The glutathione S-transferase gene superfamily: an in silico approach to study the post translational regulation
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Alfenito MR, Souer E, Goodman CD, Buell R, Mol J, Koes R, Walbot V (1998) Functional complementation of anthocyanin sequestration in the vacuole by widely divergent glutathione S-transferases. Plant Cell 10:1135–1150
Allocati N, Federici L, Masulli M, Di Ilio C (2012) Distribution of glutathione transferases in Gram-positive bacteria and Archaea. Biochimie 94:588–596
Banerjee S, Goswami R (2010) GST profile expression study in some selected plants: in silico approach. Mol Cell Biochem 336:109–126
Basantani M, Srivastava A (2007) Plant glutathione transferases—A decade falls short. Can J Bot 85:443–456
Basantani M, Srivastava A, Sen S (2011) Elevated antioxidant response and induction of tau-class glutathione S-transferase after glyphosate treatment in Vigna radiata (L.) Wilczek. Pest Biochem Physiol 99:111–117
Bianchi MW, Roux C, Vartanian N (2002) Drought regulation of GST8, encoding the Arabidopsis homologue of ParC/Nt107 glutathione transferase/peroxidase. Physiol Plant 116:96–105
Chen D, Kawarasaki Y, Nakano H, Yamane T (2003) Cloning and in vitro and in vivo expression of plant glutathione S-transferase zeta class genes. J Bioscience Bioengineering 95:594–600
Coleman JOD, Blake-Kalff MMA, Davies TGE (1997) Detoxification of xenobiotics by plants: chemical modification and vacuolar compartmentation. Trends Plant Sci 2:144–151
Cotroneo PS, Russo MP, Ciuni M, Recupero GR, Lo Piero AR (2006) Quantitative real-time reverse transcriptase-PCR profiling of anthocyanin biosynthetic genes during orange fruit ripening. J Amer Soc Hort Sci 131:537–543
Crifò T, Puglisi I, Petrone G, Reforgiato Recupero G, Lo Piero AR (2011) Expression analysis in response to low temperature stress in blood oranges: implication of the flavonoid biosynthetic pathway. Gene 476:1–9
Crifò T, Petrone G, Lo Cicero L, Lo Piero AR (2012) Short cold storage enhances the anthocyanin contents and level of transcripts related to their biosynthesis in blood oranges. J Agric Food Chem 60:476–481
Cunningham SD, Berti WR, Huang JW (1995) Phytoremediation of contaminated soils. Trends Biotechnol 13:393–397
Daniel X, Sugano S, Tobin EM (2004) CK2 phosphorylation of CCA1 is necessary for its circadian oscillator function in Arabidopsis. Proc Natl Acad Sci USA 101:3292–3297
de la Fuente van Bentem S, Hirt H (2009) Protein tyrosine phosphorylation in plants: more abundant than expected? Trends Plant Sci 14:71–76
Dean JD, Goodwin PH, Hsiang T (2005) Induction of glutathione S-transferase genes of Nicotiana benthamiana following infection by Colletotrichum destructivum and C. orbiculare and involvement of one in resistance. J Exp Bot 56:1525–1533
Dixon DP, Cole DJ, Edwards R (2000) Characterisation of a zeta class glutathione transferase from Arabidopsis thaliana with a putative role in tyrosine catabolism. Arch Biochem Biophys 384:407–412
Dixon DP, Lapthorn A, Edwards R (2002) Plant glutathione transferases. Genome Biol 3:1–10
Dixon DP, Skipsey M, Edwards R (2010) Roles for glutathione transferases in plant secondary metabolism. Phytochem 71:338–350
Eapen S, Singh S, D’Souza SF (2007) Advances in the development of transgenic plants for remediation of xenobiotic pollutants. Biotechnol Adv 25:442–451
Edwards R, Dixon DP (2000) The role of glutathione transferases in herbicide metabolism. In: Cobb AH, Kirkwood RC (eds) Herbicides and their mechanisms of action. Sheffield Academic, Sheffield, pp 38–71
Ezaki B, Yamamoto Y, Matsumoto H (1995) Cloning and sequencing of the cDNAs induced by aluminium treatment and Pi starvation in cultured tobacco cells. Physiol Plantarum 93:11–18
Garnier J, Osguthorpe DJ, Robson B (1978) Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J Mol Biol 120:97–120
Geourjon C, Deleage G (1995) SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments. Comput Appl Biosci 11:681–684
