ArticlePlant molecular biology2004
RNase activity requires formation of disulfide bonds and is regulated by the redox state.
Article in Plant molecular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 25 citations in OpenAlex.
- In-depth comparison of methods to isolate RNA from common human cell lines.BMC genomics · 2026Article
- Genome-wide association mapping of biochemical traits and its correlation with MYMIV resistance in mungbean (Vigna radiata L. Wilczek).Scientific reports · 2024Article
- Development and Validation of ScriptTaq COVID PCR: An In-House Multiplex rRT-PCR for Low-Cost Detection.Current issues in molecular biology · 2022Article
- Mechanical Stability of Ribonuclease A Heavily Depends on the Redox Environment.The journal of physical chemistry. B · 2022Article
- DeLTa-Seq: direct-lysate targeted RNA-Seq from crude tissue lysate.Plant methods · 2022Article
- Rational Design of CRISPR/Cas12a-RPA Based One-Pot COVID-19 Detection with Design of Experiments.ACS synthetic biology · 2022Article
- Article
- RABL6A Promotes Pancreatic Neuroendocrine Tumor Angiogenesis and Progression In Vivo.Biomedicines · 2021Article
- Article
- The rice pathogen-related protein 10 (JIOsPR10) is induced by abiotic and biotic stresses and exhibits ribonuclease activity.Plant cell reports · 2008Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.