메뉴 건너뛰기




Volumn 42, Issue 6, 1999, Pages 1077-1087

Sequence and phylogenetic analysis of the SNF4/AMPK gamma subunit gene from Drosophila melanogaster

Author keywords

AMPK gamma subunit; Derepression; Gene family; Phylogeny; SNF4

Indexed keywords

ADENOSINE PHOSPHATE ACTIVATED PROTEIN KINASE; CARBOXY TERMINAL SEQUENCE; COMPLEMENTARY DNA; ENZYME SUBUNIT; EXPRESSED SEQUENCE TAG; GENE ACTIVATION; GENE DUPLICATION; GENE PRODUCT; GENE SEQUENCE; MOLECULAR CLONING; MULTIGENE FAMILY; PHYLOGENY; SOUTHERN BLOTTING;

EID: 0033491314     PISSN: 08312796     EISSN: None     Source Type: Journal    
DOI: 10.1139/g99-059     Document Type: Article
Times cited : (8)

References (31)
  • 1
    • 0031016272 scopus 로고    scopus 로고
    • The structure of a domain common to archae-bacteria and the homocystinuria disease protein
    • Bateman, A. 1997. The structure of a domain common to archae-bacteria and the homocystinuria disease protein. TIBS, 22: 12-13.
    • (1997) TIBS , vol.22 , pp. 12-13
    • Bateman, A.1
  • 2
    • 0019322440 scopus 로고
    • The transposable element Mdg3 in Drosophila melanogaster is flanked with perfect direct and mismatched inverted repeats
    • Bayev, A.A., Jr., Krayev, A.S., Lyubomirskaya, N.V., Ilyin, Y.V., Skryabin, K.G., and Georgiev, G.P. 1980. The transposable element Mdg3 in Drosophila melanogaster is flanked with perfect direct and mismatched inverted repeats. Nucleic Acids Res. 8: 3263-3273.
    • (1980) Nucleic Acids Res. , vol.8 , pp. 3263-3273
    • Bayev A.A., Jr.1    Krayev, A.S.2    Lyubomirskaya, N.V.3    Ilyin, Y.V.4    Skryabin, K.G.5    Georgiev, G.P.6
  • 3
    • 0028310837 scopus 로고
    • Mammalian AMP-activated protein kinase is homologous to yeast and plant protein kinases involved in the regulation of carbon metabolism
    • Carling, D., Aguan, K., Woods, A., Verhoeven, A.J.M., Beri, R.K., Brennan, C.H., Sidebottom, C., Davison, M.D., and Scott, J. 1994. Mammalian AMP-activated protein kinase is homologous to yeast and plant protein kinases involved in the regulation of carbon metabolism. J. Biol. Chem. 269: 11 442-11 448.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11442-11448
    • Carling, D.1    Aguan, K.2    Woods, A.3    Verhoeven, A.J.M.4    Beri, R.K.5    Brennan, C.H.6    Sidebottom, C.7    Davison, M.D.8    Scott, J.9
  • 4
    • 0020078214 scopus 로고
    • Two differentially regulated mRNAs with different 5′ ends encode secreted and intracellular forms of yeast invertase
    • Carlson, M., and Botstein, D. 1982. Two differentially regulated mRNAs with different 5′ ends encode secreted and intracellular forms of yeast invertase. Cell, 28: 145-154.
    • (1982) Cell , vol.28 , pp. 145-154
    • Carlson, M.1    Botstein, D.2
  • 5
    • 0028998724 scopus 로고
    • GTP depletion induced by IMP dehydrogenase inhibitors blocks RNA-primed DNA synthesis
    • Catapano, C., Dayton, J., Mitchell, V., and Fernandes, D. 1995. GTP depletion induced by IMP dehydrogenase inhibitors blocks RNA-primed DNA synthesis. Mol. Pharmacol. 47: 948-955.
    • (1995) Mol. Pharmacol. , vol.47 , pp. 948-955
    • Catapano, C.1    Dayton, J.2    Mitchell, V.3    Fernandes, D.4
  • 6
    • 0024343258 scopus 로고
    • Mutational analysis of the Saccharomyces cerevisiae SNF1 protein kinase and evidence for functional interaction with the SNF4 protein
