Human mitochondrial transcription factor A binds preferentially to oxidatively damaged DNA

Yoshida, Yoichiro; Izumi, Hiroto; Ise, Tomoko; Uramoto, Hidetaka; Torigoe, Takayuki; Ishiguchi, Hiroshi; Murakami, Tadashi; Tanabe, Michiharu; Nakayama, Yoshifumi; Itoh, Hideaki; Kasai, Hiroshi; Kohno, Kimitoshi

doi:10.1016/s0006-291x(02)00757-x

Cited by 66 publications

(69 citation statements)

References 49 publications

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“…Glutaraldehyde crosslinking experiments were carried out to determine whether the presence of RNA results in a decrease in the formation of p53 tetramers. GST-p53 was highly purified by the gel-purification method as described previously ( Figure 2d, lane 2) (Yoshida et al, 2002). As shown in Figure 2d, formation of tetramers and dimers of the highly purified GST-p53 was reduced in the presence of RNA.…”

Section: Oligomerization Of P53 Is Enhanced By Rnase a Treatmentmentioning

confidence: 84%

“…GST and ThioHis fusion proteins were induced by 1 mM isopropyl-1-thio--D-galactopyranoside as described previously (Yoshida et al, 2002). The E. coli cells were sonicated for 10 s in binding buffer (50 mM Tris-HCl pH 8.0, 1 mM EDTA, 120 mM NaCl, 10% glycerol, 0.5% Nonidet P-40, 1 mM DTT, and 0.5 mM PMSF), and the soluble fraction obtained by centrifugation at 21 000 g for 10 min at 41C.…”

Section: Expression and Purification Of Gst And Thiohis Fusion Proteinsmentioning

confidence: 99%

“…GST fusion proteins were heated for 10 min at 371C in SDS-PAGE loading buffer, and separated in a SDS 10% polyacrylamide slab gel. Gel strips containing the fractionated proteins were cut transversely with a razor blade as described previously (Yoshida et al, 2002). Each gel piece was then placed into a tube containing two volumes (per weight of the polyacrylamide slice) of elution -renaturation buffer (1% Triton X-100, 20 mM HEPES pH 7.6, 1 mM EDTA, 100 mM NaCl, 2 mM DTT, 0.1 mM PMSF) and homogenized with a small stainless steel pestle.…”

Section: Glutaraldehyde Crosslinkingmentioning

confidence: 99%

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Binding of RNA to p53 regulates its oligomerization and DNA-binding activity

et al. 2004

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The C-terminus of p53 is responsible for maintaining the latent, non-DNA-binding form of p53. However, the mechanism by which the C-terminus regulates DNA binding is not yet fully understood. We show here that p53 interacts with RNA via its C-terminal domain and that disruption of this interaction, by RNase A treatment, truncation or phosphorylation of the C-terminus, restores DNA-binding activity. Furthermore, the oligomerization of p53 is significantly enhanced by disrupting the interaction between p53 and RNA. These findings suggest that binding of RNA to p53 is involved in the mechanism of p53 latency.

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Section: Oligomerization Of P53 Is Enhanced By Rnase a Treatmentmentioning

confidence: 84%

Section: Expression and Purification Of Gst And Thiohis Fusion Proteinsmentioning

confidence: 99%

Section: Glutaraldehyde Crosslinkingmentioning

confidence: 99%

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Binding of RNA to p53 regulates its oligomerization and DNA-binding activity

et al. 2004

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“…It is a member of the family of HMG proteins and can recognize both cisplatin-modified and oxidatively damaged DNA. 21 We have shown that YB-1 recognizes the inverted CCAAT box as well as cisplatin-modified DNA. 5 YB-1 is a major core protein of messenger ribonucleoprotein particles, 22 and its overexpression in mammalian cells inhibits protein synthesis.…”

Section: Figurementioning

confidence: 87%

ZNF143 activates gene expression in response to DNA damage and binds to cisplatin‐modified DNA

