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Would the real arsenate reductase please stand up?
| Content Provider | Semantic Scholar |
|---|---|
| Author | Salt, David E. |
| Copyright Year | 2017 |
| Abstract | Over the last two decades a debate has been simmering within a group of plant biologists about the true identity of the enzyme that reduces arsenate to arsenite in plants. Would the real arsenate reductase please stand up? This debate was initiated with the release of the Arabidopsis thaliana genome allowing comparisons to be made between yeast and plants, progressed through the release of rice genome, the use of gene knockout, knockdown and overexpression, and ended with the application of forward genetics. This has not been an inconsequential debate. Inorganic arsenic is classified as a non-threshold class-1 human carcinogen. Further, its elevated level in rice (Oryza sativa) produced in Bangladesh, China, and India poses a real risk of cancer given the high consumption of rice typical of many Southeast Asian countries. Rice products (such as baby food) and juices (such as apple and grape) can also contain inorganic arsenic. In this issue of New Phytologist Xu et al. (pp. ??) provide new and exciting evidence for the identity and function of an enzyme that plays an important role in controlling arsenic accumulation in rice. This enzyme was identified by Xu and co-workers based on the simple assumption that genes involved in arsenic processing in plants would, when disabled, cause the plant to become more sensitive to the toxic effects of arsenic. Using this simple assumption, Xu and co-workers generated a large population of rice plants which contained randomly mutated genes. By screening this population for individual plants with increased sensitivity to arsenic, and by applying a mapping-by-sequencing approach, they were able to efficiently identify genes that play an important role in this process. What this revealed is that a gene encoding an enzyme that chemically reduces arsenate (As) to arsenite (As) is required for resistance of rice to the toxic effects of arsenate. In itself, such a discovery was not a surprise as it builds on almost 20-years of research into how plants cope with arsenate, which is toxic because it mimics phosphate and disrupts high-energy phosphate metabolism. However, the work of Xu et al provides strong evidence that it is the HAC-like class of arsenate reductases rather than the ACR2-like class that govern this critical step in how plants process arsenate into arsenic. Extending what we knew in A. thaliana into rice, allowing us to broaden our conclusions from dicots to monocots. |
| Starting Page | 926 |
| Ending Page | 928 |
| Page Count | 3 |
| File Format | PDF HTM / HTML |
| DOI | 10.1111/nph.14691 |
| PubMed reference number | 28695678 |
| Journal | Medline |
| Volume Number | 215 |
| Issue Number | 3 |
| Alternate Webpage(s) | http://eprints.nottingham.ac.uk/47089/1/Xu%20et%20al.%202017%20Commentary_Final_V3.pdf |
| Alternate Webpage(s) | https://doi.org/10.1111/nph.14691 |
| Journal | The New phytologist |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
