The redox/DNA repair protein, Ref-1, is essential for early embryonic development in mice.

Xanthoudakis, Steven; Smeyne, Richard J.; Wallace, James D.; Curran, Tom

doi:10.1073/pnas.93.17.8919

Cited by 470 publications

(321 citation statements)

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“…B6´F1, offspring from backcrosses of Dad1 /À males with C57Bl/6 females; F1´B6, offspring from backcrosses of C57Bl/6 males with Dad1 /À females. from the previous reports which dealt with early postimplantation lethality (Spyropoulos & Capecchi 1994;Fa Èssler & Meyer 1995;Feldman et al 1995;Jones et al 1995;Montes de Oca Luna et al 1995;Stephens et al 1995;Lim & Hasty 1996;Liu et al 1996;Tsuzuki et al 1996;Xanthoudakis et al 1996;Murphy et al 1997;Takeda et al 1997). Dad1 À/À embryos displayed many cells containing fragmented, TUNEL-positive nuclei, ®ndings which differed markedly from those of the previous reports, indicating that apoptosis had occurred simultaneously in the embryo itself (Fig.…”

Section: Discussionmentioning

confidence: 59%

Abnormalities of developmental cell death in Dad1‐deficient mice

et al. 1999

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Section: Discussionmentioning

confidence: 59%

Abnormalities of developmental cell death in Dad1‐deficient mice

et al. 1999

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“…The redundancy in this repair process is in apparent contrast with the inability to generate mice that are defective in BER, as seen with HAP1 (Xanthoudakis et al, 1996) and Pol b (Gu et al, 1994). It will be interesting to know whether the e ect on embryonic development resides in functions other than DNA repair (Xanthoudakis et al, 1992;Plug et al, 1997).…”

Section: Discussionmentioning

confidence: 99%

Mammalian base excision repair by DNA polymerases δ and ε

et al. 1998

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Two distinct pathways for completion of base excision repair (BER) have been discovered in eukaryotes: the DNA polymerase b (Pol b )-dependent short-patch pathway that involves the replacement of a single nucleotide and the long-patch pathway that entails the resynthesis of 2-6 nucleotides and requires PCNA. We have used cell extracts from Pol b-deleted mouse ®broblasts to separate subfractions containing either Pol d or Pol e. These fractions were then tested for their ability to perform both short-and long-patch BER in an in vitro repair assay, using a circular DNA template, containing a single abasic site at a de®ned position. Remarkably, both Pol d and Pol e were able to replace a single nucleotide at the lesion site, but the repair reaction is delayed compared to single nucleotide replacement by Pol b. Furthermore, our observations indicated, that either Pol d and/or Pol e participate in the long-patch BER. PCNA and RF-C, but not RP-A are required for this process. Our data show for the ®rst time that Pol d and/or Pol e are directly involved in the long-patch BER of abasic sites and might function as back-up system for Pol b in one-gap ®lling reactions.

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“…APE1 recognizes these AP sites and incises the DNA 5' to the lesion, leaving the 3'OH and 5'phosphate residues, as described above. Mice with a targeted homozygous null mutation in the APE1 (Ref-1) gene die during early embryonic development [36]. Detailed analysis of APE1 null embryos (pre-implantation APE1 null embryos) following ionizing radiation indicate a role for APE1 in the repair of ionizing-induced DNA damage [37].…”

Section: Mono-functional and Bi-functional Dna Glycosylases And Ap-simentioning

confidence: 99%

A unified view of base excision repair: Lesion-dependent protein complexes regulated by post-translational modification

Almeida¹,

Sobol²

2007

DNA Repair

387

374

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Base excision repair (BER) proteins act upon a significantly broad spectrum of DNA lesions that result from endogenous and exogenous sources. Multiple sub-pathways of BER (short-path or longpatch) and newly designated DNA repair pathways (e.g., SSBR and NIR) that utilize BER proteins complicate any comprehensive understanding of BER and its role in genome maintenance, chemotherapeutic response, neurodegeneration, cancer or aging. Herein, we propose a unified model of BER, comprised of three functional processes: Lesion Recognition/Strand Scission, Gap Tailoring and DNA Synthesis/Ligation, each represented by one or more multiprotein complexes and coordinated via the XRCC1/DNA Ligase III and PARP1 scaffold proteins. BER therefore may be represented by a series of repair complexes that assemble at the site of the DNA lesion and mediates repair in a coordinated fashion involving protein-protein interactions that dictate subsequent steps or sub-pathway choice. Complex formation is influenced by post-translational protein modifications that arise from the cellular state or the DNA damage response, providing an increase in specificity and efficiency to the BER pathway. In this review, we have summarized the reported BER proteinprotein interactions and protein post-translational modifications and discuss the impact on DNA repair capacity and complex formation.

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The redox/DNA repair protein, Ref-1, is essential for early embryonic development in mice.

Abstract: The DNA-binding activity of AP-1 proteins is modulated, in vitro, by a posttranslational mechanism involving reduction oxidation. This mode of regulation has been proposed to control both the transcriptional activity and the oncogenic potential of Fos

Cited by 470 publications

References 48 publications

Abnormalities of developmental cell death in Dad1‐deficient mice

Abnormalities of developmental cell death in Dad1‐deficient mice

Mammalian base excision repair by DNA polymerases δ and ε

A unified view of base excision repair: Lesion-dependent protein complexes regulated by post-translational modification

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