Purification and characterization of glutathione S-transferase from sugarcane leaves

Singhal, Sharad S.; Tiwari, Narendra K.; Ahmad, Hassan; Srivastava, Satish K.; Awasthi, Yogesh C.

doi:10.1016/0031-9422(91)84175-r

Cited by 17 publications

(7 citation statements)

References 29 publications

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“…The result showed that FIP1 can use GSH and 1-chloro-2,4-dinitrobenzene (CDNB) as substrates with K m 5 0.467 mM and 1.794 mM, respectively (Fig. 3, B and C), which is similar to the value reported in the literature (Singhal et al, 1991;Prapanthadara et al, 1996). Thus, FIP1 interacting with FIN219 does have GST activity.…”

Section: Isolation Of Fin219-interacting Partners By the Yeast Two-hysupporting

confidence: 80%

GlutathioneS-Transferase Interacting with Far-Red Insensitive 219 Is Involved in Phytochrome A-Mediated Signaling in Arabidopsis

et al. 2007

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Far-red (FR) insensitive 219 (FIN219) was previously shown to be involved in phytochrome A-mediated FR light signaling. To further understand its function and regulatory relation with other light-signaling components, a yeast two-hybrid approach was used to isolate FIN219-interacting partners. Here, we demonstrate that FIN219-interacting protein 1 (FIP1) interacts with FIN219 in vitro and in vivo and is composed of 217 amino acids that belong to the tau class of the large glutathione S-transferase gene family. FIP1 was further shown to have glutathione S-transferase activity. The gain of function and partial loss of function of FIP1 resulted in a hyposensitive hypocotyl phenotype under continuous FR (cFR) light and a delayed flowering phenotype under long-day conditions, which suggests that FIP1 may exist in a complex to function in the regulation of Arabidopsis (Arabidopsis thaliana) development. In addition, FIP1 mRNA was down-regulated in the suppressor of phytochrome A-105 1 mutant and differentially expressed in constitutive photomorphogenic 1-4 (cop1-4) and cop1-5 mutants under cFR. Intriguingly, FIP1 expression was up-regulated in the fin219 mutant under all light conditions, except cFR. Furthermore, promoter activity assays revealed that FIP1 expression was light dependent, mainly associated with vascular tissues, and developmentally regulated. Subcellular localization studies revealed that the b-glucuronidase-FIP1 fusion protein was localized in the nucleus and cytoplasm. Taken together, these data indicate that FIP1 may interact with FIN219 to regulate cell elongation and flowering in response to light.Light has a profound effect on plant growth and development. It not only provides an energy source for plant photosynthesis, but also acts as an important signal to regulate gene expression and various aspects of plant development (Kendrick and Kronenberg, 1994). Plants are equipped with different photoreceptors to sense changes in light. At least four different photoreceptor classes are found in Arabidopsis (Arabidopsis thaliana): phytochromes for red (R) and far-red (FR) light, cryptochromes and phototropins for blue (B) and UV-A light, and an unknown photoreceptor for UV-B light. Phytochromes are the most extensively studied among these photoreceptors and exist in phytochrome R-absorbing (Pr) and phytochrome FR-absorbing (Pfr) forms.Research into light signal transduction by molecular genetics, cell biology, and DNA microarray approaches has made great progress (Tepperman et al

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Section: Isolation Of Fin219-interacting Partners By the Yeast Two-hysupporting

confidence: 80%

GlutathioneS-Transferase Interacting with Far-Red Insensitive 219 Is Involved in Phytochrome A-Mediated Signaling in Arabidopsis

et al. 2007

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“…In all previous determinations of kinetic parameters for purified plant GSTs, initial-velocity data have been analyzed using the standard Michaelis-Menton equation for a unireaction (O'Connell et al, 1988;Williamson and Beverley, 1988;Singhal et al, 1991;Irzyk and Fuerst, 1993;Droog et al, 1995;Flury et al, 1995). However, kinetic models describing bireactant mechanisms are better suited for the determination of kinetic constants for GSTs, which utilize two substrates.…”

Section: Discussionmentioning

confidence: 99%

“…Acceptable and less acceptable amino acid substitutions are defined by the GCG software. Sequences from sorghum were compared with GSTs from sugarcane (Singhal et al, 1991), maize GST I, (Shah et al, 1986), maize GST III (Grove et al, 1988), maize GST IV (GST II, new nomenclature; Jepson et al, 1994;Dixon et al, 1997), wheat GST A1 (Dudler et al, 1991), Hyoscyamus muticus (Bilang et al, 1993), Arabidopsis pm239 (Bartling et al, 1993), tobacco parB (Takahashi and Nagata, 1992), Arabidopsis pm24 (Zhou and Goldsbrough, 1993), Silene cucubalus (Kutchan and Hochberger, 1992), and Arabidopsis ERD11 (Kiyosue et al, 1993).…”

Section: Discussionmentioning

confidence: 99%

Isolation and Characterization of GlutathioneS-Transferase Isozymes from Sorghum1

