Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

---

Query: EC:4.1.99.3 (PRE)
1,923 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The participation of DNA photolyase in dark repair processes has been reported in some heterotrophic organisms. To assess the role of photolyase in dark repair in photoautotrophs, double mutants of Chlamydomonas reinhardtii deficient in dark repair and photoreactivation were constructed and assayed for UV sensitivity in different posttreatment light conditions (with or without subsequent photoreactivation). We found that a functional PHR1 gene enhanced dark survival in the excision deficient (uvs9, uvs12) and in the recombination deficient (uvs10) genetic backgrounds but failed to do so in the strain deficient in a repair pathway other than excision and recombination (uvs13). Therefore we can conclude that photolyase may stimulate dark repair processes in C. reinhardtii also via pathway(s) other than nucleotide excision repair. The fact that some of the double mutants deficient in dark repair and photoreactivation survived better in the light than in the dark supports the idea that additional photorepair might be active and may enhance survival in a specific genetic background.
...
PMID:Interactions between photolyase and dark repair processes in Chlamydomonas reinhardtii. 773 13

Photolyases are DNA repair enzymes that use energy from blue light to repair pyrimidine dimers. We report the isolation of an Arabidopsis thaliana mutant (uvr2-1) that is defective in photorepair of cyclobutylpyrimidine dimers (CPDs). Whereas uvr2-1 is indistinguishable from wild type in the absence of UV light, low UV-B levels inhibit growth and cause leaf necrosis. uvr2-1 is more sensitive to UV-B than wild type when placed under white light after UV-B treatment. In contrast, recovery in darkness or in light lacking photoreactivating blue light results in equal injury in uvr2-1 and wild type. The uvr2-1 mutant is unable to remove CPDs in vivo, and plant extracts lack detectable photolyase activity. This recessive mutation segregates as a single gene located near the top of chromosome 1, and is a structural gene mutation in the type II CPD photolyase PHR1. This mutant provides evidence that CPD photolyase is required for plant survival in the presence of UV-B light.
...
PMID:An Arabidopsis photolyase mutant is hypersensitive to ultraviolet-B radiation. 899 Feb 8

A cDNA from Arabidopsis thaliana similar to microbial photolyase genes, and designated AT-PHH1, was isolated using a photolyase-like cDNA from Sinapsis alba (SA-PHR1) as a probe. Multiple isolations yielded only PHH1 cDNAs, and a few blue-light-receptor CRY1 (HY4) cDNAs (also similar to microbial photolyase genes), suggesting the absence of any other highly similar Arabidopsis genes. The AT-PHH1 and SA-PHR1 cDNA sequences predict 89% identity at the protein level, except for an AT-PHH1 C-terminal extension (111 amino acids), also not seen in microbial photolyases. AT-PHH1 and CRY1 show less similarity (54% p4erein identity), including respective C-terminal extensions that are themselves mostly dissimilar. Analysis of fifteen AT-PHH1 genomic isolates reveals a single gene, with three introns in the coding sequence and one in the 5'-untranslated leader. Full-length AT-PHH1, and both AT-PHH1 and AT-PHH1 delta C-513 (truncated to be approximately the size of microbial photolyase genes) cDNAs, were overexpressed, respectively, in yeast and Escherichia coli mutants hypersensitive to ultraviolet light. The absence of significant effects on resistance suggests either that any putative AT-PHH1 DNA repair activity requires cofactors/chromophores not present in yeast or E. coli, or that AT-PHH1 encodes a blue-light/ultraviolet-A receptor rather than a DNA repair protein.
...
PMID:PHH1, a novel gene from Arabidopsis thaliana that encodes a protein similar to plant blue-light photoreceptors and microbial photolyases. 900 12

