RNase Activity is Post-Translationally Controlled During the Dark-Induced Senescence Program

Gallie, Daniel; Chang, Su‐Chih

doi:10.1007/978-94-011-4453-7_40

Cited by 1 publication

(2 citation statements)

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“…RNase and nuclease activities also increase during senescence when a decline in the level of antioxidants occurs. Several RNase and nuclease isoforms had been observed previously (Chang and Gallie, 1997) and no change in the distribution of these isoforms was observed during seedling growth in the light or dark (Gallie and Chang, 1999), suggesting that the observed dark-induced increase in RNase and nuclease activities is not a result of a redistribution among the isoforms. Instead, RNase activity could be inhibited by reducing agents and reactivated following removal of the reductants or by oxidizing agents.…”

Section: Discussionmentioning

confidence: 59%

“…The other two are neutral RNases that are approximately 26 and 27 kDa in size (Blank and McKeon, 1991a). These RNases are present at a low level in wheat under normal growth conditions but are induced as part of the senescence program (Blank and McKeon, 1991b) as has been shown for specific RNases in Arabidopsis and other species (McHale and Dove, 1968;Taylor et al, 1993;Green, 1994;Gallie and Chang, 1999). Single-stranded-specific nucleases, which can use RNA or DNA as substrates, have also been described in wheat and are conserved in size (31-44 kDa) (Blank and McKeon, 1989).…”

Section: Introductionmentioning

confidence: 92%

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RNase activity requires formation of disulfide bonds and is regulated by the redox state

2004

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The activity of many RNases requires the formation of one or more disulfide bonds which can contribute to their stability. In this study, we show that RNase activity and, to a much lesser extent, nuclease activity, are redox regulated. Intracellular RNase activity was altered in vitro by changes in the glutathione redox state. Moreover, RNase activity was abolished following exposure to reducing agents such as beta-ME or DTT. Following reduction with glutathione (GSH), RNase activity could be fully reactivated with oxidized glutathione (GSSG). In contrast, RNase activity could not be reactivated when reduced with DTT. Decreasing the level of glutathione in vivo in wheat increased RNase activity. Tobacco engineered to have an increased glutathione redox state exhibited substantially lower RNase activity during dark-induced senescence. These results suggest that RNase activity requires the presence of one or more disulfide bonds that are regulated by glutathione and demonstrate for the first time that RNase activity can be altered with an alteration in cellular redox state.

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Section: Discussionmentioning

confidence: 59%