메뉴 건너뛰기




Volumn 290, Issue 28, 2015, Pages 17321-17330

Adaptive engineering of phytochelatin-based heavy metal tolerance

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CADMIUM; CATALYST ACTIVITY; ENZYMES; GROUNDWATER; HEAVY METALS; METABOLISM; METABOLITES; PEPTIDES; PLANTS (BOTANY); SOIL POLLUTION; YEAST;

EID: 84940069336     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.652123     Document Type: Article
Times cited : (28)

References (59)
  • 3
    • 0035118386 scopus 로고    scopus 로고
    • Directed molecular evolution in plant improvement
    • Lassner, M., and Bedbrook, J. (2001) Directed molecular evolution in plant improvement. Curr. Opin. Plant Biol. 4, 152-156
    • (2001) Curr. Opin. Plant Biol. , vol.4 , pp. 152-156
    • Lassner, M.1    Bedbrook, J.2
  • 4
    • 0029919514 scopus 로고    scopus 로고
    • Mercuric ion reduction and resistance in transgenic Arabidopsis thaliana plants expressing a modified bacterial merA gene
    • Rugh, C. L., Wilde, H. D., Stack, N. M., Thompson, D. M., Summers, A. O., and Meagher, R. B. (1996) Mercuric ion reduction and resistance in transgenic Arabidopsis thaliana plants expressing a modified bacterial merA gene. Proc. Natl. Acad. Sci. U.S.A. 93, 3182-3187
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 3182-3187
    • Rugh, C.L.1    Wilde, H.D.2    Stack, N.M.3    Thompson, D.M.4    Summers, A.O.5    Meagher, R.B.6
  • 5
    • 0033951201 scopus 로고    scopus 로고
    • Phytodetoxification of hazardous organomercurials by genetically engineered plants
    • Bizily, S. P., Rugh, C. L., and Meagher, R. B. (2000) Phytodetoxification of hazardous organomercurials by genetically engineered plants. Nat. Biotechnol. 18, 213-217
    • (2000) Nat. Biotechnol. , vol.18 , pp. 213-217
    • Bizily, S.P.1    Rugh, C.L.2    Meagher, R.B.3
  • 6
    • 0036843447 scopus 로고    scopus 로고
    • Engineering tolerance and hyperaccumulation of arsenic in plants by combining arsenate reductase and γ-glutamylcysteine synthetase expression
    • Dhankher, O. P., Li, Y., Rosen, B. P., Shi, J., Salt, D., Senecoff, J. F., Sashti, N. A., and Meagher, R. B. (2002) Engineering tolerance and hyperaccumulation of arsenic in plants by combining arsenate reductase and γ-glutamylcysteine synthetase expression. Nat. Biotechnol. 20, 1140-1145
    • (2002) Nat. Biotechnol. , vol.20 , pp. 1140-1145
    • Dhankher, O.P.1    Li, Y.2    Rosen, B.P.3    Shi, J.4    Salt, D.5    Senecoff, J.F.6    Sashti, N.A.7    Meagher, R.B.8
  • 8
    • 79961093413 scopus 로고    scopus 로고
    • Toward protein engineering for phytoremediation: Possibilities and challenges
    • Jez, J. M. (2011) Toward protein engineering for phytoremediation: possibilities and challenges. Int. J. Phytoremediation 13, 77-89
    • (2011) Int. J. Phytoremediation , vol.13 , pp. 77-89
    • Jez, J.M.1
  • 9
    • 84873180865 scopus 로고    scopus 로고
    • Plant science: The key to preventing slow cadmium poisoning
    • Clemens, S., Aarts, M. G., Thomine, S., and Verbruggen, N. (2013) Plant science: the key to preventing slow cadmium poisoning. Trends Plant Sci. 18, 92-99