    • Celenza, J.L., and Carlson, M. 1989. Mutational analysis of the Saccharomyces cerevisiae SNF1 protein kinase and evidence for functional interaction with the SNF4 protein. Mol. Cell. Biol. 9: 5034-5044.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 5034-5044
    • Celenza, J.L.1    Carlson, M.2
  • 7
    • 0024325465 scopus 로고
    • Molecular analysis of the SNF4 gene of Saccharomyces cerevisiae: Evidence for physical association of the SNF4 protein with the SNF1 protein kinase
    • Celenza, J.L., Eng, F.J., and Carlson, M. 1989. Molecular analysis of the SNF4 gene of Saccharomyces cerevisiae: Evidence for physical association of the SNF4 protein with the SNF1 protein kinase. Mol. Cell. Biol. 9: 5045-5054.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 5045-5054
    • Celenza, J.L.1    Eng, F.J.2    Carlson, M.3
  • 8
    • 0028942747 scopus 로고
    • Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I
    • Dale, S., Wilson, W.A., Edelman, A.M., and Hardie, D.G. 1995. Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I. FEBS Lett. 361: 191-195.
    • (1995) FEBS Lett. , vol.361 , pp. 191-195
    • Dale, S.1    Wilson, W.A.2    Edelman, A.M.3    Hardie, D.G.4
  • 9
    • 0024152983 scopus 로고
    • Phylogenies from molecular sequences: Inference and reliability
    • Felsenstein, J. 1988. Phylogenies from molecular sequences: Inference and reliability. Annu. Rev. Genet. 22: 521-565.
    • (1988) Annu. Rev. Genet. , vol.22 , pp. 521-565
    • Felsenstein, J.1
  • 11
    • 0026604926 scopus 로고
    • Regulation of fatty acid and cholesterol metabolism by the AMP-activated protein kinase
    • Hardie, D.G. 1992. Regulation of fatty acid and cholesterol metabolism by the AMP-activated protein kinase. Biochim. Biophys. Acta, 1123: 231-238.
    • (1992) Biochim. Biophys. Acta , vol.1123 , pp. 231-238
    • Hardie, D.G.1
  • 12
    • 0027941804 scopus 로고
    • Ways of coping with stress
    • Hardie, D.G. 1994. Ways of coping with stress. Nature (London), 370: 599-600.
    • (1994) Nature (London) , vol.370 , pp. 599-600
    • Hardie, D.G.1
  • 13
    • 0031717105 scopus 로고    scopus 로고
    • The AMP-activated/SNF1 protein kinase subfamily: Metabolic sensors of the eukaryotic cell?
    • Hardie, D.G., Carling, D., and Carlson, M. 1998. The AMP-activated/SNF1 protein kinase subfamily: Metabolic sensors of the eukaryotic cell? Annu. Rev. Biochem. 67: 821-855.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 821-855
    • Hardie, D.G.1    Carling, D.2    Carlson, M.3
  • 14
    • 0020448905 scopus 로고
    • Regulation of amylase activity in Drosophila melanogaster: Effects of dietary carbohydrate
    • Hickey, D.A., and Benkel, B.F. 1982. Regulation of amylase activity in Drosophila melanogaster: Effects of dietary carbohydrate. Biochem. Genet. 20: 1117-1129.
    • (1982) Biochem. Genet. , vol.20 , pp. 1117-1129
    • Hickey, D.A.1    Benkel, B.F.2
  • 15
    • 0013633790 scopus 로고
    • Regulation of amylase gene expression: Drosophila amylases as a model experimental system
    • Hickey, D.A., and Benkel, B.F. 1987. Regulation of amylase gene expression: Drosophila amylases as a model experimental system. CRC Crit. Rev. Biotechnol. 3: 229-241.
    • (1987) CRC Crit. Rev. Biotechnol. , vol.3 , pp. 229-241
    • Hickey, D.A.1    Benkel, B.F.2
  • 17
