Cloning and sequence analysis of a cDNA encoding rice glutaredoxin

Minakuchi, Kazunobu; Yabushita, Tetsushige; Masumura, Takehiro; Ichihara, Kazuo; Tanaka, Kunisuke

doi:10.1016/0014-5793(94)80264-5

Cited by 63 publications

(34 citation statements)

References 22 publications

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“…X77150). The probe for sodCc1 was prepared as described previously primers based on the sequence of the full length cDNA of rice thioredoxin (Ishiwatari et al, 1995), and the grx probe was prepared by restriction digestion of the cDNA clone (Minakuchi et al, 1994). The blots were stripped and subsequently hybridized with rice actin cDNA (accession no.…”

Section: Northern-blot Analysismentioning

confidence: 99%

A Novel cis-Element That Is Responsive to Oxidative Stress Regulates Three Antioxidant Defense Genes in Rice

et al. 2005

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All organisms have defense systems against oxidative stress that include multiple genes of antioxidant defense. These genes are induced by reactive oxygen species under condition of oxidative stress. In this study, we found that a 28-bp motif is conserved on the promoter regions of three antioxidant defense genes in rice (Oryza sativa): cytosolic superoxide dismutase (sodCc1), cytosolic thioredoxin (trxh), and glutaredoxin (grx). We demonstrated that the 28-bp sequence acts as a cis-element responsive to oxidative stress by transient expression assay and designated it as CORE (coordinate regulatory element for antioxidant defense). The CORE was activated by methyl viologen treatment and induced a 3.1-fold increase in expression of the reporter gene, but it did not respond to hydrogen peroxide. The expressions of the sodCc1, trxh, and grx genes were coordinately induced by methyl viologen, suggesting that multiple genes involved in antioxidant defense are controlled by a common regulatory mechanism via CORE. Application of the mitogen-activated protein kinase kinase inhibitor caused the constitutive induction of the sodCc1, trxh, and grx genes and the activation of CORE without methyl viologen treatment. These results indicate that a mitogen-activated protein kinase cascade is involved in the gene regulation mediated by CORE.

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Section: Northern-blot Analysismentioning

confidence: 99%

A Novel cis-Element That Is Responsive to Oxidative Stress Regulates Three Antioxidant Defense Genes in Rice

et al. 2005

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“…For collection of NOE upper distance constraints, 3D 13 C-edited (Muhandiram et al, 1993) and 15 N-edited NOESY (Zhang et al, 1994) spectra were recorded with a 60 ms mixing time on the 1.8 mM 13 C/ 15 N-labeled sample in 95% H 2 O/ 2 H 2 O. Two separate 13 C-edited NOESY spectra were recorded with the 13 C carrier positioned at 43 ppm for aliphatic carbon atoms and at 132.3 ppm for the aromatic carbon atoms.…”

Section: Nmr Spectroscopymentioning

confidence: 99%

“…Glutaredoxins have now been identi®ed in numerous species including Escherichia coli, bacteriophage T4, vaccinia virus, yeast, rabbit, pig, and human (Ahn & Moss, 1992;Gan & Wells, 1987a;Gan et al, 1990;Ho È o È g et al, 1983;Hopper et al, 1989;Johnson et al, 1991;Klintrot et al, 1984;Minakuchi et al, 1994;Padilla et al, 1995). This important family of protein disul®de reductants has been shown to play numerous important roles in the cell.…”

