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      Iron content and ferritin gene expression in common bean (Phaseolus vulgaris L.) Translated title: Contenido de hierro y expresión del gen ferritina en frijol común (Phaseolus vulgaris L.)

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          Abstract

          An experimental analysis was conducted to determine iron content, ferritin gene activity and ferritin protein content, in different plant organs and growth stages of four common bean cultivars. Ferritin mRNA expression, determined by quantitative PCR, showed differential expression among cultivars and was not stable across growth stages and plant organs. Ferritin protein content was significantly higher in seeds (65.6-271.1 mg kg-1 fresh weight), whereas pods, roots, stems and leaves had significant lower levels (3.7-26.7 mg kg-1 fresh weight). Iron content in leaves was found in outstanding amounts (643 mg kg-1), up to 12 times higher than in seeds (52 mg kg-1); no relationship was found between ferritin transcriptional levels and ferritin protein contents with iron content. Results indicated that ferritin gene regulation is non-iron dependent in common bean.

          Translated abstract

          Se condujo un análisis experimental para determinar el contenido de hierro, actividad del gen ferritina y contenido de la proteína codificada por el gen en diferentes órganos y etapas de crecimiento de cuatro cultivares de frijol común. La expresión de mRNA de ferritina por PCR cuantitativo mostró expresión diferencial entre cultivares y no fue estable a través de diferentes etapas de desarrollo y tipos de órganos. El contenido de la proteína ferritina fue significativamente superior en semillas (65.6-271.1 mg kg-1 peso fresco), mientras que en vainas, raíces, tallos y hojas los valores fueron significativamente menores (3.7-26.7 mg kg-1peso fresco). El contenido de hierro en hojas tuvo niveles sobresalientes (643 mg kg-1), representando niveles hasta 12 veces superiores a los encontrados en semilla (52 mg kg-1). No se encontró relación entre los niveles transcripcionales de ferritina y los contenidos de proteína con el contenido de hierro. Los resultados indican que la regulación del gen ferritina en frijol común no depende del contenido de hierro.

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          Localization of iron in Arabidopsis seed requires the vacuolar membrane transporter VIT1.

          Iron deficiency is a major human nutritional problem wherever plant-based diets are common. Using synchrotron x-ray fluorescence microtomography to directly visualize iron in Arabidopsis seeds, we show that iron is localized primarily to the provascular strands of the embryo. This localization is completely abolished when the vacuolar iron uptake transporter VIT1 is disrupted. Vacuolar iron storage is also critical for seedling development because vit1-1 seedlings grow poorly when iron is limiting. We have uncovered a fundamental aspect of seed biology that will ultimately aid the development of nutrient-rich seed, benefiting both human health and agricultural productivity.
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            Ferritin: structure, gene regulation, and cellular function in animals, plants, and microorganisms.

            E H Theil (1986)
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              Mineralization in ferritin: an efficient means of iron storage.

              Ferritins are a class of iron storage and mineralization proteins found throughout the animal, plant, and microbial kingdoms. Iron is stored within the protein shell of ferritin as a hydrous ferric oxide nanoparticle with a structure similar to that of the mineral "ferrihydrite." The eight hydrophilic channels that traverse the protein shell are thought to be the primary avenues by which iron gains entry to the interior of eukaryotic ferritins. Twenty-four subunits constitute the protein shell and, in mammalian ferritins, are of two types, H and L, which have complementary functions in iron uptake. The H chain contains a dinuclear ferroxidase site that is located within the four-helix bundle of the subunit; it catalyzes the oxidation of ferrous iron by O(2), producing H(2)O(2). The L subunit lacks this site but contains additional glutamate residues on the interior surface of the protein shell which produce a microenvironment that facilitates mineralization and the turnover of iron(III) at the H subunit ferroxidase site. Recent spectroscopic studies have shown that a di-Fe(III) peroxo intermediate is produced at the ferroxidase site followed by formation of a mu-oxobridged dimer, which then fragments and migrates to the nucleation sites to form incipient mineral core species. Once sufficient core has developed, iron oxidation and mineralization occur primarily on the surface of the growing crystallite, thus minimizing the production of potentially harmful H(2)O(2). Copyright 1999 Academic Press.
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                Author and article information

                Contributors
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Journal
                agritm
                Agricultura técnica en México
                Agric. Téc. Méx
                Instituto Nacional de Investigaciones Forestales, Agrícolas y Pecuarias (México )
                0568-2517
                December 2008
                : 34
                : 4
                : 481-489
                Affiliations
                [1 ] Instituto Nacional de Investigaciones Forestales, Agrícolas y Pecuarias Mexico
                [2 ] Instituto Nacional de Investigaciones Forestales, Agrícolas y Pecuarias Mexico
                Article
                S0568-25172008000400011
                a13760c0-ed5b-4fb5-b005-e35cf0fb54fa

                http://creativecommons.org/licenses/by/4.0/

                History
                Categories
                Agriculture, Dairy & Animal Science
                Forestry

                Animal agriculture,Forestry
                gene expression,nutritional value,protein,quantitative PCR,expresión de genes,PCR cuantitativo,proteína,valor nutricional

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