, K.1    Ogawa, N.2    Oshima, Y.3
  • 7
    • 0026573235 scopus 로고
    • Negative regulators of the PHO system of Saccharomyces cerevisiae: Characterization of PHO80 and PHO85
    • [7] Y. Uesono, N. Tokai, K. Tanaka and A. Toh-E, Negative regulators of the PHO system of Saccharomyces cerevisiae: characterization of PHO80 and PHO85. Mol. Gen. Genet., 231 (1992) 426-432.
    • (1992) Mol. Gen. Genet. , vol.231 , pp. 426-432
    • Uesono, Y.1    Tokai, N.2    Tanaka, K.3    Toh-E, A.4
  • 8
    • 0017099269 scopus 로고
    • Phosphatases of Chlamydomonas: Biochemical and cytological approach with specific mutants
    • [8] R.F. Matagne, R. Loppes and R. Deltour, Phosphatases of Chlamydomonas: biochemical and cytological approach with specific mutants. J. Bacteriol., 125 (1976) 937-950.
    • (1976) J. Bacteriol. , vol.125 , pp. 937-950
    • Matagne, R.F.1    Loppes, R.2    Deltour, R.3
  • 9
    • 0016771817 scopus 로고
    • Isolation and study of mutants lacking a derepressible phosphatase in Chlamydomonas reinhardtii
    • [9] R. Matagne and R. Loppes, Isolation and study of mutants lacking a derepressible phosphatase in Chlamydomonas reinhardtii. Genetics, 80 (1975) 239-250.
    • (1975) Genetics , vol.80 , pp. 239-250
    • Matagne, R.1    Loppes, R.2
  • 10
    • 0017726727 scopus 로고
    • Regulation of the neutral phosphatase in Chlamydomonas reinhardi: An immunogenetic study of wild-type and mutant strains
    • [10] R. Loppes, J. Braipson, R.F. Matagne, A. Sassen and L. Ledoux, Regulation of the neutral phosphatase in Chlamydomonas reinhardi: an immunogenetic study of wild-type and mutant strains. Biochem. Genet., 15 (1977) 1147-1157.
    • (1977) Biochem. Genet. , vol.15 , pp. 1147-1157
    • Loppes, R.1    Braipson, J.2    Matagne, R.F.3    Sassen, A.4    Ledoux, L.5
  • 11
    • 0017147106 scopus 로고
    • Genes involved in the regulation of the neutral phosphatase in Chlamydomonas reinhardi
    • [11] R. Loppes, Genes involved in the regulation of the neutral phosphatase in Chlamydomonas reinhardi. Mol. Gen. Genet., 148 (1976) 315-321.
    • (1976) Mol. Gen. Genet. , vol.148 , pp. 315-321
    • Loppes, R.1
  • 12
    • 0011425803 scopus 로고
    • Regulation of the neutral phosphatase in Chlamydomonas reinhardi: Study of a thermosensitive mutant
    • [12] R. Loppes, Regulation of the neutral phosphatase in Chlamydomonas reinhardi: study of a thermosensitive mutant. Mol. Gen. Genet., 158 (1977) 165-169.
    • (1977) Mol. Gen. Genet. , vol.158 , pp. 165-169
    • Loppes, R.1
  • 13
    • 0000415582 scopus 로고
    • New polypeptides and in vitro translatable mRNAs are produced by phosphate-starved cells of the unicellular alga Chlamydomonas reinhardtii
    • [13] F. Dumont, R. Loppes and P. Kremers, New polypeptides and in vitro translatable mRNAs are produced by phosphate-starved cells of the unicellular alga Chlamydomonas reinhardtii. Planta, 182 (1990) 610-616.
    • (1990) Planta , vol.182 , pp. 610-616
    • Dumont, F.1    Loppes, R.2    Kremers, P.3
  • 14
    • 0011383724 scopus 로고
    • Allelic complementation between arg7 mutants in Chlamydomonas reinhardi
    • [14] R. Loppes and R. Matagne, Allelic complementation between arg7 mutants in Chlamydomonas reinhardi. Genetica, 43 (1972) 422-430.
    • (1972) Genetica , vol.43 , pp. 422-430
    • Loppes, R.1    Matagne, R.2
  • 16
    • 0017151059 scopus 로고
    • Release of enzymes by normal and wall-free cells of Chlamydomonas reinhardi
    • [16] R. Loppes, Release of enzymes by normal and wall-free cells of Chlamydomonas reinhardi. J. Bacteriol., 128 (1976) 114-116.
    • (1976) J. Bacteriol. , vol.128 , pp. 114-116
    • Loppes, R.1
  • 17
    • 0015779421 scopus 로고
    • Acid phosphatase mutants in Chlamydomonas: Isolation and characterization by biochemical, electrophoretic and genetic analysis
    • [17] R. Loppes and R. Matagne, Acid phosphatase mutants in Chlamydomonas: isolation and characterization by biochemical, electrophoretic and genetic analysis. Genetics, 75 (1973) 593-604.
    • (1973) Genetics , vol.75 , pp. 593-604
    • Loppes, R.1    Matagne, R.2
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • [18] M.M. Bradford, A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72 (1976) 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 38149143750 scopus 로고
    • Isolation and characterization of biochemical and morphological mutants in Chlamydomonas smithii
    • [19] R.F. Matagne and M.-C. Beckers, Isolation and characterization of biochemical and morphological mutants in Chlamydomonas smithii. Plant Sci., 49 (1987) 85-88.
