Characterization and primary structure of a second thioredoxin from the green alga, <i>Chlamydomonas reinhardtii</i>

Decottignies, Paulette; Schmitter, Jean‐Marie; Dutka, Sophie; Jacquot, Jean‐Pierre; Miginiac‐Maslow, Myroslawa

doi:10.1111/j.1432-1033.1991.tb16043.x

Cited by 45 publications

(32 citation statements)

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“…As an initial step, we recently reported an in-depth biochemical and genetic characterisation and a complete ('H, I3C, "N)-NMR frequency assignment of oxidised thioredoxin h (11.7 kDa and 122 amino acids) from the eukaryotic green alga Chlamydomonas reinhardtii (Decottignies et al, 1990(Decottignies et al, , 1991Huppe et al, 1991). We describe here a plant-thioredoxin-11-structure determination by means of NMR, and discuss it in terms of structural comparisons with known thioredoxins (Katti et al, 1990;Jeng et al, 1994;Qin et al, 1994Qin et al, .…”

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confidence: 99%

NMR Solution Structure of an Oxidised Thioredoxin h from the Eukaryotic Green Alga Chlamydomonas reinhardtii

Mittard

Blackledge

Stein

et al. 1997

European Journal of Biochemistry

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NMR solution structures of a cytosolic plant thioredoxin h (112 amino acids, 11.7 kDa) from the green alga Chlamydomonas reinhardtii have been calculated on the basis of 1904 NMR distance restraints, which include 90 distances used to restrain 45 hydrogen bonds, and 44 4 dihedral restraints. The structure of C. reinhardtii thioredoxin h was solved in its oxidised form, and the ensemble of 23 converged structures superpose to the geometric average structure with an atomic rmsd of 0.080 nm ? 0.016 for the (N, Ca, C) backbone atoms of residues 4 -110. Comparisons with other thioredoxins, such as thioredoxin from the bacterium Escherichia coli, thioredoxin 2 from a cyanobacterium of the Anahaena genus, and human thioredoxin, showed that thioredoxin h models share more structural features with human thioredoxin than with other bacterial thioredoxins. Examination of the accessible surface around the redoxactive peptide sequence indicates that a potent thioredoxin-h -substrate interaction could be similar to the vertebrate thioredoxin-substrate interactions.

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confidence: 99%

NMR Solution Structure of an Oxidised Thioredoxin h from the Eukaryotic Green Alga Chlamydomonas reinhardtii

Mittard

Blackledge

Stein

et al. 1997

European Journal of Biochemistry

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“…The sequences compared are those of Chromatium vinosum (13), Eschenchia coli (20), Corynebacterium nephnidii (27), Anabaena sp. strain 7199 (21), Bacillus subtllis (6), Streptomyces clavuligerus (this work), rats (43), humans (46), chickens (14), Saccharomyces cerevisiae (8), Aspergillus nidulans (19), and Chlamydomonas reinhardtii CH1 (7).…”

Section: Discussionmentioning

confidence: 99%

Thioredoxin-thioredoxin reductase system of Streptomyces clavuligerus: sequences, expression, and organization of the genes

et al. 1993

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The genes that encode thioredoxin and thioredoxin reductase of Streptomyces clavuligerus were cloned, and their DNA sequences were determined. Previously, we showed that S. clavuligerus possesses a disulfide reductase with broad substrate specificity that biochemically resembles the thioredoxin oxidoreductase system and may play a role in the biosynthesis of 13-lactam antibiotics. It consists of two components, a 70-kDa NADPH-dependent flavoprotein disulfide reductase with two identical subunits and a 12-kDa heat-stable protein general disulfide reductant. In this study, we found, by comparative analysis of their predicted amino acid sequences, that the 35-kDa protein is in fact thioredoxin reductase; it shares 48.7% amino acid sequence identity with Escherichia coil thioredoxin reductase, the 12-kDa protein is thioredoxin, and it shares 28 to 56% amino acid sequence identity with other thioredoxins. The streptomycete thioredoxin reductase has the identical cysteine redox-active region-Cys-Ala-Thr-Cys-and essentially the same flavin adenine dinucleotideand NADPH dinucleotide-binding sites as E. colt thioredoxin reductase and is partially able to accept E. coli thioredoxin as a substrate. The streptomycete thioredoxin has the same cysteine redox-active segment-TrpCys-Gly-Pro-Cys-that is present in virtually all eucaryotic and procaryotic thioredoxins. However, in vivo it is unable to donate electrons to E. colt methionine sulfoxide reductase and does not serve as a substrate in vitro for E. coli thioredoxin reductase. The S. clavuligerus thioredoxin (tixA) and thioredoxin reductase (trxB) genes are organized in a cluster. They are transcribed in the same direction and separated by 33 nucleotides. In contrast, the trx4 and txB genes of E. coli, the only other organism in which both genes have been characterized, are physically widely separated.In a recent article, we described the characterization of a broad-range disulfide reductase from Streptomyces clavuligerus, a producer of penicillin and cephalosporin antibiotics (2). This study was prompted by the finding that the activity of isopenicillin-N-synthase, a key enzyme in the biosynthesis of these 3-lactam compounds, and its tripeptide substrate 8-(L-a-aminoadipyl)-L-cysteinyl-D-valine (ACV) are dependent on the redox state of their cysteine amino acid residues (3, 32). Thus, in vitro conversion of ACV to isopenicillin N occurs only if both enzyme and substrate are in their reduced-thiol state. Isopenicillin-N-synthase reactions are therefore carried out in the presence of an excess of a thiol reagent such as dithiothreitol. We looked for and identified in S. clavuligerus an enzymatic system that replaces the need for dithiothreitol in isopenicillin-N-synthase reactions. That system efficiently reduces bis-ACV, the oxidized disulfide form of ACV, to its thiol state, and modulates the activity of isopenicillin-N-synthase (2). Because ACV structurally resembles glutathione, y-glutamyl-cysteinyl-glycine, the most common intracellular lowmolecular-weight thiol, we r...

