A role for iron–sulfur clusters in DNA repair

Lukianova, O.A.; David, Sheila S.

doi:10.1016/j.cbpa.2005.02.006

Cited by 130 publications

(120 citation statements)

References 32 publications

Supporting

Mentioning

118

Contrasting

Order By: Relevance

“…ferritin | phytoplankton | Ostreococcus | circadian | iron I ron is a cofactor involved in numerous redox-based biological processes such as DNA synthesis, photosynthesis, nitrogen fixation, mitochondrial respiration, and the detoxification of reactive oxygen species (1)(2)(3)(4)(5)(6). Although iron is essential for living organisms, it also is highly reactive and toxic via the Fenton reaction (7).…”

mentioning

confidence: 99%

Central role for ferritin in the day/night regulation of iron homeostasis in marine phytoplankton

Botebol

Lesuisse

Šuták

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

In large regions of the open ocean, iron is a limiting resource for phytoplankton. The reduction of iron quota and the recycling of internal iron pools are among the diverse strategies that phytoplankton have evolved to allow them to grow under chronically low ambient iron levels. Phytoplankton species also have evolved strategies to cope with sporadic iron supply such as long-term storage of iron in ferritin. In the picophytoplanktonic species Ostreococcus we report evidence from observations both in the field and in laboratory cultures that ferritin and the main ironbinding proteins involved in photosynthesis and nitrate assimilation pathways show opposite diurnal expression patterns, with ferritin being maximally expressed during the night. Biochemical and physiological experiments using a ferritin knock-out line subsequently revealed that this protein plays a central role in the diel regulation of iron uptake and recycling and that this regulation of iron homeostasis is essential for cell survival under iron limitation.

show abstract

mentioning

confidence: 99%

Central role for ferritin in the day/night regulation of iron homeostasis in marine phytoplankton

Botebol

Lesuisse

Šuták

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…3,4 Early evidence indicated that Fe-S clusters in these enzymes are not amenable to oxidation or reduction in solution and suggested structural or regulatory roles of the cofactor. 5,6 More recent electrochemical studies of glycosylases immobilised on DNA-modified electrodes indicated that the [4Fe-4S] cluster is activated towards oxidation upon binding to DNA. It was proposed that the cluster exerts a function in DNAmediated signalling for detection of DNA lesions, [7][8][9][10][11][12] but based on data obtained by electrochemical approaches, which cannot provide any information about the molecular origin of the electrochemical signal.…”

mentioning

confidence: 99%

Surface enhanced vibrational spectroscopic evidence for an alternative DNA-independent redox activation of endonuclease III

