Seed thioredoxin h

2016 ◽  
Vol 1864 (8) ◽  
pp. 974-982 ◽  
Author(s):  
Per Hägglund ◽  
Christine Finnie ◽  
Hiroyuki Yano ◽  
Azar Shahpiri ◽  
Bob B. Buchanan ◽  
...  
Keyword(s):  
Thioredoxin H

scholarly journals Arabidopsis Disulfide Reductase, Trx-h2, Functions as an RNA Chaperone under Cold Stress

2021 ◽  
Vol 11 (15) ◽  
pp. 6865
Author(s):  
Eun Seon Lee ◽  
Joung Hun Park ◽  
Seong Dong Wi ◽  
Ho Byoung Chae ◽  
Seol Ki Paeng ◽  
...  
Keyword(s):  
Cold Stress ◽  
Wild Type ◽  
Rna Chaperone ◽  
E Coli ◽  
Cold Sensitive ◽  
Thioredoxin H ◽  
Functional Rnas

The thioredoxin-h (Trx-h) family of Arabidopsis thaliana comprises cytosolic disulfide reductases. However, the physiological function of Trx-h2, which contains an additional 19 amino acids at its N-terminus, remains unclear. In this study, we investigated the molecular function of Trx-h2 both in vitro and in vivo and found that Arabidopsis Trx-h2 overexpression (Trx-h2OE) lines showed significantly longer roots than wild-type plants under cold stress. Therefore, we further investigated the role of Trx-h2 under cold stress. Our results revealed that Trx-h2 functions as an RNA chaperone by melting misfolded and non-functional RNAs, and by facilitating their correct folding into active forms with native conformation. We showed that Trx-h2 binds to and efficiently melts nucleic acids (ssDNA, dsDNA, and RNA), and facilitates the export of mRNAs from the nucleus to the cytoplasm under cold stress. Moreover, overexpression of Trx-h2 increased the survival rate of the cold-sensitive E. coli BX04 cells under low temperature. Thus, our data show that Trx-h2 performs function as an RNA chaperone under cold stress, thus increasing plant cold tolerance.

Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism

2001 ◽  
Vol 359 (1) ◽  
pp. 65-75 ◽  
Author(s):  
Valeria MENCHISE ◽  
Catherine CORBIER ◽  
Claude DIDIERJEAN ◽  
Michele SAVIANO ◽  
Ettore BENEDETTI ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Proton Transfer ◽  
Chlamydomonas Reinhardtii ◽  
Catalytic Mechanism ◽  
Structural Data ◽  
Careful Analysis ◽  
Wild Type ◽  
Thioredoxin H ◽  
Dynamics Simulations

Thioredoxins are ubiquitous proteins which catalyse the reduction of disulphide bridges on target proteins. The catalytic mechanism proceeds via a mixed disulphide intermediate whose breakdown should be enhanced by the involvement of a conserved buried residue, Asp-30, as a base catalyst towards residue Cys-39. We report here the crystal structure of wild-type and D30A mutant thioredoxin h from Chlamydomonas reinhardtii, which constitutes the first crystal structure of a cytosolic thioredoxin isolated from a eukaryotic plant organism. The role of residue Asp-30 in catalysis has been revisited since the distance between the carboxylate OD1 of Asp-30 and the sulphur SG of Cys-39 is too great to support the hypothesis of direct proton transfer. A careful analysis of all available crystal structures reveals that the relative positioning of residues Asp-30 and Cys-39 as well as hydrophobic contacts in the vicinity of residue Asp-30 do not allow a conformational change sufficient to bring the two residues close enough for a direct proton transfer. This suggests that protonation/deprotonation of Cys-39 should be mediated by a water molecule. Molecular-dynamics simulations, carried out either in vacuo or in water, as well as proton-inventory experiments, support this hypothesis. The results are discussed with respect to biochemical and structural data.

Evidence for a subgroup of thioredoxin h that requires GSH/Grx for its reduction

FEBS Letters ◽  
2003 ◽  
Vol 555 (3) ◽  
pp. 443-448 ◽  
Author(s):  
Eric Gelhaye ◽  
Nicolas Rouhier ◽  
Jean-Pierre Jacquot
Keyword(s):  
Thioredoxin H

Structural Studies on Wheat Thioredoxin h

1998 ◽  
pp. 52-57
Author(s):  
F. de Lamotte-Guery ◽  
C. Pruvost ◽  
V. Lullien-Pellerin ◽  
M.-F. Gautier ◽  
P. Joudrier ◽  
...  
Keyword(s):  
Structural Studies ◽  
Thioredoxin H

Identification and characterization of a third thioredoxin h in poplar

2003 ◽  
Vol 41 (6-7) ◽  
pp. 629-635 ◽  
Author(s):  
Eric Gelhaye ◽  
Nicolas Rouhier ◽  
Alexios Vlamis-Gardikas ◽  
Jean-Michel Girardet ◽  
Pierre-Eric Sautière ◽  
...  
Keyword(s):  
Thioredoxin H ◽  
Identification And Characterization

Characterization of wheat thioredoxin h cDNA and production of an active Triticum aestivum protein in Escherichia coli

1998 ◽  
Vol 252 (2) ◽  
pp. 314-324 ◽  
Author(s):  
Marie-Francoise Gautier ◽  
Valerie Lullien-Pellerin ◽  
Frederic de Lamotte-Guery ◽  
Anne Guirao ◽  
Philippe Joudrier
Keyword(s):  
Escherichia Coli ◽  
Triticum Aestivum ◽  
Thioredoxin H

Rice phloem thioredoxin h has the capacity to mediate its own cell-to-cell transport through plasmodesmata

Planta ◽  
1998 ◽  
Vol 205 (1) ◽  
pp. 12-22 ◽  
Author(s):  
Yutaka Ishiwatari ◽  
Toru Fujiwara ◽  
K. C. McFarland ◽  
Keisuke Nemoto ◽  
Hiroaki Hayashi ◽  
...  
Keyword(s):  
Cell Transport ◽  
Thioredoxin H

Oil body mobilization in sunflower seedlings is potentially regulated by thioredoxin h

2012 ◽  
Vol 57 ◽  
pp. 134-142 ◽  
Author(s):  
Nahid Babazadeh ◽  
Maral Poursaadat ◽  
Hamid Reza Sadeghipour ◽  
Abasalt Hossein Zadeh Colagar
Keyword(s):  
Oil Body ◽  
Thioredoxin H
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