메뉴 건너뛰기




Volumn 130, Issue 4, 2002, Pages 1797-1806

Molecular characterization of a novel gene family encoding ACT domain repeat proteins in Arabidopsis

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; BIOSENSORS; CHROMOSOMES; ENZYMES; PLANTS (BOTANY);

EID: 0036921696     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.007484     Document Type: Article
Times cited : (42)

References (37)
  • 1
    • 0033574503 scopus 로고    scopus 로고
    • Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database search
    • Aravind L, Koonin EV (1999) Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database search. J Mol Biol 287: 1023-1040
    • (1999) J Mol Biol , vol.287 , pp. 1023-1040
    • Aravind, L.1    Koonin, E.V.2
  • 2
    • 0022402203 scopus 로고
    • Role of glnB and glnD gene products in regulation of the glnALG operon of Escherichia coli
    • Bueno R, Pahel G, Magasanik B (1985) Role of glnB and glnD gene products in regulation of the glnALG operon of Escherichia coli. J Bacteriol 164: 816-822
    • (1985) J Bacteriol , vol.164 , pp. 816-822
    • Bueno, R.1    Pahel, G.2    Magasanik, B.3
  • 4
    • 0032483527 scopus 로고    scopus 로고
    • Amino acid substitutions in the C-terminal regulatory domain disrupt allosteric effector binding to biosynthetic threonine deaminase from Escherichia coli
    • Chinchilla D, Schwarz FP, Eisenstein E (1998) Amino acid substitutions in the C-terminal regulatory domain disrupt allosteric effector binding to biosynthetic threonine deaminase from Escherichia coli. J Biol Chem 273: 23219-23224
    • (1998) J Biol Chem , vol.273 , pp. 23219-23224
    • Chinchilla, D.1    Schwarz, F.P.2    Eisenstein, E.3
  • 6
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough SJ, Bent AF (1998) Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J 16: 735-743
    • (1998) Plant J , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 7
    • 0035146278 scopus 로고    scopus 로고
    • Nitrogen and carbon nutrient and metabolite signaling in plants
    • Coruzzi G, Bush DR (2001) Nitrogen and carbon nutrient and metabolite signaling in plants. Plant Physiol 125: 61-64
    • (2001) Plant Physiol , vol.125 , pp. 61-64
    • Coruzzi, G.1    Bush, D.R.2
  • 8
    • 0036007028 scopus 로고    scopus 로고
    • ABA and sugar interactions regulating development: Cross-talk or voices in a crowd?
    • Finkelstein RR, Gibson SI (2002) ABA and sugar interactions regulating development: Cross-talk or voices in a crowd? Curr Opin Plant Biol 5: 26-32
    • (2002) Curr Opin Plant Biol , vol.5 , pp. 26-32
    • Finkelstein, R.R.1    Gibson, S.I.2
  • 10
    • 0035847109 scopus 로고    scopus 로고
    • Specific interactions at the regulatory domain-substrate binding domain interface influence the cooperativity of inhibition and effector binding in Escherichia coli D-3-phosphoglycerate dehydrogenase
    • Grant GA, Hu Z, Xu XL (2001) Specific interactions at the regulatory domain-substrate binding domain interface influence the cooperativity of inhibition and effector binding in Escherichia coli D-3-phosphoglycerate dehydrogenase. J Biol Chem 276: 1078-1083
    • (2001) J Biol Chem , vol.276 , pp. 1078-1083
    • Grant, G.A.1    Hu, Z.2    Xu, X.L.3
  • 11
    • 0344076344 scopus 로고    scopus 로고
    • The contribution of adjacent subunits to the active sites of D-3-phosphoglycerate dehydrogenase
    • Grant GA, Kim SJ, Xu XL, Hu Z (1999) The contribution of adjacent subunits to the active sites of D-3-phosphoglycerate dehydrogenase. J Biol Chem 274: 5357-5361
