Capítulos de libros
Ferritin As Part Of The Antioxidative Machinery In Plants Under Stress
Registro en:
9781619423473
Ferritin: Functions, Biosynthesis And Regulation. Nova Science Publishers, Inc., v. , n. , p. 65 - 82, 2012.
2-s2.0-84892902579
Autor
Bottcher A.
Mazzafera P.
Institución
Resumen
Ferritins are a superfamily of iron-storage proteins that are found in all living organisms with the exception of yeast. They are ubiquitous, iron-binding proteins that play an important role in cellular iron homoeostasis, storing up to 4,500 iron atoms in their central cavities. In plants, ferritins are preferentially localised in the plastids but are also found in mitochondria. Ferritin expression is developmentally regulated and plays a role in the synthesis of iron-containing proteins that are involved in photosynthesis in the early stages of plant development. It accumulates in seeds during embryo maturation to provide iron during germination, allowing for the proper formation of the photosynthetic apparatus. Ferritins are transcriptionally controlled by iron, which induces the production of reactive oxygen species (ROS) in the Fenton reaction in its free form and thus has a high potential for toxicity. Several reports have shown that the transcription of ferritin in plants may be induced by environmental factors, such as drought, salinity, cold, light intensity, pathogen attack, NO and ozone, which then stimulate ROS production. Studies that have analysed other stresses, such as those caused by herbicides and heavy metals, have also shown increased expression levels of the ferritin genes. These reports suggest that ROS induces ferritin transcription and that ferritin plays a protective role by capturing free iron and limiting oxidative damage to the cell. Recent evidence of ferritins effectively participating in the defensive machinery of plants under oxidative stress was obtained from transgenic plants that overexpressed ferritin genes. This review is focused on the protective role of ferritin in plants that are threatened by oxidative damage in response to biotic and abiotic stresses. © 2012 by Nova Science Publishers, Inc. All rights reserved.
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