    • 0002426158 scopus 로고
    • Gene duplication, gene conversion and codon bias
    • Edited by B. Golding. Chapman and Hall, New York
    • Hickey, D.A., Wang, S., and Magoulas, C. 1994. Gene duplication, gene conversion and codon bias. In Non-neutral evolution. Edited by B. Golding. Chapman and Hall, New York. pp. 199-207.
    • (1994) Non-neutral Evolution , pp. 199-207
    • Hickey, D.A.1    Wang, S.2    Magoulas, C.3
  • 18
    • 0000632439 scopus 로고
    • Regulation of carbon and phosphate utilization
    • Edited by E.W. Jones, J.R. Pringle, and J.R. Broach. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Johnston, M., and Carlson, M. 1992. Regulation of carbon and phosphate utilization. In The molecular and cellular biology of the yeast Saccharomyces. Edited by E.W. Jones, J.R. Pringle, and J.R. Broach. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. pp. 194-241.
    • (1992) The Molecular and Cellular Biology of the Yeast Saccharomyces , pp. 194-241
    • Johnston, M.1    Carlson, M.2
  • 19
    • 0031983739 scopus 로고    scopus 로고
    • Glucose control in Saccharomyces cerevisiae: The role of MIG1 in metabolic functions
    • Klein, C.J.L., Olson, L., and Nielson, J. 1998. Glucose control in Saccharomyces cerevisiae: The role of MIG1 in metabolic functions. Microbiology, 144: 13-24.
    • (1998) Microbiology , vol.144 , pp. 13-24
    • Klein, C.J.L.1    Olson, L.2    Nielson, J.3
  • 20
    • 0021770224 scopus 로고
    • Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs
    • Kozak, M. 1984. Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs. Nucleic Acids Res. 12: 857-872.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 857-872
    • Kozak, M.1
  • 21
    • 0026808466 scopus 로고
    • Glucose regulation of acetyl-CoA carboxylase in hepatoma and islet cells
    • Louis, N.A., and Witters, L.A. 1992. Glucose regulation of acetyl-CoA carboxylase in hepatoma and islet cells. J. Biol. Chem. 267: 2287-2293.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2287-2293
    • Louis, N.A.1    Witters, L.A.2
  • 22
    • 0027932717 scopus 로고
    • Mammalian AMP-activated protein kinase shares structural and functional homology with the catalytic domain of yeast Snf1 protein kinase
    • Mitchelhill, K.I., Stapelton, D.A., Gao, G., House, C., Michell, B., Katsis, F., Witters, L.A., and Kemp, B.E. 1994. Mammalian AMP-activated protein kinase shares structural and functional homology with the catalytic domain of yeast Snf1 protein kinase. J. Biol. Chem. 269: 2361-2364.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2361-2364
    • Mitchelhill, K.I.1    Stapelton, D.A.2    Gao, G.3    House, C.4    Michell, B.5    Katsis, F.6    Witters, L.A.7    Kemp, B.E.8
  • 23
    • 0023056570 scopus 로고
    • Sequence signals which may be required for efficient formation of mRNA 3′ termini
    • Nussinov, R. 1986. Sequence signals which may be required for efficient formation of mRNA 3′ termini. Nucleic Acids Res. 14: 3557-3571.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 3557-3571
    • Nussinov, R.1
  • 24
    • 0032519837 scopus 로고    scopus 로고
    • Negative control of the Mig1p repressor by Snf1p-dependent phosphorylation in the absence of glucose
    • Östling, J., and Ronne, H. 1998. Negative control of the Mig1p repressor by Snf1p-dependent phosphorylation in the absence of glucose. Eur. J. Biochem. 252: 162-168.