    • (2013) Trends Plant Sci. , vol.18 , pp. 92-99
    • Clemens, S.1    Aarts, M.G.2    Thomine, S.3    Verbruggen, N.4
  • 10
    • 0037002169 scopus 로고    scopus 로고
    • Phytochelatins and metallothioneins: Roles in heavy metal detoxification and homeostasis
    • Cobbett, C., and Goldsbrough, P. (2002) Phytochelatins and metallothioneins: roles in heavy metal detoxification and homeostasis. Annu. Rev. Plant Biol. 53, 159-182
    • (2002) Annu. Rev. Plant Biol. , vol.53 , pp. 159-182
    • Cobbett, C.1    Goldsbrough, P.2
  • 11
    • 0033535991 scopus 로고    scopus 로고
    • AtPCS1, a phytochelatin synthase from Arabidopsis: Isolation and in vitro reconstitution
    • Vatamaniuk, O. K., Mari, S., Lu, Y. P., and Rea, P. A. (1999) AtPCS1, a phytochelatin synthase from Arabidopsis: isolation and in vitro reconstitution. Proc. Natl. Acad. Sci. U.S.A. 96, 7110-7115
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 7110-7115
    • Vatamaniuk, O.K.1    Mari, S.2    Lu, Y.P.3    Rea, P.A.4
  • 13
    • 0033564244 scopus 로고    scopus 로고
    • Tolerance to toxic metals by a gene family of phytochelatin synthases from plants and yeast
    • Clemens, S., Kim, E. J., Neumann, D., and Schroeder, J. I. (1999) Tolerance to toxic metals by a gene family of phytochelatin synthases from plants and yeast. EMBO J. 18, 3325-3333
    • (1999) EMBO J. , vol.18 , pp. 3325-3333
    • Clemens, S.1    Kim, E.J.2    Neumann, D.3    Schroeder, J.I.4
  • 14
    • 0029278660 scopus 로고
    • Cadmium-sensitive, cad1 mutants of Arabidopsis thaliana are phytochelatin deficient
    • Howden, R., Goldsbrough, P. B., Andersen, C. R., and Cobbett, C. S. (1995) Cadmium-sensitive, cad1 mutants of Arabidopsis thaliana are phytochelatin deficient. Plant Physiol. 107, 1059-1066
    • (1995) Plant Physiol. , vol.107 , pp. 1059-1066
    • Howden, R.1    Goldsbrough, P.B.2    Andersen, C.R.3    Cobbett, C.S.4
  • 15
    • 0029278723 scopus 로고
    • A cadmium-sensitive, glutathione-deficient mutant of Arabidopsis thaliana
    • Howden, R., Andersen, C. R., Goldsbrough, P. B., and Cobbett, C. S. (1995) A cadmium-sensitive, glutathione-deficient mutant of Arabidopsis thaliana. Plant Physiol. 107, 1067-1073
    • (1995) Plant Physiol. , vol.107 , pp. 1067-1073
    • Howden, R.1    Andersen, C.R.2    Goldsbrough, P.B.3    Cobbett, C.S.4
  • 16
    • 84859835900 scopus 로고    scopus 로고
    • Phytochelatin synthase: Of a protease a peptide polymerase made
    • Rea, P. A. (2012) Phytochelatin synthase: of a protease a peptide polymerase made. Physiol. Plant. 145, 154-164
    • (2012) Physiol. Plant. , vol.145 , pp. 154-164
    • Rea, P.A.1
  • 17
    • 0034613243 scopus 로고    scopus 로고
    • Mechanism of heavy metal ion activation of phytochelatin (PC) synthase: Blocked thiols are sufficient for PC synthase-catalyzed transpeptidation of glutathione and related thiol peptides
    • Vatamaniuk, O. K., Mari, S., Lu, Y. P., and Rea, P. A. (2000) Mechanism of heavy metal ion activation of phytochelatin (PC) synthase: blocked thiols are sufficient for PC synthase-catalyzed transpeptidation of glutathione and related thiol peptides. J. Biol. Chem. 275, 31451-31459
