Changing paradigms for the micronutrient zinc, a known protein cofactor, as a signal relaying also cellular redox state
The micronutrient zinc (Zn) is often poorly available but toxic when present in excess, so a tightly controlled Zn homoeostasis network operates in all organisms. This review summarizes our present understanding of plant Zn homoeostasis. In Arabidopsis, about 1,900 Zn-binding metalloproteins require...
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| Format: | Article |
| Language: | English |
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Cambridge University Press
2025-01-01
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| Series: | Quantitative Plant Biology |
| Subjects: | |
| Online Access: | https://www.cambridge.org/core/product/identifier/S2632882825000049/type/journal_article |
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| Summary: | The micronutrient zinc (Zn) is often poorly available but toxic when present in excess, so a tightly controlled Zn homoeostasis network operates in all organisms. This review summarizes our present understanding of plant Zn homoeostasis. In Arabidopsis, about 1,900 Zn-binding metalloproteins require Zn as a cofactor. Abundant Zn metalloproteins reside in plastids, mitochondria and peroxisomes, emphasizing the need to address how Zn reaches these proteins. Apo–Zn metalloproteins do not acquire Zn2+ from a cytosolic pool of free cations, but instead through associative ligand exchange from Zn-buffering molecules. The importance of cytosolic thiols in Zn buffering suggests that, besides elevated Zn influx, a more oxidized redox state is also predicted to cause elevated labile-bound Zn levels, consistent with the suppression of a Zn deficiency marker under oxidative stress. Therefore, we consider a broadened physiological scope in plants for a possible signalling role of Zn2+, experimentally supported only in animals to date. |
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| ISSN: | 2632-8828 |