Abstract：
:In fission yeast, the transcription factor Pap1 undergoes H2O2-dependent oxidation that promotes its nuclear accumulation and the activation of an antioxidant gene program. However, the mechanisms that regulate the sensitivity and selectivity of Pap1 activation by peroxides are not fully understood. Here, we demonstrate that the peroxiredoxin Tpx1, the sensor of this signaling cascade, activates the otherwise unresponsive Pap1 protein once the main cytosolic reduced thioredoxin, Trx1, becomes transiently depleted. In other words, Pap1 works as an alternative electron donor for oxidized Tpx1. We have trapped the very transient Tpx1-Pap1 intermediate in cells depleted in Trx1, as we show here using mass spectrometry. Recycling of Tpx1 by Trx1 is required for the efficient signaling to Pap1, suggesting that the complete cycle of H2O2 scavenging by Tpx1 and further recycling of oxidized Tpx1 by Trx1 is required for full downstream activation of the redox cascade.
journal_name
Cell Repjournal_title
Cell reportsauthors
Calvo IA,Boronat S,Domènech A,García-Santamarina S,Ayté J,Hidalgo Edoi
10.1016/j.celrep.2013.11.027subject
Has Abstractpub_date
2013-12-12 00:00:00pages
1413-24issue
5issn
2211-1247pii
S2211-1247(13)00694-3journal_volume
5pub_type
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