1998

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Two glutathione S-transferase (GST) isozymes, A1/A1 and B1/B2, were purified from etiolated, O-1,3-dioxolan-2-yl-methyl-2,2,2,-trifluoro-4 -chloroacetophenone-oxime-treated sorghum (Sorghum bicolor L. Moench) shoots. GST A1/A1, a constitutively expressed homodimer, had a subunit molecular mass of 26 kD and an isoelectric point of 4.9. GST A1/A1 exhibited high activity with 1-chloro-2, 4,dinitrobenzene (CDNB) but low activity with the chloroacetanilide herbicide metolachlor. For GST A1/A1, the random, rapidequilibrium bireactant kinetic model provided a good description of the kinetic data for the substrates CDNB and glutathione (GSH). GST B1/B2 was a heterodimer with subunit molecular masses of 26 kD (designated the B1 subunit) and 28 kD (designated the B2 subunit) and a native isoelectric point of 4.8. GST B1/B2 exhibited low activity with CDNB and high activity with metolachlor as the substrate. The kinetics of GST B1/B2 activity with GSH and metolachlor fit a model describing a multisite enzyme having two binding sites with different affinities for these substrates. Both GST A1/A1 and GST B1/B2 exhibited GSH-conjugating activity with ethacrynic acid and GSH peroxidase activity with cumene hydroperoxide, 9-hydroperoxy-trans-10,cis-12-octadecadienoic acid and 13-hydroperoxy-cis-9,trans-11-octadecadienoic acid. Both GST A1/A1 and GST B1/B2 are glycoproteins, as indicated by their binding of concanavalin A. Polyclonal antibodies raised against GST A1/A1 exhibited cross-reactivity with the B1 subunit of GST B1/B2. Comparisons of the N-terminal amino acid sequences of the GST A1, B1, and B2 subunits with other type I -GSTs indicated a high degree of homology with the maize GST I subunit and a sugarcane GST.GSTs (EC 2.5.1.18) are dimeric enzymes found in mammals, insects, plants, and microbes that catalyze nucleophilic attack by the thiolate anion of GSH at electrophilic centers of hydrophobic molecules (Mannervik and Danielson, 1988). In addition to catalyzing GSH conjugation, GSTs also exhibit GSH peroxidase activity and ligandbinding functions (Mannervik and Danielson, 1988;Marrs, 1996). Mammalian GSTs compose a multigene family; in rat liver at least 13 different cytosolic GST subunits are found as either heterodimers or homodimers . Mammalian cytosolic GSTs have been divided into four classes (␣, , , and ) based on immunological, biochemical, and sequence similarities (Buetler and Eaton, 1992). It is well established that mammalian GSTs play an important role in the detoxification of electrophilic xenobiotics (Mannervik and Danielson, 1988). Although endogenous substrates for mammalian GSTs have not been clearly defined, there is evidence that ␣-GSTs protect against oxidative stress by detoxifying reactive products generated by lipid peroxidation (Ålin et al., 1985;Ketterer and Coles, 1991;Singhal et al., 1992).In general, plant GSTs have not been as well characterized as mammalian GSTs. Plant cytosolic GSTs belong to the archaic class of GSTs (Meyer et al., 1991;Marrs, 1996). This class, which is very heterog...

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“…As with the multiple GSTs found in animal species, plant GSTs may be constitutively expressed and induced by external stimuli. Constitutive GSTs have been identified in several plant species including maize (GST III) [22,23], sugarcane [29] and Silene cucubalus [ 16]. In addition to these constitutively expressed isoforms, differential screening techniques have been used to isolate a number of inducible cDNA clones, which share significant homology with known GSTs.…”

Section: Introductionmentioning

confidence: 99%

Cloning and characterization of maize herbicide safener-induced cDNAs encoding subunits of glutathione S-transferase isoforms I, II and IV

Jepson¹,

Lay²,

Holt³

et al. 1994

Plant Mol Biol

132

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Several GSTs have been characterised in maize. GST I is a homodimer of 29 kDa subunits, GST II a hetrodimer of 27 kDa and 29 kDa subunits and GST IV a homodimer of 27 kDa subunits. We report the isolation and characterization of a herbicide-safener inducible cDNA clone, GST-27. Based on partial amino acid sequence, GST-27 encodes the 27 kDa subunit present in both glutathione S-transferase isoforms GST II and IV. Northern blotting was used to compare the expression patterns of GST-27 with that of GST-29. Transcripts corresponding to GST-27 were found to be constitutively expressed in RNA isolated from the root, but no expression was detected in RNA isolated from aerial parts of the plant. The application of herbicide safener caused a dramatic increase in the expression of GST-27 in all aerial plant parts tested. GST-29 was found to be constitutively expressed in RNA isolated from a number of maize tissues. The basal level of GST-29 expression showed a minimal increase upon herbicide safener treatment. Although a range of hormonal, environmental and physiological stimuli failed to elevate GST-27 levels, some increase in GST-27 mRNA was observed in the late stages of leaf senescence and after treatments resulting in phytotoxic effects.

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Purification and characterization of glutathione S-transferase from sugarcane leaves

Cited by 17 publications

References 29 publications

GlutathioneS-Transferase Interacting with Far-Red Insensitive 219 Is Involved in Phytochrome A-Mediated Signaling in Arabidopsis

GlutathioneS-Transferase Interacting with Far-Red Insensitive 219 Is Involved in Phytochrome A-Mediated Signaling in Arabidopsis

Isolation and Characterization of GlutathioneS-Transferase Isozymes from Sorghum1

Cloning and characterization of maize herbicide safener-induced cDNAs encoding subunits of glutathione S-transferase isoforms I, II and IV

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