    • (2000) J. Biol. Chem. , vol.275 , pp. 31451-31459
    • Vatamaniuk, O.K.1    Mari, S.2    Lu, Y.P.3    Rea, P.A.4
  • 18
    • 2542475908 scopus 로고    scopus 로고
    • Phytochelatin synthase, a dipeptidyltransferase that undergoes multisite acylation with γ-glutamylcysteine during catalysis: Stoichiometric and site-directed mutagenic analysis of Arabidopsis thaliana PCS1-catalyzed phytochelatin synthesis
    • Vatamaniuk, O. K., Mari, S., Lang, A., Chalasani, S., Demkiv, L. O., and Rea, P. A. (2004) Phytochelatin synthase, a dipeptidyltransferase that undergoes multisite acylation with γ-glutamylcysteine during catalysis: stoichiometric and site-directed mutagenic analysis of Arabidopsis thaliana PCS1-catalyzed phytochelatin synthesis. J. Biol. Chem. 279, 22449-22460
    • (2004) J. Biol. Chem. , vol.279 , pp. 22449-22460
    • Vatamaniuk, O.K.1    Mari, S.2    Lang, A.3    Chalasani, S.4    Demkiv, L.O.5    Rea, P.A.6
  • 21
    • 84855681112 scopus 로고    scopus 로고
    • The phytochelatin transporters AtABCC1 and AtABCC2 mediate tolerance to cadmium and mercury
    • Park, J., Song, W. Y., Ko, D., Eom, Y., Hansen, T. H., Schiller, M., Lee, T. G., Martinoia, E., and Lee, Y. (2012) The phytochelatin transporters AtABCC1 and AtABCC2 mediate tolerance to cadmium and mercury. Plant J. 69, 278-288
    • (2012) Plant J. , vol.69 , pp. 278-288
    • Park, J.1    Song, W.Y.2    Ko, D.3    Eom, Y.4    Hansen, T.H.5    Schiller, M.6    Lee, T.G.7    Martinoia, E.8    Lee, Y.9
  • 22
    • 16544384050 scopus 로고    scopus 로고
    • Weeds, worms, and more: Papain's long-lost cousin, phytochelatin synthase
    • Rea, P. A., Vatamaniuk, O. K., and Rigden, D. J. (2004) Weeds, worms, and more: papain's long-lost cousin, phytochelatin synthase. Plant Physiol. 136, 2463-2474
    • (2004) Plant Physiol. , vol.136 , pp. 2463-2474
    • Rea, P.A.1    Vatamaniuk, O.K.2    Rigden, D.J.3
  • 23
    • 0035877698 scopus 로고    scopus 로고
    • A new pathway for heavy metal detoxification in animals: Phytochelatin synthase is required for cadmium tolerance in Caenorhabditis elegans
    • Vatamaniuk, O. K., Bucher, E. A., Ward, J. T., and Rea, P. A. (2001) A new pathway for heavy metal detoxification in animals: phytochelatin synthase is required for cadmium tolerance in Caenorhabditis elegans. J. Biol. Chem. 276, 20817-20820
    • (2001) J. Biol. Chem. , vol.276 , pp. 20817-20820
    • Vatamaniuk, O.K.1    Bucher, E.A.2    Ward, J.T.3    Rea, P.A.4
  • 24
    • 2442427592 scopus 로고    scopus 로고
    • Domain organization of phytochelatin synthase: Functional properties of truncated enzyme species identified by limited proteolysis
    • Ruotolo, R., Peracchi, A., Bolchi, A., Infusini, G., Amoresano, A., and Ottonello, S. (2004) Domain organization of phytochelatin synthase: functional properties of truncated enzyme species identified by limited proteolysis. J. Biol. Chem. 279, 14686-14693
    • (2004) J. Biol. Chem. , vol.279 , pp. 14686-14693
    • Ruotolo, R.1    Peracchi, A.2    Bolchi, A.3    Infusini, G.4    Amoresano, A.5    Ottonello, S.6