    • (1999) J Biol Chem , vol.274 , pp. 5357-5361
    • Grant, G.A.1    Kim, S.J.2    Xu, X.L.3    Hu, Z.4
  • 12
    • 0032898091 scopus 로고    scopus 로고
    • Regulation of serine biosynthesis in Arabidopsis: Crucial role of plastidic 3-phosphoglycerate dehydrogenase in non-photosynthetic tissues
    • Ho CL, Noji M, Saito M, Saito K (1999) Regulation of serine biosynthesis in Arabidopsis: Crucial role of plastidic 3-phosphoglycerate dehydrogenase in non-photosynthetic tissues. J Biol Chem 274: 397-402
    • (1999) J Biol Chem , vol.274 , pp. 397-402
    • Ho, C.L.1    Noji, M.2    Saito, M.3    Saito, K.4
  • 13
  • 14
    • 0002077139 scopus 로고
    • Influence of ionic strength, pH and chelation of divalent metals on isolation of polyribosomes from tobacco leaves
    • Jackson AD, Larkins BA (1976) Influence of ionic strength, pH and chelation of divalent metals on isolation of polyribosomes from tobacco leaves. Plant Physiol 57: 5-10
    • (1976) Plant Physiol , vol.57 , pp. 5-10
    • Jackson, A.D.1    Larkins, B.A.2
  • 15
    • 0342444416 scopus 로고
    • GUS fusions: Betaglucuronidase as a sensitive and versatile gene fusion marker in higher plants
    • Jefferson RA, Kavanagh TA, Bevan MW (1987) GUS fusions: Betaglucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO J 6: 3901-3907
    • (1987) EMBO J , vol.6 , pp. 3901-3907
    • Jefferson, R.A.1    Kavanagh, T.A.2    Bevan, M.W.3
  • 16
    • 0033039869 scopus 로고    scopus 로고
    • Mutational analysis of the feedback sites of lysine-sensitive aspartokinase of Escherichia coli
    • Kikuchi Y, Kojima H, Tanaka T (1999) Mutational analysis of the feedback sites of lysine-sensitive aspartokinase of Escherichia coli. FEMS Microbiol Lett 173: 211-215
    • (1999) FEMS Microbiol Lett , vol.173 , pp. 211-215
    • Kikuchi, Y.1    Kojima, H.2    Tanaka, T.3
  • 19
    • 0032213203 scopus 로고    scopus 로고
    • Reciprocal regulation of distinct asparagine synthetase genes by light and metabolites in Arabidopsis thaliana
    • Lam HM, Hsieh MH, Coruzzi G (1998b) Reciprocal regulation of distinct asparagine synthetase genes by light and metabolites in Arabidopsis thaliana. Plant J 16: 345-353
    • (1998) Plant J , vol.16 , pp. 345-353
    • Lam, H.M.1    Hsieh, M.H.2    Coruzzi, G.3
  • 20
    • 0035849510 scopus 로고    scopus 로고
    • Identification of the regulatory subunit of Arabidopsis thaliana acetohydroxyacid synthase and reconstitution with its catalytic subunit
    • Lee YT, Duggleby RG (2001) Identification of the regulatory subunit of Arabidopsis thaliana acetohydroxyacid synthase and reconstitution with its catalytic subunit. Biochemistry 40: 6836-6844
    • (2001) Biochemistry , vol.40 , pp. 6836-6844
    • Lee, Y.T.1    Duggleby, R.G.2
  • 21
    • 0035896041 scopus 로고    scopus 로고
    • Acetohydroxyacid synthase: A proposed structure for regulatory subunits supported by evidence from mutagenesis
    • Mendel S, Elkayam T, Sella C, Vinogradov V, Vyazmensky M, Chipman DM, Barak Z (2001) Acetohydroxyacid synthase: A proposed structure for regulatory subunits supported by evidence from mutagenesis. J Mol Biol 307: 465-477
    • (2001) J Mol Biol , vol.307 , pp. 465-477
    • Mendel, S.1    Elkayam, T.2    Sella, C.3    Vinogradov, V.4    Vyazmensky, M.5    Chipman, D.M.6    Barak, Z.7
  • 22
    • 0026085514 scopus 로고
    • Producing single-stranded DNA probes with the Taq DNA polymerase: A high yield protocol