The important issue of photoreactivation DNA repair in plants has become even more interesting in recent years because a family of genes that are highly homologous to photoreactivating DNA repair enzymes but that function as blue light photoreceptors has been isolated. Here, we report the isolation of a novel photolyase-like sequence from Arabidopsis designated PHR1 (for photoreactivating enzyme). It shares little sequence similarity with either type I photolyases or the cryptochrome family of blue light photoreceptors. Instead, the PHR1 gene encodes an amino acid sequence with significant homology to the recently characterized type II photolyases identified in a number of prokaryotic and animal systems. PHR1 is a single-copy gene and is not expressed in dark-grown etiolated seedlings: the message is light inducible, which is similar to the expression profile for photoreactivation activity in plants. The PHR1 protein complements a photolyase-deficient mutant of Escherichia coli and thus confers photoreactivation activity. In addition, an Arabidopsis mutant that is entirely lacking in photolyase activity has been found to contain a lesion within this Arabidopsis type II photolyase sequence. We conclude that PHR1 represents a genuine plant photolyase gene and that the plant genes with homology to type I photolyases (the cryptochrome family of blue light photoreceptors) do not contribute to photoreactivation repair, at least in the case of Arabidopsis.
...
PMID:An enzyme similar to animal type II photolyases mediates photoreactivation in Arabidopsis. 906 51

Photolyase is an enzyme that repairs ultraviolet (UV)-damaged DNA by photoreactivation. In higher plants, accumulation of photolyase (PHR1) mRNA is induced by either UV or visible light. In order to know the molecular mechanism by which PHR1 gene expression is induced by light, we have determined the genomic structure and the 5'-flanking sequence of the Arabidopsis PHR1 gene. The PHR1 gene spans approximately 2.5 kb of genomic DNA and consists of 9 exons. In the promoter region of PHR1, there are two pairs of inverted repeats spanning more than sixty base pairs. The promoter also contains DNA motifs similar to the GT-1 box or G-box found in many light-inducible gene promoters. EMSA analysis showed that several proteins in Arabidopsis nuclear extract bound to the G-box-like motifs. These results raise the possibility that the Arabidopsis PHR1 gene is regulated by transcription factors which interact with these motifs.
...
PMID:Molecular cloning of Arabidopsis photolyase gene (PHR1) and characterization of its promoter region. 1052 61

The discovery of enzymatic photoreactivation and of photolyase produced a paradigm shift in the way investigators thought about the cellular consequences of DNA damage and about how these consequences could be avoided. The in vitro photoreactivation system, which utilized crude extracts from Saccharomyces cerevisiae as the source of photolyase, not only provided information about the mechanism of photoreactivation, but also played an important role in the discovery of nucleotide excision repair (NER) and the identification of the pyrimidine dimer as the primary lethal lesion induced by 254 nm radiation. More recently, mechanistic studies using homogenous purified yeast photolyase have yielded insight into how DNA repair enzymes recognize specific structures in DNA, while investigations looking at the repair of lesions in chromatin have begun to elucidate how DNA repair enzymes deal with damage in the context of eukaryotic chromosomes. Additionally, genetic and molecular studies of PHR1, the S. cerevisiae gene encoding the apoenzyme of photolyase, have led to the identification of previously unknown damage-responsive transcriptional regulators.
...
PMID:Enzymatic photoreactivation: 50 years and counting. 1091 63

DNA photolyases catalyze the blue light-dependent repair of UV light-induced damage in DNA. DNA photolyases are specific for either cyclobutane-type pyrimidine dimers or (6-4) photoproducts. PHR2 is a gene that in Chlamydomonas reinhardtii encodes a class II DNA photolyase which catalyzes the photorepair of cyclobutane-type pyrimidine dimers. Based on amino acid sequence analysis of PHR2, which indicates the presence of a chloroplast targeting sequence, PHR2 was predicted to encode the chloroplast photolyase of Chlamydomonas. Using a sensitive gene-specific in vivo repair assay, we found that overexpression of PHR2 in Chlamydomonas results in targeting of the protein to not only the chloroplast, but also to the nucleus. Overexpression of PHR2 photolyase in a photoreactivation-deficient mutant, phr1, results in a largely inactive product. The phr1 mutant was found to be deficient in both photorepair of a chloroplast gene, rbcL, and a nuclear gene, rDNA. These results suggest that PHR2 is the structural gene for the photolyase targeted to both the chloroplast and the nucleus, and that the PHR1 gene product is necessary for full activity of PHR2 protein. To our knowledge, the requirement for a second gene for full activity of a DNA photolyase is novel.
...
PMID:A gene required for the novel activation of a class II DNA photolyase in Chlamydomonas. 1169 35

