Interactions and Reactions of Ferritin with DNA

Surguladze, Nodar; Thompson, Khristy M.; Beard, John L.; Connor, James R.; Fried, Mike

doi:10.1074/jbc.m313348200

Cited by 67 publications

(65 citation statements)

References 50 publications

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“…A wide range of nucleic acid sizes (lengths from short oligonucleotides to several thousand nt/bp 18,19 ) and structures (single-stranded, duplex, triplex 20 and quadruplex 21 nucleic acids as well as small circular DNAs 22 ) are compatible with the assay. Under favorable conditions, the distribution of proteins between several nucleic acid molecules can be monitored within a single solution 18,23 , as can the presence of complexes differing in protein stoichiometry and/or binding site distribution 7,24 . Proteins ranging in size from small oligopeptides to transcription complexes with M r ≥ 10 6 can give useful mobility shifts 25,26 and the assay works well with both highly-purified proteins and crude cell extracts 27 .…”

Section: Advantages and Limitations Of Emsamentioning

confidence: 99%

Electrophoretic mobility shift assay (EMSA) for detecting protein–nucleic acid interactions

2007

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The gel electrophoresis mobility shift assay (EMSA) is used to detect protein complexes with nucleic acids. It is the core technology underlying a wide range of qualitative and quantitative analyses for the characterization of interacting systems. In the classical assay, solutions of protein and nucleic acid are combined and the resulting mixtures are subjected to electrophoresis under native conditions through polyacrylamide or agarose gel. After electrophoresis, the distribution of species containing nucleic acid is determined, usually by autoradiography of 32 P-labeled nucleic acid. In general, protein-nucleic acid complexes migrate more slowly than the corresponding free nucleic acid. In this article, we identify the most important factors that determine the stabilities and electrophoretic mobilities of complexes under assay conditions. A representative protocol is provided and commonly used variants are discussed. Expected outcomes are briefly described. References to extensions of the method and a troubleshooting guide are provided.

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Section: Advantages and Limitations Of Emsamentioning

confidence: 99%

Electrophoretic mobility shift assay (EMSA) for detecting protein–nucleic acid interactions

2007

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“…This places the H-subunit rich ferritins in a strategic position to ward off possible oxidative onslaughts to DNA or, alternatively, to donate iron for enzyme activity and possibly the nicking of double stranded DNA that could result in relaxation of superhelical stress (Surguladze et al, 2004). It was shown that not only does H-subunit rich ferritin form a stable complex with DNA (Surguladze et al, 2004), but that DNA also contains specific iron-binding sites (Thompson et al, 2002).…”

Section: Ferritin In Cellular Organellesmentioning

confidence: 99%

“…It was shown that not only does H-subunit rich ferritin form a stable complex with DNA (Surguladze et al, 2004), but that DNA also contains specific iron-binding sites (Thompson et al, 2002).…”

Section: Ferritin In Cellular Organellesmentioning

confidence: 99%

Ferritin and ferritin isoforms I: Structure–function relationships, synthesis, degradation and secretion

Koorts

Viljoen

2007

Archives of Physiology and Biochemistry

134

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Ferritin is the intracellular protein responsible for the sequestration, storage and release of iron. Ferritin can accumulate up to 4500 iron atoms as a ferrihydrite mineral in a protein shell and releases these iron atoms when there is an increase in the cell's need for bioavailable iron. The ferritin protein shell consists of 24 protein subunits of two types, the H-subunit and the L-subunit. These ferritin subunits perform different functions in the mineralization process of iron. The ferritin protein shell can exist as various combinations of these two subunit types, giving rise to heteropolymers or isoferritins. Isoferritins are functionally distinct and characteristic populations of isoferritins are found depending on the type of cell, the proliferation status of the cell and the presence of disease. The synthesis of ferritin is regulated both transcriptionally and translationally. Translation of ferritin subunit mRNA is increased or decreased, depending on the labile iron pool and is controlled by an ironresponsive element present in the 5'-untranslated region of the ferritin subunit mRNA. The transcription of the genes for the ferritin subunits is controlled by hormones and cytokines, which can result in a change in the pool of translatable mRNA. The levels of intracellular ferritin are determined by the balance between synthesis and degradation. Degradation of ferritin in the cytosol results in complete release of iron, while degradation in secondary lysosomes results in the formation of haemosiderin and protection against iron toxicity. The majority of ferritin is found in the cytosol. However, ferritin with slightly different properties can also be found in organelles such as nuclei and mitochondria. Most of the ferritin produced intracellularly is harnessed for the regulation of iron bioavailability; however, some of the ferritin is secreted and internalized by other cells. In addition to the regulation of iron bioavailability ferritin may contribute to the control of myelopoiesis and immunological responses.

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“…The ethyl acetate and methanol extracts showed lower protection. Surguladze et al 28 also reported the scission of supercoiled DNA strand to nicked circular form by free radicals. The rate of nicking correlated with the iron content and was strongly inhibited by radical scavengers and chelators.…”

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Chemical composition, angiotensin I-converting enzyme (ACE) inhibitory, antioxydant and antimicrobial activities of Ononis natrix leaves extracts

Sayari

Saidi

Sila

et al. 2016

FRA

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Background and aim:The use of synthetic antioxidants has begun to be restricted because of their induction of DNA damage and their toxicity. So, it is an interesting and useful task to find new sources for natural antioxidant and functional food. The health benefits of Ononis natrix leaves were widely investigated. The present study describes for the first time the antioxidant, antibacterial and antihypertensive activities of various solvent extracts of Ononis natrix leaves. Method: The aerial parts (leaves) of O. natrix were collected from the South of Tunisia and different solvent extracts were prepared. The antioxidant activities of extracts at different concentrations were evaluated using various in vitro antioxidant assays, including 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging, reducing power, β-carotene bleaching and DNA nicking assays. The antibacterial and angiotensin I-converting enzyme (ACE) inhibitory were also investigated. Results: All the extracts showed strong antioxidant activity. The radical scavenging activities and reducing powers of all the extracts were close to those of the synthetic antioxidant BHA. The chloroform extract exhibited high inhibition of β-carotene bleaching and also showed a well DNA protection against degradation by hydroxyl radicals. Moreover, the antimicrobial activities of the extracts were tested against nine species of microorganisms, and the results obtained showed significant antibacterial activity against the Gram-positive and Gram-negative bacteria. O. natrix extract showed also important antihypertensive activities. Conclusion: The obtained results demonstrated the health benefit features of Ononis natrix leaves and their potential uses as feedstock of bioactive molecules.

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Interactions and Reactions of Ferritin with DNA

Cited by 67 publications

References 50 publications

Electrophoretic mobility shift assay (EMSA) for detecting protein–nucleic acid interactions

Electrophoretic mobility shift assay (EMSA) for detecting protein–nucleic acid interactions

Ferritin and ferritin isoforms I: Structure–function relationships, synthesis, degradation and secretion

Chemical composition, angiotensin I-converting enzyme (ACE) inhibitory, antioxydant and antimicrobial activities of Ononis natrix leaves extracts

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