Komatsu S, Hirano H (1993) Protein kinase activity and protein phosphorylation in rice (Oryza sativa L.) leaf. Plant Sci 94:127–137
Lo Piero AR, Puglisi I, Petrone G (2006) Gene isolation, analysis of expression, and in vitro synthesis of glutathione S-transferase from orange fruit [Citrus sinensis L. (Osbeck)]. J Agric Food Chem 54:9227–9233
Lo Piero AR, Mercurio V, Puglisi I, Petrone G (2009) Gene isolation and expression analysis of two distinct sweet orange [Citrus sinensis L. (Osbeck)] tau-type glutathione transferases. Gene 443:143–150
Lo Piero AR, Mercurio V, Puglisi I, Petrone G (2010) Different roles of functional residues in the hydrophobic binding site of two sweet orange tau glutathione S-transferases. FEBS J 277:255–262
Martin DDO, Vilas GL, Prescher JA, Rajaiah G, Falck JR, Bertozzi CR, Berthiaume LG (2008) Rapid detection, discovery, and identification of post-translationally myristoylated proteins during apoptosis using a bio-orthogonal azidomyristate analog. FASEB J 22:797–806
Mauch F, Dudler R (1993) Differential induction of distinct glutathione transferases of wheat by xenobiotics and by pathogen attack. Plant Physiol 102:1193–1201
McGoldrick S, O’Sullivan SM, Sheehan D (2005) Glutathione transferase-like proteins encoded in genomes of yeasts and fungi: insights into evolution of a multifunctional protein superfamily. FEMS Microbiol Lett 242:1–12
Moons A (2003) Osgstu3 and osgtu4, encoding tau class glutathione S-transferases, are heavy metal and hypoxic stress-induced and differentially salt stress-responsive in rice roots. FEBS Lett 553:427–432
Oakley A (2011) Glutathione transferases: a structural perspective. Drug Metab Rev 43:138–151
Pflugmacher S, Sandermann H, Schröder P (2000) Taxonomic distribution of plant glutathione S-transferases acting on xenobiotics. Phytochem 54:267–273
Qian N, Sejnowski TJ (1988) Predicting the secondary structure of globular proteins using neural network models. J Mol Biol 202:865–884
Rodriguez P, Mitton B, Kranias E (2005) Phosphorylation of Glutathione-S-transferase by protein kinase C-α implications for affinity-tag purification. Biotechnol Lett 27:1869–1873
Schröder P, Stampfl A (1999) Visualization of glutathione conjugation and induction of glutathione S-transferases in onion (Allium cepa L.) epidermal tissue. Z Naturforsch 54c:1033–1041
Schröder P, Wolf AE (1996) Characterization of glutathione S-transferase from needles of spruce trees from a forest decline stand. Tree Physiol 16:503–508
Stone JM, Walker JC (1995) Plant protein kinase families and signal transduction. Plant Physiol 108:451–457
Takahashi Y, Nagata T (1992a) parB: an auxin-regulated gene encoding glutathione S-transferase. Proc Natl Acad Sci USA 89:56–59
Takahashi Y, Nagata T (1992b) Differential expression of an auxin-regulated gene, parC, and a novel related gene, C-7, from tobacco mesophyll protoplasts in response to external stimuli and in plant tissues. Plant Cell Physiol 33:779–787
Takahashi Y, Kuroda H, Tanaka T, Machida Y, Takebe I, Nagata T (1989) Isolation of an auxin-regulated gene cDNA expressed during the transition from G0 to S phase in tobacco mesophyll protoplasts. Proc Natl Acad Sci USA 86:9279–9283
Takahashi Y, Shomura A, Sasaki T, Yano M (2001) Hd6, a rice quantitative trait locus involved in photoperiod sensitivity, encodes the α subunit of protein kinase CK2. Proc Natl Acad Sci USA 98:7922–7927
Traverso JA, Meinnel T, Giglione C (2008) Expanded impact of protein N-myristoylation in plants. Plant Signal Behav 3:501–502
Vollenweider S, Weber H, Stolz S, Chetelat A, Farmer EE (2000) Fatty acid ketodienes and fatty acid ketotrienes: michael addition acceptors that accumulate in wounded and diseased Arabidopsis leaves. Plant J 24:467–476
Zaal EJ, Droog FNJ, Boot CJM, Hensgens LAM, Hoge JHC, Schilperoort RA, Libbenga KR (1991) Promoters of auxin-induced genes from tobacco can lead to auxin-inducible and root tip-specific expression. Plant Mol Biol 16:983–998