| dc.creator |
Traverso, José A. |
|
| dc.creator |
Vignols, Florence |
|
| dc.creator |
Cazalis, Roland |
|
| dc.creator |
Pulido, Amada |
|
| dc.creator |
Sahrawy, Mariam |
|
| dc.creator |
Cejudo, Francisco Javier |
|
| dc.creator |
Meyer, Yves |
|
| dc.creator |
Chueca, Ana |
|
| dc.date |
2008-04-10T09:54:26Z |
|
| dc.date |
2008-04-10T09:54:26Z |
|
| dc.date |
2007-01 |
|
| dc.date.accessioned |
2017-01-31T01:01:47Z |
|
| dc.date.available |
2017-01-31T01:01:47Z |
|
| dc.identifier |
Plant Physiology 143(1): 300–311 (2007) |
|
| dc.identifier |
1532-2548 |
|
| dc.identifier |
http://hdl.handle.net/10261/3509 |
|
| dc.identifier |
10.1104/pp.106.089524 |
|
| dc.identifier.uri |
http://dspace.mediu.edu.my:8181/xmlui/handle/10261/3509 |
|
| dc.description |
12 páginas. |
|
| dc.description |
Thioredoxins (TRXs) are small ubiquitous oxidoreductases involved in disulfide bond reduction of a large panel of target
proteins. The most complex cluster in the family of plant TRXs is formed by h-type TRXs. In Arabidopsis (Arabidopsis thaliana),
nine members of this subgroup were described, which are less well known than their plastidial counterparts. The functional
study of type-h TRXs is difficult because of the high number of isoforms and their similar biochemical characteristics, thus
raising the question whether they have specific or redundant functions. Type-h TRXs are involved in seed germination and self
incompatibility in pollen-pistil interaction. Their function as antioxidants has recently been proposed, but further work is
needed to clarify this function in plants. In this study, we describe two new h-type TRXs from pea (Pisum sativum; stated
PsTRXh1 and PsTRXh2). By functional complementation of a yeast (Saccharomyces cerevisiae) trx1D trx2D double mutant, we
demonstrate that PsTRXh1 is involved in the redox-imbalance control, possibly through its interaction with peroxiredoxins. In
contrast, PsTRXh2 provokes a phenotype of hypersensitivity to hydrogen peroxide in the yeast mutant. Furthermore, we show
differential gene expression and protein accumulation of the two isoforms, PsTRXh1 protein being abundantly detected in
vascular tissue and flowers, whereas PsTRXh2 gene expression was hardly detectable. By comparison with previous data of
additional PsTRXh isoforms, our results indicate specific functions for the pea h-type TRXs so far described. |
|
| dc.description |
This work was supported by the Dirección General de Investigación Científica y Te´cnica, Spain (grant nos. PB98–0474 and
BF12002–00401), by the Junta de Andalucía, Spain (grant no. CVI
154), by CSIC (Acción Integrada grant no. HF2001–0136), and by the
Spanish government (fellowship FPI98 to J.A.T.). |
|
| dc.description |
Peer reviewed |
|
| dc.format |
936617 bytes |
|
| dc.format |
application/pdf |
|
| dc.language |
eng |
|
| dc.publisher |
American Society of Plant Physiologists |
|
| dc.relation |
http://dx.doi.org/10.1104/pp.106.089524 |
|
| dc.rights |
closedAccess |
|
| dc.title |
PsTRXh1 and PsTRXh2 Are Both Pea h-Type Thioredoxins with Antagonistic Behavior in Redox Imbalances |
|
| dc.type |
Artículo |
|