Structural and kinetic properties of adenylyl sulfate reductase from Catharanthus roseus cell cultures

Prior, A. F.; Uhrig, Joachim F.; Heins, Lisa; Wiesmann, Annette; Lillig, Christopher Horst; Stoltze, Corinna; Soll, Jürgen; Schwenn, Jens D.

doi:10.1016/s0167-4838(98)00266-0

Cited by 34 publications

(33 citation statements)

References 53 publications

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“…Indeed, a corresponding analysis of recombinant APS reductase from A. thaliana showed that this enzyme contained iron and had an absorption spectrum typical of enzymes with iron-sulfur clusters (44). Very recently a recombinant APS reductase from C. roseus was reported (25) to have no color and a V max more than 10 times lower than V max of the recombinant enzyme from L. minor. This finding can be explained by assuming that no iron-sulfur cluster was incorporated into the recombinant C. roseus APS reductase, resulting in decreased enzyme activity.…”

Section: Discussionmentioning

confidence: 99%

“…Products of APS Sulfotransferase-The product(s) of APS reductase were not determined but was presumed to be SO 3 2Ϫ (23)(24)(25). In contrast, GSSO 3 Ϫ (17) or GSSO 3 Ϫ together with SO 3…”

Section: Fig 4 Phylogenetic Tree Of Aps and Paps Reducing Enzymesmentioning

confidence: 99%

“…tain an N-terminal extension coding for a chloroplast targeting peptide and a C-terminal extension with homology to thioredoxin (21,22). Like APS sulfotransferases, APS reductases used DTE or GSH as a reductant (21,25).…”

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confidence: 99%

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Adenosine 5′-Phosphosulfate Sulfotransferase and Adenosine 5′-Phosphosulfate Reductase Are Identical Enzymes

Suter¹,

Ballmoos²,

Kopriva³

et al. 2000

Journal of Biological Chemistry

104

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Adenosine 5-phosphosulfate (APS) sulfotransferase and APS reductase have been described as key enzymes of assimilatory sulfate reduction of plants catalyzing the reduction of APS to bound and free sulfite, respectively. APS sulfotransferase was purified to homogeneity from Lemna minor and compared with APS reductase previously obtained by functional complementation of a mutant strain of Escherichia coli with an Arabidopsis thaliana cDNA library. APS sulfotransferase was a homodimer with a monomer M r of 43,000. Its amino acid sequence was 73% identical with APS reductase. APS sulfotransferase purified from Lemna as well as the recombinant enzyme were yellow proteins, indicating the presence of a cofactor. Like recombinant APS reductase, recombinant APS sulfotransferase used APS (K m ‫؍‬ 6.5 M) and not adenosine 3-phosphate 5-phosphosulfate as sulfonyl donor. The V max of recombinant Lemna APS sulfotransferase (40 mol min ؊1 mg protein ؊1 ) was about 10 times higher than the previously published V max of APS reductase. The product of APS sulfotransferase from APS and GSH was almost exclusively SO 3 2؊ . Bound sulfite in the form of S-sulfoglutathione was only appreciably formed when oxidized glutathione was added to the incubation mixture. Because SO 3 2؊ was the first reaction product of APS sulfotransferase, this enzyme should be renamed APS reductase.Higher plants and many microorganisms growing with sulfate as sulfur source reduce it to the level of sulfide for the synthesis of cysteine, methionine, coenzymes, and iron-sulfur clusters of enzymes (1-5). The reaction sequence from sulfate to sulfide is called assimilatory sulfate reduction as opposed to dissimilatory sulfate reduction, which occurs in certain anaerobic organisms such as Desulfovibrio and Desulfotomaculum, where sulfate functions as an electron acceptor during oxidation of organic substrates and where reduced forms of sulfur are excreted into the surroundings (3).The first step of assimilatory sulfate reduction is an activation of sulfate catalyzed by ATP sulfurylase (EC 2.7.7.4). The adenosine 5Ј-phosphosulfate (APS) 1 is the substrate for APS kinase (EC 2.7.1.2.5), which forms adenosine 3Ј-phosphate 5Ј-phosphosulfate (PAPS) in a second activation step (1-5). The subsequent reduction sequence starting from PAPS is well established in bacteria (4) and fungi (6), where a PAPS reductase (EC 1.8.99) reacts first with reduced thioredoxin then with PAPS to form SO 3 2Ϫ , oxidized thioredoxin, and adenosine 3Ј-phosphate 5Ј-phosphate (PAP) (4, 7, 8). The SO 3 2Ϫ is reduced to sulfide by sulfite reductase (EC 1.8.7.1). Sulfide is finally incorporated into O-acetyl-L-serine via O-acetyl-L-serine thiollyase (EC 4.2.99.8), thus forming cysteine (1-4). All these enzymes were detected in plants (1-5, 7-11), indicating that the identical reaction sequence is operative. In two early reports it was demonstrated, however, that plants and algae use APS rather than PAPS as sulfonyl donor for the first reduction step (12, 13). APS-dependent enzymes were partially p...