et al. 2015

View full text Add to dashboard Cite

Surface enhanced vibrational spectro-electrochemistry of endonuclease III provides direct evidence that the [4Fe-4S] cluster is responsible for the enzyme redox activity, and that this process is not exclusively DNA-mediated, as currently proposed. We report the first surface enhanced resonance Raman spectrum of a [4Fe-4S] 2+ cluster containing enzyme.Deinococcus radiodurans is an extremely radiation and desiccation resistant bacterium, which can withstand 200-fold higher irradiation doses than other bacteria. 1,2 The resistance mechanism is not known, but an efficient DNA repair machinery is considered to play a key role in it. Endonuclease III (EndoIII) is a [4Fe-4S] cluster containing DNA repair enzyme from the helix-hairpin-helix family of DNA glycosylases, crucial for removal of oxidation damaged bases in DNA. 3,4 Early evidence indicated that Fe-S clusters in these enzymes are not amenable to oxidation or reduction in solution and suggested structural or regulatory roles of the cofactor. 5,6 More recent electrochemical studies of glycosylases immobilised on DNA-modified electrodes indicated that the [4Fe-4S] cluster is activated towards oxidation upon binding to DNA. It was proposed that the cluster exerts a function in DNAmediated signalling for detection of DNA lesions, 7-12 but based on data obtained by electrochemical approaches, which cannot provide any information about the molecular origin of the electrochemical signal. Here we employed surface enhanced resonance Raman (SERR) spectroscopy and surfaced enhanced IR absorption (SEIRA) spectro-electrochemistry to demonstrate that the cluster of the immobilised EndoIII from D. radiodurans (DrEndoIII) is prone to reduction, which is not necessarily DNA-mediated.DrEndoIII was electronically coupled to metal electrodes modified with bifunctional alkanethiol-based self assembled monolayers (SAMs). 13 The cluster integrity of DrEndoIII immobilised on the 11-mercapto-undecanoic acid (MUA)-coated nanostructured Ag working electrode was probed by SERR spectroscopy. For DrEndoIII, which has a broad electronic absorption band centered at 410 nm, both the plasmonic and the resonance enhancement conditions are well matched using 413 nm excitation. 14 The negatively charged MUA surface readily interacts with the highly positively charged DNA binding site of DrEndoIII (vide infra) that includes the active site pocket and the [4Fe-4S] cluster (Fig. S1, ESI †), which is in glycosylases optimised for a fast and precise accommodation of the negatively charged DNA substrate. 4,[15][16][17] Upon protein immobilisation and removal of the loosely bound molecules by rinsing with buffer, the functionalised flat disk Ag electrode was inserted into a pre-cooled cryostat that was rapidly cooled to 77 K. The SERR spectrum of the Ag-MUADrEndoIII construct was measured at 77 K since the intrinsically weak RR bands of Fe-S clusters can only be detected at low temperatures. 18,19 The spectrum shows well defined modes at 337, 363 and 384 cm À1 (Fig. 1a), indicative of a [4Fe-4S] clus...

show abstract

“…Several DNA repair proteins contain redox-active [4Fe-4S] clusters that are not required for folding (12,13). Examples of these proteins from the BER pathway, EndoIII, and MutY, are activated toward oxidation as they bind DNA (14)(15)(16). While EndoIII effectively removes oxidized pyrimidines, the repair protein is found in very low copy number in E. coli (approximately 500 copies per cell) (17,18).…”

mentioning

confidence: 99%

DNA charge transport as a first step in coordinating the detection of lesions by repair proteins

Sontz

Mui

Fuss

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

127

View full text Add to dashboard Cite

Damaged bases in DNA are known to lead to errors in replication and transcription, compromising the integrity of the genome. We have proposed a model where repair proteins containing redoxactive [4Fe-4S] clusters utilize DNA charge transport (CT) as a first step in finding lesions. In this model, the population of sites to search is reduced by a localization of protein in the vicinity of lesions. Here, we examine this model using single-molecule atomic force microscopy (AFM). XPD, a 5′-3′ helicase involved in nucleotide excision repair, contains a [4Fe-4S] cluster and exhibits a DNAbound redox potential that is physiologically relevant. In AFM studies, we observe the redistribution of XPD onto kilobase DNA strands containing a single base mismatch, which is not a specific substrate for XPD but, like a lesion, inhibits CT. We further provide evidence for DNA-mediated signaling between XPD and Endonuclease III (EndoIII), a base excision repair glycosylase that also contains a [4Fe-4S] cluster. When XPD and EndoIII are mixed together, they coordinate in relocalizing onto the mismatched strand. However, when a CT-deficient mutant of either repair protein is combined with the CT-proficient repair partner, no relocalization occurs. These data not only indicate a general link between the ability of a repair protein to carry out DNA CT and its ability to redistribute onto DNA strands near lesions but also provide evidence for coordinated DNA CT between different repair proteins in their search for damage in the genome.DNA electron transfer | iron-sulfur clusters | oxidative damage

show abstract

A role for iron–sulfur clusters in DNA repair

Cited by 130 publications

References 32 publications

Central role for ferritin in the day/night regulation of iron homeostasis in marine phytoplankton

Central role for ferritin in the day/night regulation of iron homeostasis in marine phytoplankton

Surface enhanced vibrational spectroscopic evidence for an alternative DNA-independent redox activation of endonuclease III

DNA charge transport as a first step in coordinating the detection of lesions by repair proteins

Contact Info

Product

Resources

About