Ishiguchi

Izumi

Torigoe

et al. 2004

Intl Journal of Cancer

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We have identified a cisplatin-inducible gene, the mitochondrial ribosomal protein S11 (MRP S11) gene, by means of mRNA differential display. Functional analysis of the MRP S11 promoter showed that a Staf binding site in the promoter is required for both basal promoter activity and cisplatin-inducible activity. We also found that Cisplatin is a widely used anticancer agent, and DNA damage is believed to be the main basis of the antitumor effect of cisplatin. Since cisplatin resistance is a major obstacle to the treatment of solid tumors, understanding the molecular basis of the DNA damage response and of cisplatin resistance is important for clinical protocols. Cisplatin resistance is thought to involve several mechanisms, including increased drug efflux, the presence of cellular thiols, increased nucleotide excision repair activity and decreased mismatch repair activity. [1][2][3][4] In addition, several mechanisms are thought to contribute to the DNA damage response associated with cisplatin resistance. To understand fully these molecular mechanisms, it is desirable to identify and characterize all the transcription factors that are activated by DNA damage. We have previously shown that transcription factors such as Y-box binding protein (YB-1) and the CCAAT-binding transcription factor 2 (CTF2) are overexpressed in human cancer cell lines resistant to cisplatin. 5,6 YB-1 has been shown to bind preferentially to cisplatin-modified DNA 5 and is activated by nuclear translocation and by transcriptional mechanisms. Oct1 participates in the cellular response to DNA damage, 7,8 and its induction involves posttranscriptional mechanisms. Both c-Myc and AP-1 are also activated and involved in cellular responses to cisplatin. 8 One cisplatininducible cDNA clone has been shown to encode the vacuolar H ϩ -ATPase subunit c (ATP6L), 9,10 and analysis of its expression revealed that both Sp1 and Oct1 are critical for its activation by anticancer agents. 11 In order to identify novel mechanisms involved in the DNA damage response, we have used differential display to compare gene expression between control and cisplatin-treated cells. Here, we characterize one cisplatin-inducible gene, MRP S11, whose product, MRP S11, is a component of the ribosomal small subunit and binds to 12S rRNA. 12 MRP S11 appears to have RNA binding but not DNA binding activity. We have isolated the promoter region of MRP S11 in order to identify its transcriptional activators. Functional analysis revealed a critical Staf binding site in the core of the promoter. The zinc finger transcription factor, Staf, originally identified in the frog, is involved in transcriptional regulation of snRNA type and mRNA promoters transcribed either by RNA polymerase II or III. 13 Two human homologues of Staf, ZNF 76 and ZNF 143, have been isolated. 14 Here we show that activation of the transcriptional activator ZNF 143 upregulates the transcription of MRP S11. We present evidence that ZNF 143, but not ZNF 76, is induced by DNA damage. We further demonstrate that ZN...

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“…Furthermore, TFAM has been shown to be intricately involved in the constitution of mtDNA nucleoids and the maintenance of the organelle genome (Kaufman et al 2007). TFAM has also been suggested to be a member of a system responsible for the sensing and repair of oxidative damage to mtDNA (Canugovi et al 2010;Yoshida et al 2002). Data about changes of TFAM content in various tissues during aging show a trend toward an increase (Dinardo et al 2003;Lezza et al 2001).…”

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confidence: 99%

Age- and calorie restriction-related changes in rat brain mitochondrial DNA and TFAM binding

Picca

Fracasso

Pesce

et al. 2012

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Aging markedly affects mitochondrial biogenesis and functions particularly in tissues highly dependent on the organelle's bioenergetics capability such as the brain's frontal cortex. Calorie restriction (CR) diet is, so far, the only intervention able to delay or prevent the onset of several age-related alterations in different organisms. We determined the contents of mitochondrial transcription factor A (TFAM), mitochondrial DNA (mtDNA), and the 4.8-kb mtDNA deletion in the frontal cortex from young (6-monthold) and aged (26-month-old), ad libitum-fed (AL) and calorie-restricted (CR), rats. We found a 70 % increase in TFAM amount, a 25 % loss in mtDNA content, and a 35 % increase in the 4.8-kb deletion content in the aged AL animals with respect to the young rats. TFAM-specific binding to six mtDNA regions was analyzed by mtDNA immunoprecipitation and semiquantitative polymerase chain reaction (PCR), showing a marked age-related decrease. Quantitative realtime PCR at two subregions involved in mtDNA replication demonstrated, in aged AL rats, a remarkable decrease (60-70 %) of TFAM-bound mtDNA. The decreased TFAM binding is a novel finding that may explain the mtDNA loss in spite of the compensatory TFAM increased amount. In aged CR rats, TFAM amount increased and mtDNA content decreased with respect to young rats' values, but the extent of the changes was smaller than in aged AL rats. Attenuation of the age-related effects due to the diet in the CR animals was further evidenced by the unchanged content of the 4.8-kb deletion with respect to that of young animals and by the partial prevention of the age-related decrease in TFAM binding to mtDNA.

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Human mitochondrial transcription factor A binds preferentially to oxidatively damaged DNA

Cited by 66 publications

References 49 publications

Binding of RNA to p53 regulates its oligomerization and DNA-binding activity

Binding of RNA to p53 regulates its oligomerization and DNA-binding activity

ZNF143 activates gene expression in response to DNA damage and binds to cisplatin‐modified DNA

Age- and calorie restriction-related changes in rat brain mitochondrial DNA and TFAM binding

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