Light-illumination effects on the cellular concentration of photolyase molecules in yeast

Fukui, Atsushi; Laskowski, Wolfgang

doi:10.1007/bf01210932

Cited by 12 publications

(8 citation statements)

References 18 publications

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“…Moreover, our estimate for the abundance of the yeast binding factor agrees with previous estimates for yeast photolyase (11). However, it is possible that either of the two protein-DNA complexes observed in the gel assay might contain other proteins in tight association with photolyase.…”

Section: Resultssupporting

confidence: 81%

Evidence that xeroderma pigmentosum cells from complementation group E are deficient in a homolog of yeast photolyase.

Patterson

Chu

1989

Mol. Cell. Biol.

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Xeroderma pigmentosum (XP) patients are deficient in the excision repair of damaged DNA. Recognition of the DNA lesion appears to involve a nuclear factor that is defective in complementation group E (XPE binding factor). We have now identified a factor in the yeast Saccharomyces cerevisiae that shares many properties with XPE binding factor, including cellular location, abundance, magnesium dependence, and relative affinities for multiple forms of damaged DNA. Yeast binding activity is dependent on photolyase, which catalyzes the photoreactivation of pyrimidine dimers. These results suggest that yeast photolyase may also function as an auxiliary protein in excision repair. Furthermore, XPE binding factor appears to be the human homolog of yeast photolyase.

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Section: Resultssupporting

confidence: 81%

Evidence that xeroderma pigmentosum cells from complementation group E are deficient in a homolog of yeast photolyase.

Patterson

Chu

1989

Mol. Cell. Biol.

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“…Another possibility is that the different rates of photoreactivation at, a,, a, may be attributed to the presence of three different types of DNA photolyase molecules, as already suggested for XS774-6A cells by Fukui and Laskowski (1985). Our results indicate that all three photolyase types are active at 23°C and that two types are active at 37"C, whereas Fukui and Laskowski (1985) have suggested that only one type is normally active. Our inferences about the number of types of photolyase molecule are drawn, however, from the presence of different photoreactivation rates, rather than from changes in the inferred numbers of photolyase molecules per cell under different treatments.…”

Section: Discussionsupporting

confidence: 69%

“…From this the number of P R E molecules per cell is determined. From changes brought about in the cellular concentration of PRE molecules by growth of the cells at different temperatures, with or without illumination during growth, by holding cells in buffer with or without illumination, and with or without cycloheximide present, Fukui and Laskowski (1985) concluded that yeast cells may contain three classes of PRE molecules. One class (PRE,) is normally active.…”

Section: Introductionmentioning

confidence: 99%

Evidence From Photoreactivation Kinetics for Multiple Dna Photolyases in Yeast

Johnson¹,

Haynes²

1986

Photochem & Photobiology

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Abstract— We have analyzed the kinetics of photoreactivation of ultraviolet‐light‐irradiated cells of two strains of the yeast Saccharomyces cerevisiae. The analysis yields plots of h(t), the number of photorepairable lethal hits remaining in the cell as a function of the time t of exposure to a continuous source of photoreactivating light. In the case of one of the strains studied, an excision‐deficient haploid strain, it is found that the time‐dependence of h(t) is given by the sum of three decreasing exponential functions of t for stationary phase cultures grown at 23 or 30°C. When the culture is grown at 37°C. the fastest component is absent and the intermediate component is reduced in importance relative to the remaining slow component. In the case of the other strain, a diploid of wild‐type radiation resistance, h(t) is found to contain just one decreasing exponential for cultures grown at 23, 30, and 37°C. The rate constant depends on the growth temperature of the cells, decreasing with increasing temperature. The results are interpreted as evidence for multiple DNA photolyases in the sensitive haploid strain.

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“…The transcription of the gene for CPD photolyase is strongly regulated by environmental factors in many species (20)(21)(22)(23). The gene for photolyase in fish cells is induced by fluorescent light and by hydrogen peroxide (15,24).…”

Section: Discussionmentioning

confidence: 99%

Induction of Cyclobutane Pyrimidine Dimer Photolyase in Cultured Fish Cells by UVA and Blue Light

Mikami

Uchida

Shima

1996

Photochem & Photobiology

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The cyclobutane pyrimidine dimer (CPD) photolyase in fish cells is known to be regulated by environmental factors, such as light, hydrogen peroxide and growth inhibition. The induction of CPD photolyase by light in cultured goldfish cells was dependent on the wavelength of the light, and UVA and blue light had high inductive activity. The spectrum for CPD photolyase activity was different from that for the induction. Treatment with blue or yellow light for a short time, which did not induce any CPD photolyase, induced high CPD photolyase activity in the presence of the photosensitizers, TPPS (monosulfonated meso-tetraphenyl porphine) and ALPS (aluminum phthalocyanine tetrasulfonate), respectively. These results suggest that the induction of CPD photolyase might be triggered by active oxygen produced by light and cellular photosensitizers. We also found that immediately after treatment with UVA, blue light or a photosensitizer in combination with light, cellular attachment to the substratum was enhanced, as was the CPD photolyase activity. Pretreatment with a flavonoid, quercetin, inhibited both photoinduction of CPD photolyase and enhancement of cellular attachment. Vitamin E inhibited only photoinduction of CPD photolyase activity.Treatment with H7, a strong inhibitor for protein kinase C, after light treatment inhibited photoinduction of CPD photolyase activity, but an analogue of H7, Ha1004, which is a weak inhibitor of protein kinase C, did not have such an effect.

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Light-illumination effects on the cellular concentration of photolyase molecules in yeast

Cited by 12 publications

References 18 publications

Evidence that xeroderma pigmentosum cells from complementation group E are deficient in a homolog of yeast photolyase.

Evidence that xeroderma pigmentosum cells from complementation group E are deficient in a homolog of yeast photolyase.

Evidence From Photoreactivation Kinetics for Multiple Dna Photolyases in Yeast

Induction of Cyclobutane Pyrimidine Dimer Photolyase in Cultured Fish Cells by UVA and Blue Light

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