Role of Iron and Superoxide for Generation of Hydroxyl Radical, Oxidative DNA Lesions, and Mutagenesis in Escherichia coli

Nunoshiba, Tatsuo; Obata, Fumio; Boss, Antoine C.; Oikawa, Shinji; Mori, Toshiaki; Kawanishi, Shousuke; Yamamoto, Kazuo

doi:10.1074/jbc.274.49.34832

Cited by 105 publications

(77 citation statements)

References 37 publications

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“…A misbalance in iron homeostasis is well known to cause DNA damage (Nunoshiba et al, 1999). Therefore, we analyzed the expression of genes encoding plant poly(ADPribose) polymerases (APP and ZAP) and Rad51-like protein (AtRAD51), which might constitute the components of the base excision repair (Babiychuk et al, 1998) and recombination repair pathways (Doutriaux et al, 1998;Ries et al, 2000), respectively.…”

Section: The Classical Fe/s Cluster Biosynthesis Pathway Is Present Imentioning

confidence: 99%

A Mutation of the Mitochondrial ABC Transporter Sta1 Leads to Dwarfism and Chlorosis in the Arabidopsis Mutant starik

et al. 2001

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A mutation in the Arabidopsis gene STARIK leads to dwarfism and chlorosis of plants with an altered morphology of leaf and cell nuclei. We show that the STARIK gene encodes the mitochondrial ABC transporter Sta1 that belongs to a subfamily of Arabidopsis half-ABC transporters. The severity of the starik phenotype is suppressed by the ectopic expression of the STA2 homolog; thus, Sta1 function is partially redundant. Sta1 supports the maturation of cytosolic Fe/S protein in ⌬ atm1 yeast, substituting for the ABC transporter Atm1p. Similar to Atm1p-deficient yeast, mitochondria of the starik mutant accumulated more nonheme, nonprotein iron than did wild-type organelles. We further show that plant mitochondria contain a putative L -cysteine desulfurase. Taken together, our results suggest that plant mitochondria possess an evolutionarily conserved Fe/S cluster biosynthesis pathway, which is linked to the intracellular iron homeostasis by the function of Atm1p-like ABC transporters. INTRODUCTIONABC transporters constitute one of the largest protein families with diverse functions in membrane transport. The designation of ABC transporter recognizes a highly conserved ATP binding cassette, which is the most characteristic feature of this superfamily. These proteins mediate the relatively specific, active transmembrane transport of molecules that can range in size from small ions to proteins (reviewed in Higgins, 1992) and utilize the energy of ATP hydrolysis to pump substrates across membranes, usually against a concentration gradient. The typical ABC transporter consists of four domains. Two of these domains are hydrophobic, and each comprises six membrane-spanning segments. The transmembrane domains are believed to form a channel and to determine the specificity of the transporter. The other two domains are located at the periphery of the membrane and couple ATP hydrolysis to the transport process.The ABC transporter Atm1p of budding yeast mitochondria represents a "half-transporter" in which one transmembrane and one ATP binding domain are expressed in a single polypeptide (Leighton and Schatz, 1995). Atm1p is localized in the mitochondrial inner membrane and is believed to function as an exporter, because its ABC domains face the mitochondrial matrix. The ATM1 loss-of-function results in respiration-deficient mitochondria that lack cytochromes (Leighton and Schatz, 1995; Kispal et al., 1997) and that tend to loose their DNA (Leighton and Schatz, 1995). These pleiotropic effects of the Atm1p deficiency are generally attributed to the fact that in ⌬ atm1 cells, mitochondria accumulate up to 30-fold higher levels of iron than do wild-type organelles (Kispal et al., 1997;Mitsuhashi et al., 2000). The Atm1p transport function appears to be conserved in eukaryotes, and the human mitochondrial ABC transporters Abc7 and MTABC3 have been shown to be true functional orthologs of the Atm1p (Csere et al., 1998;Mitsuhashi et al., 2000). The human ABC7 gene has been implicated in hereditary X-linked sideroblastic anemia and a...

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Section: The Classical Fe/s Cluster Biosynthesis Pathway Is Present Imentioning

confidence: 99%

A Mutation of the Mitochondrial ABC Transporter Sta1 Leads to Dwarfism and Chlorosis in the Arabidopsis Mutant starik

et al. 2001

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“…It was recently suggested that a central function of Fur is sequestration of Fe(II). Various phenotypes associated with null mutations in fur have been attributed to a concomitant increase in cellular Fe(II) levels, one being increased mutagenesis (16,17). It has been suggested that, at least in part, the increased mutagene-sis is due to the lack of Fur to sequester the free iron (18).…”

mentioning

confidence: 99%

The YggX Protein of Salmonella enterica Is Involved in Fe(II) Trafficking and Minimizes the DNA Damage Caused by Hydroxyl Radicals

Gralnick

Downs

2003

Journal of Biological Chemistry

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“…Nunoshiba et al (31) suggest that the increased sensitivity to oxidative stress found in an E. coli fur mutant is due to a 2.5-fold increase in the amount of intracellular iron. This excess iron is thought to participate in Fenton chemistry, catalyzing the formation of damaging hydroxyl radicals in the presence of hydrogen peroxide.…”

Section: Resultsmentioning

confidence: 99%

“…Oxidative stress. E. coli and P. aeruginosa fur mutants have been shown to be more sensitive to oxidative stress, presumably due to an increase in intracellular iron (18,31). In order to test sensitivity to oxidative stress, cultures of wild-type and mutant B. japonicum strains were grown and spread plated, and filters with either sterile, distilled water or 3% H 2 O 2 were added to the plates.…”

Section: Resultsmentioning

confidence: 99%

A Dominant-NegativefurMutation inBradyrhizobium japonicum

2004

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In many bacteria, the ferric uptake regulator (Fur) protein plays a central role in the regulation of iron uptake genes. Because iron figures prominently in the agriculturally important symbiosis between soybean and its nitrogen-fixing endosymbiont Bradyrhizobium japonicum, we wanted to assess the role of Fur in the interaction. We identified a fur mutant by selecting for manganese resistance. Manganese interacts with the Fur protein and represses iron uptake genes. In the presence of high levels of manganese, bacteria with a wild-type copy of the fur gene repress iron uptake systems and starve for iron, whereas fur mutants fail to repress iron uptake systems and survive. The B. japonicum fur mutant, as expected, fails to repress iron-regulated outer membrane proteins in the presence of iron. Unexpectedly, a wild-type copy of the fur gene cannot complement the fur mutant. Expression of the fur mutant allele in wild-type cells leads to a fur phenotype. Unlike a B. japonicum fur-null mutant, the strain carrying the dominant-negative fur mutation is unable to form functional, nitrogen-fixing nodules on soybean, mung bean, or cowpea, suggesting a role for a Fur-regulated protein or proteins in the symbiosis.

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Role of Iron and Superoxide for Generation of Hydroxyl Radical, Oxidative DNA Lesions, and Mutagenesis in Escherichia coli

Cited by 105 publications

References 37 publications

A Mutation of the Mitochondrial ABC Transporter Sta1 Leads to Dwarfism and Chlorosis in the Arabidopsis Mutant starik

A Mutation of the Mitochondrial ABC Transporter Sta1 Leads to Dwarfism and Chlorosis in the Arabidopsis Mutant starik

The YggX Protein of Salmonella enterica Is Involved in Fe(II) Trafficking and Minimizes the DNA Damage Caused by Hydroxyl Radicals

A Dominant-NegativefurMutation inBradyrhizobium japonicum

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