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Section: Discussionmentioning

confidence: 99%

Section: Fig 4 Phylogenetic Tree Of Aps and Paps Reducing Enzymesmentioning

confidence: 99%

See 1 more Smart Citation

Adenosine 5′-Phosphosulfate Sulfotransferase and Adenosine 5′-Phosphosulfate Reductase Are Identical Enzymes

Suter¹,

Ballmoos²,

Kopriva³

et al. 2000

Journal of Biological Chemistry

104

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“…Based on the number of secondary subunits and variations at the TRX catalytic motifs, 104 putative protein sequences with TRX domains have been identified in Arabidopsis, grouping into five families: the TRXs, glutaredoxins (GRXs), PDILs, peroxiredoxins (PRXs) and ferredoxins (FRXs). The plant PDILs further include PDIs, the QSOX-like proteins (QSOXLs; see QSOX above), and as well as the unique adenosine 5'-phosphosulfate reductase-like (APRL) group with an N-terminal chloroplast targeting peptide, an adenylyl sulphate reductase (APR) activity core and a C-terminal WCXXC (Prior et al 1999;Jacquot et al 2002;Houston et al 2005). Recent work (d'Aloisio et al 2010) has confirmed the complexity of plant PDILs, with 109 members identified from nine plant species (including wheat, rice and ), grouping into eight subfamilies: I (typical PDIs), II and III (both with two TRX domains, one each at the N-and C-terminus); IV and V (two TRX domains, at the N-terminus); and VI, VII, and VIII (each with a single TRX domain).…”

Section: Introductionmentioning

confidence: 99%

In silico identification and analysis of the protein disulphide isomerases in wheat and rice

Dorse

Bhave

2012

Biologia

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The protein disulphide isomerases (PDI) typically catalyse the formation and isomerization of disulphide bonds during the folding of nascent proteins. Some PDI isoforms may also have chaperone roles under house-keeping and/or stress conditions. Human PDIs and PDI-like (PDIL) proteins show a diverse array of catalytic and chaperone roles. However, understanding of the diversity and roles of plant PDILs is limited. This work aimed to identify the PDIL superfamilies in the two main cereals, rice and wheat, to identify candidates with potential roles in seed storage protein deposition and stress response processes. Searches of the rice genomic and wheat transcript assembly databases, with the Arabidopsis PDILs as queries, led to the identification of twenty two genomic loci in rice, encoding up to thirty two putative coding sequences, as well as twenty expressed sequence tags in wheat. The gene structures in rice ranged from 3 to 15 exons, the exon lengths ranging from 22 to 1,054 base pairs (bp) and the intron lengths from 74 to 1345 bp. The wheat TAs ranged from 584-2,444 bp and many sequences appeared to be orthologous to some of the rice loci. The putative proteins of both plants exhibited the characteristic thioredoxin active-site motif WCXXC, but significant diversity in the lengths of putative proteins and the composition or positions of functional domains therein. The PDILs thus fell into five major groups: PDIL1 (7 in rice; 4 in wheat); PDIL2 (9 rice; 4 wheat); PDIL5 (7 rice; 10 wheat); QSOXL (2 rice; 1 wheat); APRL (7 rice; 1 wheat). The analysis of the gene and putative protein sequences, the functional domains of the latter, and comparisons to literature have led to identification of a number of sequences with potential enzymatic and/or chaperone roles. Several of these appear to be candidates for key roles in seed storage protein folding, plant development and stress response processes in these important crops.