    • (1987) Plant Sci. , vol.49 , pp. 85-88
    • Matagne, R.F.1    Beckers, M.-C.2
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • [20] U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0018605295 scopus 로고
    • Glycoprotein nature of yeast alkaline phosphatase
    • [21] H.R. Onishi, J.S. Tkacz and J.O. Lampen, Glycoprotein nature of yeast alkaline phosphatase. J. Biol. Chem., 10 (1979) 11943-11952.
    • (1979) J. Biol. Chem. , vol.10 , pp. 11943-11952
    • Onishi, H.R.1    Tkacz, J.S.2    Lampen, J.O.3
  • 22
    • 0021518752 scopus 로고
    • Role of the carbohydrate part of yeast acid phosphatase
    • [22] S. Barbaric, V. Mrsa, B. Ries and P. Mildner, Role of the carbohydrate part of yeast acid phosphatase. Arch. Biochem. Biophys., 234 (1984) 564-575.
    • (1984) Arch. Biochem. Biophys. , vol.234 , pp. 564-575
    • Barbaric, S.1    Mrsa, V.2    Ries, B.3    Mildner, P.4
  • 23
    • 0022551799 scopus 로고
    • Purification and characterization of the secreted alkaline phosphatase of Bacillus licheniformis MC14: Identification of a possible precursor
    • [23] F.M. Hulett, K. Stuckmann, D.B. Spencer and T. Sanopoulou, Purification and characterization of the secreted alkaline phosphatase of Bacillus licheniformis MC14: identification of a possible precursor. J. Gen. Microbiol., 132 (1986) 2387-2395.
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 2387-2395
    • Hulett, F.M.1    Stuckmann, K.2    Spencer, D.B.3    Sanopoulou, T.4
  • 24
    • 0000792336 scopus 로고
    • Properties of a repressible alkaline phosphatase secreted by the wild-type strain 74A of Neurospora crassa
    • [24] E. Nahas and A. Rossi, Properties of a repressible alkaline phosphatase secreted by the wild-type strain 74A of Neurospora crassa. Phytochemistry, 23 (1984) 507-510.
    • (1984) Phytochemistry , vol.23 , pp. 507-510
    • Nahas, E.1    Rossi, A.2
  • 25
    • 0011474030 scopus 로고
    • Cell-wall synthesis in Chlamydomonas reinhardtii: An immunological study of the wild type and wall-less mutants CW2 and CW15
    • [25] Y.H. Zhang and D.G. Robinson, Cell-wall synthesis in Chlamydomonas reinhardtii: an immunological study of the wild type and wall-less mutants CW2 and CW15. Planta, 180 (1990) 229-236.
    • (1990) Planta , vol.180 , pp. 229-236
    • Zhang, Y.H.1    Robinson, D.G.2
  • 26
    • 0017151703 scopus 로고
    • Characterization of membrane proteins in detergent solutions
    • [26] C. Tanford and J. Reynolds, Characterization of membrane proteins in detergent solutions. Biochim. Biophys. Acta, 457 (1976) 133-170.
    • (1976) Biochim. Biophys. Acta , vol.457 , pp. 133-170
    • Tanford, C.1    Reynolds, J.2
  • 27
    • 30344463700 scopus 로고
    • Molecular weight determination of glycoproteins by polyacrylamide gel electrophoresis in sodium dodecylsulfate
    • [27] J.P. Segrest and R.L. Jackson, Molecular weight determination of glycoproteins by polyacrylamide gel electrophoresis in sodium dodecylsulfate. Methods Enzymol., 28 (1972) 54-63.
    • (1972) Methods Enzymol. , vol.28 , pp. 54-63
    • Segrest, J.P.1    Jackson, R.L.2
  • 28
    • 0002150243 scopus 로고
    • Regulatory circuit for phosphatase synthesis in Saccharomyces cerevisiae
    • A. Torriani-Gorini, F.G. Rothman, S. Silver, A. Wright and E. Yagil (Eds.), American Society for Microbiology, Washington, DC
    • [28] K. Yoshida, Z. Kuromitsu, N. Ogawa, K. Ogawa and K. Oshima, Regulatory circuit for phosphatase synthesis in Saccharomyces cerevisiae, in: A. Torriani-Gorini, F.G. Rothman, S. Silver, A. Wright and E. Yagil (Eds.), Phosphate Metabolism and Cellular Regulation in Microorganisms, American Society for Microbiology, Washington, DC, 1987, pp. 49-55.
    • (1987) Phosphate Metabolism and Cellular Regulation in Microorganisms , pp. 49-55
    • Yoshida, K.1    Kuromitsu, Z.2    Ogawa, N.3    Ogawa, K.4    Oshima, K.5
  • 29
    • 0002464183 scopus 로고
    • Isolation and characterization of cDNA sequences controlled by inorganic phosphate in Chlamydomonas reinhardtii
    • [29] F. Dumont, B. Joris, A. Gumusboga, M. Bruyninx and R. Loppes, Isolation and characterization of cDNA sequences controlled by inorganic phosphate in Chlamydomonas reinhardtii. Plant Sci., 89 (1993) 55-67.
    • (1993) Plant Sci. , vol.89 , pp. 55-67
    • Dumont, F.1    Joris, B.2    Gumusboga, A.3    Bruyninx, M.4    Loppes, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.