  • 25
    • 30044442427 scopus 로고    scopus 로고
    • A papain-like enzyme at work: Native and acyl-enzyme intermediate structures in phytochelatin synthesis
    • Vivares, D., Arnoux, P., and Pignol, D. (2005) A papain-like enzyme at work: native and acyl-enzyme intermediate structures in phytochelatin synthesis. Proc. Natl. Acad. Sci. U.S.A. 102, 18848-18853
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 18848-18853
    • Vivares, D.1    Arnoux, P.2    Pignol, D.3
  • 26
    • 33745960735 scopus 로고    scopus 로고
    • Mutagenic definition of a papain-like catalytic triad, sufficiency of the N-terminal domain for single-site core catalytic enzyme acylation, and C-terminal domain for augmentative metal activation of a eukaryotic phytochelatin synthase
    • Romanyuk, N. D., Rigden, D. J., Vatamaniuk, O. K., Lang, A., Cahoon, R. E., Jez, J. M., and Rea, P. A. (2006) Mutagenic definition of a papain-like catalytic triad, sufficiency of the N-terminal domain for single-site core catalytic enzyme acylation, and C-terminal domain for augmentative metal activation of a eukaryotic phytochelatin synthase. Plant Physiol. 141, 858-869
    • (2006) Plant Physiol. , vol.141 , pp. 858-869
    • Romanyuk, N.D.1    Rigden, D.J.2    Vatamaniuk, O.K.3    Lang, A.4    Cahoon, R.E.5    Jez, J.M.6    Rea, P.A.7
  • 27
    • 0030743851 scopus 로고    scopus 로고
    • AtMRP1 gene of Arabidopsis encodes a glutathione S-conjugate pump: Isolation and functional definition of a plant ATP-binding cassette transporter gene
    • Lu, Y. P., Li, Z. S., and Rea, P. A. (1997) AtMRP1 gene of Arabidopsis encodes a glutathione S-conjugate pump: isolation and functional definition of a plant ATP-binding cassette transporter gene. Proc. Natl. Acad. Sci. U.S.A. 94, 8243-8248
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 8243-8248
    • Lu, Y.P.1    Li, Z.S.2    Rea, P.A.3
  • 28
    • 0031013876 scopus 로고    scopus 로고
    • A new pathway for vacuolar cadmium sequestration in Saccharomyces cerevisiae: YCF1-catalyzed transport of bis(glutathionato)cadmium
    • Li, Z. S., Lu, Y. P., Zhen, R. G., Szczypka, M., Thiele, D. J., and Rea, P. A. (1997) A new pathway for vacuolar cadmium sequestration in Saccharomyces cerevisiae: YCF1-catalyzed transport of bis(glutathionato)cadmium. Proc. Natl. Acad. Sci. U.S.A. 94, 42-47
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 42-47
    • Li, Z.S.1    Lu, Y.P.2    Zhen, R.G.3    Szczypka, M.4    Thiele, D.J.5    Rea, P.A.6
  • 29
    • 0029983266 scopus 로고    scopus 로고
    • The yeast cadmium factor protein (YCF1) is a vacuolar glutathione S-conjugate pump
    • Li, Z. S., Szczypka, M., Lu, Y. P., Thiele, D. J., and Rea, P. A. (1996) The yeast cadmium factor protein (YCF1) is a vacuolar glutathione S-conjugate pump. J. Biol. Chem. 271, 6509-6517
    • (1996) J. Biol. Chem. , vol.271 , pp. 6509-6517
    • Li, Z.S.1    Szczypka, M.2    Lu, Y.P.3    Thiele, D.J.4    Rea, P.A.5
  • 30
    • 0027012738 scopus 로고
    • A versatile binary vector system with a T-DNA organisational structure conducive to efficient integration of cloned DNA into the plant genome