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“…Beyond stress perception and signaling processes, glutathione is involved in a wide range of different metabolic functions, ranging from detoxification of heavy metals (Cobbett and Goldsbrough, 2002) and conjugation of electrophilic xenobiotics (Marrs, 1996) to reductive processes, such as scavenging of reactive oxygen species (ROS; Noctor and Foyer, 1998). Furthermore, GSH is required as a cofactor for several other metabolic processes, including the detoxification of methylglyoxal, a cytotoxic compound that is formed as a byproduct of glycolysis under stress conditions (Zang et al, 2001;Singla-Pareek et al, 2003) and the reduction of adenosine 5#-phosphosulfate as the first reductive step of sulfate assimilation (Bick et al, 1998;Prior et al, 1999;Weber et al, 2000).…”

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confidence: 99%

Maturation of Arabidopsis Seeds Is Dependent on Glutathione Biosynthesis within the Embryo

et al. 2006

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Glutathione (GSH) has been implicated in maintaining the cell cycle within plant meristems and protecting proteins during seed dehydration. To assess the role of GSH during development of Arabidopsis (Arabidopsis thaliana [L.] Heynh.) embryos, we characterized T-DNA insertion mutants of GSH1, encoding the first enzyme of GSH biosynthesis, g-glutamyl-cysteine synthetase. These gsh1 mutants confer a recessive embryo-lethal phenotype, in contrast to the previously described GSH1 mutant, root meristemless 1(rml1), which is able to germinate, but is deficient in postembryonic root development. Homozygous mutant embryos show normal morphogenesis until the seed maturation stage. The only visible phenotype in comparison to wild type was progressive bleaching of the mutant embryos from the torpedo stage onward. Confocal imaging of GSH in isolated mutant and wild-type embryos after fluorescent labeling with monochlorobimane detected residual amounts of GSH in rml1 embryos. In contrast, gsh1 T-DNA insertion mutant embryos could not be labeled with monochlorobimane from the torpedo stage onward, indicating the absence of GSH. By using high-performance liquid chromatography, however, GSH was detected in extracts of mutant ovules and imaging of intact ovules revealed a high concentration of GSH in the funiculus, within the phloem unloading zone, and in the outer integument. The observation of high GSH in the funiculus is consistent with a high GSH1-promoter::b-glucuronidase reporter activity in this tissue. Development of mutant embryos could be partially rescued by exogenous GSH in vitro. These data show that at least a small amount of GSH synthesized autonomously within the developing embryo is essential for embryo development and proper seed maturation.

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Structural and kinetic properties of adenylyl sulfate reductase from Catharanthus roseus cell cultures

Cited by 34 publications

References 53 publications

Adenosine 5′-Phosphosulfate Sulfotransferase and Adenosine 5′-Phosphosulfate Reductase Are Identical Enzymes

Adenosine 5′-Phosphosulfate Sulfotransferase and Adenosine 5′-Phosphosulfate Reductase Are Identical Enzymes

In silico identification and analysis of the protein disulphide isomerases in wheat and rice

Maturation of Arabidopsis Seeds Is Dependent on Glutathione Biosynthesis within the Embryo

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