Section: Introductionmentioning

confidence: 99%

The NMR solution structure of human glutaredoxin in the fully reduced form

Sun

Berardi

Bushweller

1998

Journal of Molecular Biology

100

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The determination of the nuclear magnetic resonance (NMR) solution structure of fully reduced human glutaredoxin is described. A total of 1159 useful nuclear Overhauser effect (NOE) upper distance constraints and 187 dihedral angle constraints were obtained as the input for the structure calculations for which the torsion angle dynamics program DYANA has been utilized followed by energy minimization in water with the AMBER force ®eld as implemented in the program OPAL. The resulting 20 conformers have an average root-mean-square deviation value relative to the mean coordinates of 0.54 A Ê for all the backbone atoms N, C a and C H , and of 1.01 A Ê for all heavy atoms. Human glutaredoxin consists of a four-stranded mixed b-sheet composed of residues 15 to 19, 43 to 47, 72 to 75 and 78 to 81, and ®ve a-helices composed of residues 4 to 9, 24 to 34, 54 to 65, 83 to 91, and 94 to 100. Comparisons with the structures of Escherichia coli glutaredoxin-1, pig liver glutaredoxin and human thioredoxin were made. Electrostatic calculations on the human glutaredoxin structure and that of related proteins provide an understanding of the variation of pK a values for the nucleophilic cysteine in the active site observed among these proteins. In addition, the high-resolution NMR solution structure of human glutaredoxin has been used to model the binding site for glutathione and for ribonucleotide reductase B1 by molecular dynamics simulations.

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“…Indeed the active site sequences differ from the one of thioredoxin (CPYC for glutaredoxin, CPHC for DsbA), but the same relative role of the cysteines apply for these proteins (Grauschopf e;. Glutaredoxins have indeed been found in plant cells (Minakuchi et al, 1994). So far, in contrast to the extreme diversity of thioredoxins in plants, there is however evidence for the existence of only two glutaredoxin isoforms in A. thaliana and no report of chloroplastic glutaredoxins, whilst three variants coexist in E. coli (Aslund et al, 1994).…”

Section: Thioredoxin Active Site and Thioredoxin Related Proteins In mentioning

confidence: 99%

Thioredoxins: structure and function in plant cells

1997

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SUMMARY Thioredoxins are ubiquitous small‐molecular‐weight proteins (typically 100–120 amino‐acid residues) containing an extremely reactive disulphide bridge with a highly conserved sequence ‐Cys‐Gly(Ala/Pro)‐Pro‐Cys‐. In bacteria and animal cells, thioredoxins participate in multiple reactions which require reduction of disulphide bonds on selected target proteins/ enzymes. There is now ample biochemical evidence that thioredoxins exert very specific functions in plants, the best documented being the redox regulation of chloroplast enzymes. Another area in which thioredoxins are believed to play a prominent role is in reserve protein mobilization during the process of germination. It has been discovered that thioredoxins constitute a large multigene family in plants with different‐subcellular localizations, a unique feature in living cells so far. Evolutionary studies based on these molecules will be discussed, as well as the available biochemical and genetic evidence related to their functions in plant cells. Eukaryotic photosynthetic plant cells are also unique in that they possess two different reducing systems, one extrachloroplastic dependent on NADPH as an electron donor, and the other one chloroplastic, dependent on photoreduced ferredoxin. This review will examine in detail the latest progresses in the area of thioredoxin structural biology in plants, this protein being an excellent model for this purpose. The structural features of the reducing enzymes ferredoxin thioredoxin reductase and NADPH thioredoxin reductase will also be described. The properties of the target enzymes known so far in plants will be detailed with special emphasis on the structural features which make them redox regulatory. Based on sequence analysis, evidence will be presented that redox regulation of enzymes of the biosynthetic pathways first appeared in cyanobacteria possibly as a way to cope with the oxidants produced by oxygenic photosynthesis. It became more elaborate in the chloroplasts of higher plants where a co‐ordinated functioning of the chloroplastic and extra chloroplastic metabolisms is required.

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Cloning and sequence analysis of a cDNA encoding rice glutaredoxin

Cited by 63 publications

References 22 publications

A Novel cis-Element That Is Responsive to Oxidative Stress Regulates Three Antioxidant Defense Genes in Rice

A Novel cis-Element That Is Responsive to Oxidative Stress Regulates Three Antioxidant Defense Genes in Rice

The NMR solution structure of human glutaredoxin in the fully reduced form

Thioredoxins: structure and function in plant cells

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