    • Gleave, A. P. (1992) A versatile binary vector system with a T-DNA organisational structure conducive to efficient integration of cloned DNA into the plant genome. Plant Mol. Biol. 20, 1203-1207
    • (1992) Plant Mol. Biol. , vol.20 , pp. 1203-1207
    • Gleave, A.P.1
  • 31
    • 0032838738 scopus 로고    scopus 로고
    • Overexpression of glutathione synthetase in indian mustard enhances cadmium accumulation and tolerance
    • Liang Zhu, Y., Pilon-Smits, E. A., Jouanin, L., and Terry, N. (1999) Overexpression of glutathione synthetase in indian mustard enhances cadmium accumulation and tolerance. Plant Physiol. 119, 73-80
    • (1999) Plant Physiol. , vol.119 , pp. 73-80
    • Liang Zhu, Y.1    Pilon-Smits, E.A.2    Jouanin, L.3    Terry, N.4
  • 32
    • 0001076785 scopus 로고    scopus 로고
    • Cadmium tolerance and accumulation in Indian mustard is enhanced by overexpressing γ-glutamylcysteine synthetase
    • Zhu, Y. L., Pilon-Smits, E. A., Tarun, A. S., Weber, S. U., Jouanin, L., and Terry, N. (1999) Cadmium tolerance and accumulation in Indian mustard is enhanced by overexpressing γ-glutamylcysteine synthetase. Plant Physiol. 121, 1169-1178
    • (1999) Plant Physiol. , vol.121 , pp. 1169-1178
    • Zhu, Y.L.1    Pilon-Smits, E.A.2    Tarun, A.S.3    Weber, S.U.4    Jouanin, L.5    Terry, N.6
  • 33
    • 78649762173 scopus 로고    scopus 로고
    • Essential role of glutathione in acclimation to environmental and redox perturbations in the cyanobacterium Synechocystis sp. PCC 6803
    • Cameron, J. C., and Pakrasi, H. B. (2010) Essential role of glutathione in acclimation to environmental and redox perturbations in the cyanobacterium Synechocystis sp. PCC 6803. Plant Physiol. 154, 1672-1685
    • (2010) Plant Physiol. , vol.154 , pp. 1672-1685
    • Cameron, J.C.1    Pakrasi, H.B.2
  • 34
    • 0019167355 scopus 로고
    • Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine
    • Griffith, O. W. (1980) Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine. Anal. Biochem. 106, 207-212
    • (1980) Anal. Biochem. , vol.106 , pp. 207-212
    • Griffith, O.W.1
  • 35
    • 12244287603 scopus 로고    scopus 로고
    • Overexpression of Arabidopsis phytochelatin synthase paradoxically leads to hypersensitivity to cadmium stress
    • Lee, S., Moon, J. S., Ko, T. S., Petros, D., Goldsbrough, P. B., and Korban, S. S. (2003) Overexpression of Arabidopsis phytochelatin synthase paradoxically leads to hypersensitivity to cadmium stress. Plant Physiol. 131, 656-663
    • (2003) Plant Physiol. , vol.131 , pp. 656-663
    • Lee, S.1    Moon, J.S.2    Ko, T.S.3    Petros, D.4    Goldsbrough, P.B.5    Korban, S.S.6
  • 36
    • 12444322132 scopus 로고    scopus 로고
    • Overexpression of phytochelatin synthase in Arabidopsis leads to enhanced arsenic tolerance and cadmium hypersensitivity
    • Li, Y., Dhankher, O. P., Carreira, L., Lee, D., Chen, A., Schroeder, J. I., Balish, R. S., and Meagher, R. B. (2004) Overexpression of phytochelatin synthase in Arabidopsis leads to enhanced arsenic tolerance and cadmium hypersensitivity. Plant Cell Physiol. 45, 1787-1797
