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Eukaryotic Cell, December 2007, p. 2323-2331, Vol. 6, No. 12
1535-9778/07/$08.00+0 doi:10.1128/EC.00083-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.
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and
Philippe Silar1,2
Institut de Génétique et Microbiologie, UMR CNRS-Université de Paris 11, UPS Bât. 400, 91405 Orsay Cedex, France,1 UFR de Biochimie, Université de Paris 7-Denis Diderot, Case 7006, 2 Place Jussieu, 75005 Paris, France2
Received 15 March 2007/ Accepted 24 September 2007
In various organisms, thioredoxins are known to be involved in the reduction of protein disulfide bonds and in protecting the cell from oxidative stress. Genes encoding thioredoxins were found by searching the complete genome sequence of the filamentous ascomycete Podospora anserina. Among them, PaTrx1, PaTrx2, and PaTrx3 are predicted to be canonical cytosolic proteins without additional domains. Targeted disruption of PaTrx1, PaTrx2, and PaTrx3 shows that PaTrx1 is the major thioredoxin involved in sulfur metabolism. Deletions have no effect on peroxide resistance; however, data show that either PaTrx1 or PaTrx3 is necessary for sexual reproduction and for the development of the crippled growth cell degeneration (CG), processes that also required the PaMpk1 mitogen-activated protein kinase (MAPK) pathway. Since PaTrx1 PaTrx3 mutants show not an enhancement but rather an impairment in CG, it seems unlikely that PaTrx1 and PaTrx3 thioredoxins participate in the inhibition of this MAPK pathway. Altogether, these results underscore a role for thioredoxins in fungal development.
Published ahead of print on 12 October 2007.
Supplemental material for this article may be found at http://ec.asm.org/.
Present address: Institut Curie, 26 Rue d'Ulm, 75248 Paris Cedex 05, France.
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