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“…nidulans, using the dithiothreitol-dependent activation of chloroplastic NADP-MDH to monitor thc activity. Activation of NADP-MDH usually represents a valuable test ~ fast and sensitive ~ to screen for the presence of thioredoxins, since this enzyme has been reported to be easily activated by non-chloroplastic thioredoxins [20,31,53,541. Moreover, several proteins, first identified as thioredoxins and which were not able to activate NADP-MDH, were recently shown to be more related to glutaredoxins than to thioredoxins [54,551.…”

Section: Discusslonmentioning

confidence: 99%

“…Numbering is based on the E. coli sequence, the length of each sequence being indicated in parentheses. 6. coli [19]; Rhodospirillum rubrum [25]; Corynebacterium nephridii C1 [20]; Rhodobacter sphaeroides [24]; Chlamydomonas reinhardtii (Ch2) [30]; Anahaena from strain 7119 [26] [36]; human lymphocytes [37]; rat liver [39]; C. reinhardtii (Chl) [31]; Dictyostelium discoideum [28] (X, leucine residue could not be distinguished from isoleucine). Dots indicate residues exactly conserved across all the sequences.…”

Section: Discusslonmentioning

confidence: 99%

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Purification, properties and primary structure of thioredoxin from Aspergillus nidulans

Maréchal

Hoang

Schmitter

et al. 1992

European Journal of Biochemistry

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This paper reports the purification and the properties of a thioredoxin from the fungus Aspergillus nidulans. This thioredoxin is an acidic protein which exhibits an unusual fluorescence emission spectrum. characterized by a high contribution of tyrosine residues. Thioredoxin from A . nidulans cannot serve as a substrate for Escherichia coli thioredoxin reductase. Corn NADP-malate dehydrogenase is activated by this thioredoxin in the presence of dithiothreitol, while fructose-I ,6-bisphosphatase is not. The amino acid sequence of Aspergillus thioredoxin was determined by automated Edman degradation after cleavage with trypsin, SV, protease, chymotrypsin and cyanogen bromide. The masses of tryptic peptides were verified by plasma-desorption mass spectrometry. The mass of the protein was determined by electrospray mass spectrometry and shown to be in agreement with the calculated mass derived from the sequence ( M , = 11 564). Compared to thioredoxins from other sources, the protein from A . niduluns displays a maximal sequence similarity with that from yeast (45%).Thioredoxins are a group of small heat-stable proteins found in numerous organisms. They are structurally characterized by a redox active site exhibiting the well-conserved sequence -Trp-Cys-Gly-Pro-Cys- [I]. Thioredoxin was first identified in Escherichia coli where it can serve as a reducing agent for different reductases, involved in the reduction of ribonucleotide [2], sulfate [3] and methionine sulfoxide [4]. The oxidized form of thioredoxin is reduced by a specific NADPH-dependent reductase [5].In higher plants, thioredoxins are involved in the modulation ofenzymic activities by thiol redox control, during light: dark transitions [6]. Three different thioredoxins have been purified from spinach leaves and characterized; two, located in the chloroplast, regulate the activity of target enzymes such as NADP-malate dehydrogenase, (m-type thioredoxin) and fmctose-l,6-bisphosphatase (f-type thioredoxin) [7], by reducing disulfide bonds. These chloroplast thioredoxins are reduced by a specific ferredoxin-thioredoxin reductase [8]. The third thioredoxin, called thioredoxin h [9] was purified from other compartments of the cell (mitochondria, cytosol, endoplasmic reticulum) [lo]. It has been assigned a physiological function only in seeds, where it reduces cystine-rich proteins, such as purothionin, a-amylase and trypsin inhibitors [ll].

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Characterization and primary structure of a second thioredoxin from the green alga, Chlamydomonas reinhardtii

Cited by 45 publications

References 46 publications

NMR Solution Structure of an Oxidised Thioredoxin h from the Eukaryotic Green Alga Chlamydomonas reinhardtii

NMR Solution Structure of an Oxidised Thioredoxin h from the Eukaryotic Green Alga Chlamydomonas reinhardtii

Thioredoxin-thioredoxin reductase system of Streptomyces clavuligerus: sequences, expression, and organization of the genes

Purification, properties and primary structure of thioredoxin from Aspergillus nidulans

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