    • (2004) Plant Cell Physiol. , vol.45 , pp. 1787-1797
    • Li, Y.1    Dhankher, O.P.2    Carreira, L.3    Lee, D.4    Chen, A.5    Schroeder, J.I.6    Balish, R.S.7    Meagher, R.B.8
  • 38
    • 34249783484 scopus 로고    scopus 로고
    • Transgenic Indian mustard (Brassica juncea) plants expressing an Arabidopsis phytochelatin synthase (At-PCS1) exhibit enhanced As and Cd tolerance
    • Gasic, K., and Korban, S. S. (2007) Transgenic Indian mustard (Brassica juncea) plants expressing an Arabidopsis phytochelatin synthase (At-PCS1) exhibit enhanced As and Cd tolerance. Plant Mol. Biol. 64, 361-369
    • (2007) Plant Mol. Biol. , vol.64 , pp. 361-369
    • Gasic, K.1    Korban, S.S.2
  • 39
    • 33947252342 scopus 로고    scopus 로고
    • Expression of Arabidopsis phytochelatin synthase in Indian mustard (Brassica juncea) plants enhances tolerance for Cd and Zn
    • Gasic, K., and Korban, S. S. (2007) Expression of Arabidopsis phytochelatin synthase in Indian mustard (Brassica juncea) plants enhances tolerance for Cd and Zn. Planta 225, 1277-1285
    • (2007) Planta , vol.225 , pp. 1277-1285
    • Gasic, K.1    Korban, S.S.2
  • 40
    • 0036030038 scopus 로고    scopus 로고
    • Phytoremediation of metals using transgenic plants
    • Pilon-Smits, E. A., and Pilon, M. (2002) Phytoremediation of metals using transgenic plants. Crit. Rev. Plant Sci. 21, 439-456
    • (2002) Crit. Rev. Plant Sci. , vol.21 , pp. 439-456
    • Pilon-Smits, E.A.1    Pilon, M.2
  • 41
    • 84891935769 scopus 로고    scopus 로고
    • Tentative identification of the second substrate binding site in Arabidopsis phytochelatin synthase
    • Chia, J. C., Yang, C. C., Sui, Y. T., Lin, S. Y., and Juang, R. H. (2013) Tentative identification of the second substrate binding site in Arabidopsis phytochelatin synthase. PLoS One 8, e82675
    • (2013) PLoS One , vol.8
    • Chia, J.C.1    Yang, C.C.2    Sui, Y.T.3    Lin, S.Y.4    Juang, R.H.5
  • 42
    • 0002430320 scopus 로고
    • Termination of the phytochelatin synthase reaction through sequestration of heavy metals by the reaction product
    • Loeffler, S., Hochberger, A., Grill, E., Winnacker, E. L., and Zenk, M. H. (1989) Termination of the phytochelatin synthase reaction through sequestration of heavy metals by the reaction product. FEBS Lett. 258, 42-46
    • (1989) FEBS Lett. , vol.258 , pp. 42-46
    • Loeffler, S.1    Hochberger, A.2    Grill, E.3    Winnacker, E.L.4    Zenk, M.H.5
  • 43
    • 42249088093 scopus 로고    scopus 로고
    • Reconciling the chemistry and biology of reactive oxygen species
    • Winterbourn, C. C. (2008) Reconciling the chemistry and biology of reactive oxygen species. Nat. Chem. Biol. 4, 278-286
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 278-286
    • Winterbourn, C.C.1
  • 44
    • 0029197657 scopus 로고
    • Glutathione biosynthesis and its inhibition
    • Meister, A. (1995) Glutathione biosynthesis and its inhibition. Methods Enzymol. 252, 26-30
    • (1995) Methods Enzymol. , vol.252 , pp. 26-30
    • Meister, A.1
  • 45
    • 4043059910 scopus 로고    scopus 로고