    • Myerson D (1991) Producing single-stranded DNA probes with the Taq DNA polymerase: A high yield protocol. Biotechniques 10: 35-38
    • (1991) Biotechniques , vol.10 , pp. 35-38
    • Myerson, D.1
  • 23
  • 24
    • 0027513393 scopus 로고
    • Nucleotide sequence of the Serratia marcescens threonine operon and analysis of the threonine operon mutations which alter feedback inhibition of both aspartokinase I and homoserine dehydrogenase I
    • Omori K, Imai Y, Suzuki S, Komatsubara S (1993) Nucleotide sequence of the Serratia marcescens threonine operon and analysis of the threonine operon mutations which alter feedback inhibition of both aspartokinase I and homoserine dehydrogenase I. J Bacteriol 175: 785-794
    • (1993) J Bacteriol , vol.175 , pp. 785-794
    • Omori, K.1    Imai, Y.2    Suzuki, S.3    Komatsubara, S.4
  • 25
    • 0027400945 scopus 로고
    • Role of serine 352 in the allosteric response of Serratia marcescens aspartokinase 1-homoserine dehydrogenase I analyzed by using site-directed mutagenesis
    • Omori K, Komatsubara S (1993) Role of serine 352 in the allosteric response of Serratia marcescens aspartokinase 1-homoserine dehydrogenase I analyzed by using site-directed mutagenesis. J Bacteriol 175: 959-965
    • (1993) J Bacteriol , vol.175 , pp. 959-965
    • Omori, K.1    Komatsubara, S.2
  • 26
    • 0030203778 scopus 로고    scopus 로고
    • The various strategies within the TyrR regulation of Escherichia coli to modulate gene expression
    • Pittard J (1996) The various strategies within the TyrR regulation of Escherichia coli to modulate gene expression. Genes Cells 1: 717-725
    • (1996) Genes Cells , vol.1 , pp. 717-725
    • Pittard, J.1
  • 27
    • 0022295062 scopus 로고
    • The role of adenylyltransferase and uridylyltransferase in the regulation of glutamine synthetase in Escherichia coli
    • Rhee SG, Park SC, Koo JH (1985) The role of adenylyltransferase and uridylyltransferase in the regulation of glutamine synthetase in Escherichia coli. Curr Top Cell Reg 27: 221-232
    • (1985) Curr Top Cell Reg , vol.27 , pp. 221-232
    • Rhee, S.G.1    Park, S.C.2    Koo, J.H.3
  • 28
    • 0026078249 scopus 로고
    • Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of bipartite nuclear targeting sequence
    • Robbins J, Dilworth SM, Laskey RA, Dingwall C (1991) Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of bipartite nuclear targeting sequence. Cell 64: 615-623
    • (1991) Cell , vol.64 , pp. 615-623
    • Robbins, J.1    Dilworth, S.M.2    Laskey, R.A.3    Dingwall, C.4
  • 29
    • 0032078837 scopus 로고    scopus 로고
    • A response-regulator homologue possibly involved in nitrogen signal transduction mediated by cytokinin in maize
    • Sakakibara H, Suzuki M, Takei K, Deji A, Taniguchi M, Sugiyama T (1998) A response-regulator homologue possibly involved in nitrogen signal transduction mediated by cytokinin in maize. Plant J 14: 337-344
    • (1998) Plant J , vol.14 , pp. 337-344
    • Sakakibara, H.1    Suzuki, M.2    Takei, K.3    Deji, A.4    Taniguchi, M.5    Sugiyama, T.6
  • 30
    • 0028951187 scopus 로고
    • The allosteric ligand site in the V-max-type cooperative enzyme phosphoglycerate dehydrogenase
    • Schuller DJ, Grant GA, Banaszak LJ (1995) The allosteric ligand site in the V-max-type cooperative enzyme phosphoglycerate dehydrogenase. Nat Struct Biol 2: 69-76
    • (1995) Nat Struct Biol , vol.2 , pp. 69-76
    • Schuller, D.J.1    Grant, G.A.2    Banaszak, L.J.3
  • 31
    • 0023955699 scopus 로고