    • (1998) Eur. J. Biochem. , vol.252 , pp. 162-168
    • Östling, J.1    Ronne, H.2
  • 25
    • 0030249128 scopus 로고    scopus 로고
    • Caprine homologue of rodent 5′-AMP-activated protein kinase subunit and yeast SNF4/CAT3 is down-regulated by thyroid hormone
    • Piosik, P.A., Van Groenigen, M., Ponne, N.J., Valentijn, L.J., Bolhuis, P.A., and Baas, R. 1996. Caprine homologue of rodent 5′-AMP-activated protein kinase subunit and yeast SNF4/CAT3 is down-regulated by thyroid hormone. Mol. Brain Res. 40: 240-253.
    • (1996) Mol. Brain Res. , vol.40 , pp. 240-253
    • Piosik, P.A.1    Van Groenigen, M.2    Ponne, N.J.3    Valentijn, L.J.4    Bolhuis, P.A.5    Baas, R.6
  • 26
    • 0029899127 scopus 로고    scopus 로고
    • Structure and mechanism of inosine monophosphate dehydrogenase in complex with the immunosuppressant mycophenolic acid
    • Sintchak, M.D., Fleming, M.A., Futer, O., Raybuck, S.A., Chambers, S.P., Caron, P.R., Murcko, M.A., and Wilson, K.P. 1996. Structure and mechanism of inosine monophosphate dehydrogenase in complex with the immunosuppressant mycophenolic acid. Cell, 85: 921-930.
    • (1996) Cell , vol.85 , pp. 921-930
    • Sintchak, M.D.1    Fleming, M.A.2    Futer, O.3    Raybuck, S.A.4    Chambers, S.P.5    Caron, P.R.6    Murcko, M.A.7    Wilson, K.P.8
  • 28
    • 0028970369 scopus 로고
    • Repression by SSN6-TUP1 is directed by MIG1, a repressor/activator protein
    • Treitel, M.A., and Carlson, M. 1995. Repression by SSN6-TUP1 is directed by MIG1, a repressor/activator protein. Proc. Natl. Acad. Sci. U.S.A. 92: 3132-3126.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 3132-13126
    • Treitel, M.A.1    Carlson, M.2
  • 29
    • 0031740335 scopus 로고    scopus 로고
    • Snf1 protein kinase regulates phosphorylation of the Mig1 repressor in Saccharomyces cerevisiae
    • Treitel, M.A., Kuchin, S., and Carson, M. 1998. Snf1 protein kinase regulates phosphorylation of the Mig1 repressor in Saccharomyces cerevisiae. Mol Cell. Biol. 18: 6270-6280.
    • (1998) Mol Cell. Biol. , vol.18 , pp. 6270-6280
    • Treitel, M.A.1    Kuchin, S.2    Carson, M.3
  • 30
    • 0027440990 scopus 로고
    • Specificity determinants for the AMP-activated protein kinase and its plant homologue analysed using synthetic peptides
    • Weekes, J., Ball, K.L., Caudwell, F.B., and Hardie, D.G. 1993. Specificity determinants for the AMP-activated protein kinase and its plant homologue analysed using synthetic peptides. FEBS Lett. 334: 335-339.
    • (1993) FEBS Lett. , vol.334 , pp. 335-339
    • Weekes, J.1    Ball, K.L.2    Caudwell, F.B.3    Hardie, D.G.4
  • 31
    • 0029925785 scopus 로고    scopus 로고
    • Characterization of AMP-activated protein kinase β and γ subunits. Assembly of the heterotrimeric complex in vitro
    • Woods, A., Cheung, P.C.F., Smith, F.C., Davison, M.D., Scott, J., Beri, R.K., and Carling, D. 1996. Characterization of AMP-activated protein kinase β and γ subunits. Assembly of the heterotrimeric complex in vitro. J. Biol. Chem. 271: 10 282-10 290.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10282-10290
    • Woods, A.1    Cheung, P.C.F.2    Smith, F.C.3    Davison, M.D.4    Scott, J.5    Beri, R.K.6    Carling, D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.