    • Arabidopsis thaliana glutamate-cysteine ligase: Functional properties, kinetic mechanism, and regulation of activity
    • Jez, J. M., Cahoon, R. E., and Chen, S. (2004) Arabidopsis thaliana glutamate-cysteine ligase: functional properties, kinetic mechanism, and regulation of activity. J. Biol. Chem. 279, 33463-33470
    • (2004) J. Biol. Chem. , vol.279 , pp. 33463-33470
    • Jez, J.M.1    Cahoon, R.E.2    Chen, S.3
  • 46
    • 5644261234 scopus 로고    scopus 로고
    • Kinetic mechanism of glutathione synthetase from Arabidopsis thaliana
    • Jez, J. M., and Cahoon, R. E. (2004) Kinetic mechanism of glutathione synthetase from Arabidopsis thaliana. J. Biol. Chem. 279, 42726-42731
    • (2004) J. Biol. Chem. , vol.279 , pp. 42726-42731
    • Jez, J.M.1    Cahoon, R.E.2
  • 47
    • 35348880995 scopus 로고    scopus 로고
    • Thiol-based regulation of redox-active glutamate-cysteine ligase from Arabidopsis thaliana
    • Hicks, L. M., Cahoon, R. E., Bonner, E. R., Rivard, R. S., Sheffield, J., and Jez, J. M. (2007) Thiol-based regulation of redox-active glutamate-cysteine ligase from Arabidopsis thaliana. Plant Cell 19, 2653-2661
    • (2007) Plant Cell , vol.19 , pp. 2653-2661
    • Hicks, L.M.1    Cahoon, R.E.2    Bonner, E.R.3    Rivard, R.S.4    Sheffield, J.5    Jez, J.M.6
  • 49
    • 33748753075 scopus 로고    scopus 로고
    • Structural basis for the redox control of plant glutamate cysteine ligase
    • Hothorn, M., Wachter, A., Gromes, R., Stuwe, T., Rausch, T., and Scheffzek, K. (2006) Structural basis for the redox control of plant glutamate cysteine ligase. J. Biol. Chem. 281, 27557-27665
    • (2006) J. Biol. Chem. , vol.281 , pp. 27557-27665
    • Hothorn, M.1    Wachter, A.2    Gromes, R.3    Stuwe, T.4    Rausch, T.5    Scheffzek, K.6
  • 50
    • 44849098699 scopus 로고    scopus 로고
    • The redox switch of γ-glutamylcysteine ligase via a reversible monomer-dimer transition is a mechanism unique to plants
    • Gromes, R., Hothorn, M., Lenherr, E. D., Rybin, V., Scheffzek, K., and Rausch, T. (2008) The redox switch of γ-glutamylcysteine ligase via a reversible monomer-dimer transition is a mechanism unique to plants. Plant J. 54, 1063-1075
    • (2008) Plant J. , vol.54 , pp. 1063-1075
    • Gromes, R.1    Hothorn, M.2    Lenherr, E.D.3    Rybin, V.4    Scheffzek, K.5    Rausch, T.6
  • 51
    • 77950261020 scopus 로고    scopus 로고
    • Sensing sulfur conditions: Simple to complex protein regulatory mechanisms in plant thiol metabolism
    • Yi, H., Galant, A., Ravilious, G. E., Preuss, M. L., and Jez, J. M. (2010) Sensing sulfur conditions: simple to complex protein regulatory mechanisms in plant thiol metabolism. Mol. Plant 3, 269-279
    • (2010) Mol. Plant , vol.3 , pp. 269-279
    • Yi, H.1    Galant, A.2    Ravilious, G.E.3    Preuss, M.L.4    Jez, J.M.5
  • 52
    • 84855991671 scopus 로고    scopus 로고
    • Structural basis and evolution of redox regulation in plant adenosine-5′-phosphosulfate kinase
    • Ravilious, G. E., Nguyen, A., Francois, J. A., and Jez, J. M. (2012) Structural basis and evolution of redox regulation in plant adenosine-5′-phosphosulfate kinase. Proc. Natl. Acad. Sci. U.S.A. 109, 309-314