    • Kinetic and regulatory properties of arogenate dehydratase in seedlings of Sorghum bicolor (L.) Moench
    • Siehl DL, Conn EE (1988) Kinetic and regulatory properties of arogenate dehydratase in seedlings of Sorghum bicolor (L.) Moench. Arch Biochem Biophys 260: 822-829
    • (1988) Arch Biochem Biophys , vol.260 , pp. 822-829
    • Siehl, D.L.1    Conn, E.E.2
  • 32
    • 0035129207 scopus 로고    scopus 로고
    • Nitrogen-dependent accumulation of cytokinins in root and the translocation to leaf: Implication of cytokinin species that induces gene expression of maize response regulator
    • Takei K, Sakakibara H, Taniguchi M, Sugiyama T (2001) Nitrogen-dependent accumulation of cytokinins in root and the translocation to leaf: Implication of cytokinin species that induces gene expression of maize response regulator. Plant Cell Physiol 42: 85-93
    • (2001) Plant Cell Physiol , vol.42 , pp. 85-93
    • Takei, K.1    Sakakibara, H.2    Taniguchi, M.3    Sugiyama, T.4
  • 33
    • 0036010145 scopus 로고    scopus 로고
    • Multiple routes communicating nitrogen availability from roots to shoots: A signal transduction pathway mediated by cytokinin
    • Takei K, Takahashi T, Sugiyama T, Yamaya T, Sakakibara H (2002) Multiple routes communicating nitrogen availability from roots to shoots: A signal transduction pathway mediated by cytokinin. J Exp Bot 53: 971-977
    • (2002) J Exp Bot , vol.53 , pp. 971-977
    • Takei, K.1    Takahashi, T.2    Sugiyama, T.3    Yamaya, T.4    Sakakibara, H.5
  • 34
    • 0034860917 scopus 로고    scopus 로고
    • The central enzymes of the aspartate family of amino acid biosynthesis
    • Viola RE (2001) The central enzymes of the aspartate family of amino acid biosynthesis. Acc Chem Res 34: 339-349
    • (2001) Acc Chem Res , vol.34 , pp. 339-349
    • Viola, R.E.1
  • 35
    • 0034642216 scopus 로고    scopus 로고
    • Evidence for two distinct effector-binding sites in threonine deaminase by site-directed mutagenesis, kinetic, and binding experiments
    • Wessel PM, Graciet E, Douce R, Dumas R (2000) Evidence for two distinct effector-binding sites in threonine deaminase by site-directed mutagenesis, kinetic, and binding experiments. Biochemistry 39: 15136-15143
    • (2000) Biochemistry , vol.39 , pp. 15136-15143
    • Wessel, P.M.1    Graciet, E.2    Douce, R.3    Dumas, R.4
  • 36
    • 0029144438 scopus 로고
    • Evidence for two aromatic amino acid-binding sites, one ATP-dependent and the other ATP-independent, in the Escherchia coli regulatory protein TyrR
    • Wilson TJ, Argaet VP, Howlett GJ, Davidson BE (1995) Evidence for two aromatic amino acid-binding sites, one ATP-dependent and the other ATP-independent, in the Escherchia coli regulatory protein TyrR. Mol Microbiol 17: 483-492
    • (1995) Mol Microbiol , vol.17 , pp. 483-492
    • Wilson, T.J.1    Argaet, V.P.2    Howlett, G.J.3    Davidson, B.E.4
  • 37
    • 0032513052 scopus 로고    scopus 로고
    • Chorismate mutase-prephenate dehydratase from Escherichia coli: Study of catalytic and regulatory domains using genetically engineered proteins
    • Zhang S, Pohnert G, Kongsaeree P, Wilson DB, Clardy J, Ganem B (1998) Chorismate mutase-prephenate dehydratase from Escherichia coli: Study of catalytic and regulatory domains using genetically engineered proteins. J Biol Chem 273: 6248-6253
    • (1998) J Biol Chem , vol.273 , pp. 6248-6253
    • Zhang, S.1    Pohnert, G.2    Kongsaeree, P.3    Wilson, D.B.4    Clardy, J.5    Ganem, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.