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 309-314
    • Ravilious, G.E.1    Nguyen, A.2    Francois, J.A.3    Jez, J.M.4
  • 53
    • 84867547837 scopus 로고    scopus 로고
    • Redox switching of adenosine-5′-phosphosulfate kinase with photoactivatable atomic oxygen precursors
    • Zhang, M., Ravilious, G. E., Hicks, L. M., Jez, J. M., and McCulla, R. D. (2012) Redox switching of adenosine-5′-phosphosulfate kinase with photoactivatable atomic oxygen precursors. J. Am. Chem. Soc. 134, 16979-16982
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 16979-16982
    • Zhang, M.1    Ravilious, G.E.2    Hicks, L.M.3    Jez, J.M.4    McCulla, R.D.5
  • 54
    • 84865798179 scopus 로고    scopus 로고
    • Structural biology of plant sulfur metabolism: From assimilation to biosynthesis
    • Ravilious, G. E., and Jez, J. M. (2012) Structural biology of plant sulfur metabolism: from assimilation to biosynthesis. Nat. Prod. Rep. 29, 1138-1152
    • (2012) Nat. Prod. Rep. , vol.29 , pp. 1138-1152
    • Ravilious, G.E.1    Jez, J.M.2
  • 55
    • 84865772159 scopus 로고    scopus 로고
    • Nucleotide binding site communication in Arabidopsis thaliana adenosine 5′-phosphosulfate kinase
    • Ravilious, G. E., and Jez, J. M. (2012) Nucleotide binding site communication in Arabidopsis thaliana adenosine 5′-phosphosulfate kinase. J. Biol. Chem. 287, 30385-30394
    • (2012) J. Biol. Chem. , vol.287 , pp. 30385-30394
    • Ravilious, G.E.1    Jez, J.M.2
  • 56
    • 84874786114 scopus 로고    scopus 로고
    • Redox-linked gating of nucleotide binding by the N-terminal domain of adenosine 5′-phosphosulfate kinase
    • Ravilious, G. E., Westfall, C. S., and Jez, J. M. (2013) Redox-linked gating of nucleotide binding by the N-terminal domain of adenosine 5′-phosphosulfate kinase. J. Biol. Chem. 288, 6107-6115
    • (2013) J. Biol. Chem. , vol.288 , pp. 6107-6115
    • Ravilious, G.E.1    Westfall, C.S.2    Jez, J.M.3
  • 57
    • 21244491251 scopus 로고    scopus 로고
    • CeHMT-1, a putative phytochelatin transporter, is required for cadmium tolerance in Caenorhabditis elegans
    • Vatamaniuk, O. K., Bucher, E. A., Sundaram, M. V., and Rea, P. A. (2005) CeHMT-1, a putative phytochelatin transporter, is required for cadmium tolerance in Caenorhabditis elegans. J. Biol. Chem. 280, 23684-23690
    • (2005) J. Biol. Chem. , vol.280 , pp. 23684-23690
    • Vatamaniuk, O.K.1    Bucher, E.A.2    Sundaram, M.V.3    Rea, P.A.4
  • 58
    • 84859456947 scopus 로고    scopus 로고
    • Fission yeast HMT1 lowers seed cadmium through phytochelatin-dependent vacuolar sequestration in Arabidopsis
    • Huang, J., Zhang, Y., Peng, J. S., Zhong, C., Yi, H. Y., Ow, D. W., and Gong, J. M. (2012) Fission yeast HMT1 lowers seed cadmium through phytochelatin-dependent vacuolar sequestration in Arabidopsis. Plant Physiol. 158, 1779-1788
    • (2012) Plant Physiol. , vol.158 , pp. 1779-1788
    • Huang, J.1    Zhang, Y.2    Peng, J.S.3    Zhong, C.4    Yi, H.Y.5    Ow, D.W.6    Gong, J.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.