Rph1, a Cys2-His2 zinc finger protein, binds to an upstream repressing sequence of the photolyase gene PHR1, and represses its transcription in response to DNA damage in Saccharomyces cerevisiae. In this report, we have demonstrated that the phosphorylation of Rph1 protein was increased in response to DNA damage. The DNA damage-induced phosphorylation of Rph1 was missing in most damage checkpoint mutants including rad9, rad17, mec1 and rad53. These results indicate that Rph1 phosphorylation is under the control of the Mec1-Rad53 damage checkpoint pathway. Rph1 phosphorylation required the kinase activity of Rad53 since it was significantly decreased in rad53 checkpoint mutant. Furthermore, loss of other kinases including Dun1, Tel1 and Chk1, which function downstream of Mec1, did not affect the Rph1 phosphorylation. This contrasts with the derepression of Crt1-regulated genes, which requires both Rad53 and Dun1 protein kinases. These results imply that post-translational modification of Rph1 repressor is regulated by a potentially novel damage checkpoint pathway that is distinct from the RAD53-DUN1-CRT1 cascade implicated in the DNA damage-dependent transcription of ribonucleotide reductase genes.
...
PMID:Phosphorylation of Rph1, a damage-responsive repressor of PHR1 in Saccharomyces cerevisiae, is dependent upon Rad53 kinase. 1180 75

An ultraviolet-B (UV-B)-resistant mutant, uvi1 (UV-B insensitive 1), of Arabidopsis was isolated from 1,280 M(1) seeds that had been exposed to ion beam irradiation. The fresh weight of uvi1 under high-UV-B exposure was more than twice that of the wild type. A root-bending assay indicated that root growth was less inhibited by UV-B exposure in uvi1 than in the wild type. When the seedlings were grown under white light, the UV-B dose required for 50% inhibition was about 6 kJ m(-2) for the wild type and 9 kJ m(-2) for uvi1. When the seedlings were irradiated with UV-B in darkness, the dose required for 50% inhibition was about 1.5 kJ m(-2) for the wild type and 4 kJ m(-2) for uvi1. An enzyme-linked immunosorbent assay showed that the reduction in levels of cyclobutane pyrimidine dimers (CPDs) under white light and of (6-4) photoproducts in darkness occurred faster in uvi1 than in the wild type. These results indicate that uvi1 had increased photoreactivation of CPDs and dark repair of (6-4) photoproducts, leading to strong UV-B resistance. Furthermore, the transcript levels of PHR1 (CPD photolyase gene) were much higher in uvi1 than in the wild type both under white light and after UV-B exposure. Placing the plants in the dark before UV-B exposure decreases the early reduction of CPDs in the wild type but not in uvi1. Our results suggest that UVI1 is a negative regulator of two independent DNA repair systems.
...
PMID:An ultraviolet-B-resistant mutant with enhanced DNA repair in Arabidopsis. 1201 38

Survival of irradiated spores from Fusarium oxysporum with ultraviolet radiation (UV) was increased following exposition to visible light, indicating that this phytopathogenic fungus has a mechanism of photoreactivation able to counteract the lethal effects of UV. A genomic sequence containing the complete photolyase gene (phr1) from F. oxysporum was isolated by heterologous hybridisation with the Neurospora crassa photolyase gene. The F. oxysporum phr1 cDNA was isolated and expressed in a photolyase deficient Escherichia coli strain. The complementation of the photoreactivation deficiency of this E. coli mutant by phr1 cDNA demonstrated that the photolyase gene from F. oxysporum encodes a functional protein. The F. oxysporum PHR1 protein has a domain characteristic of photolyases from fungi (Trichoderma harziaium, N. crassa, Magnaporthe grisea, Saccharomyces cerevisiae) to bacteria (E. coli), and clusters in the photolyases phylogenetic tree with fungal photolyases. The F. oxysporum phr1 gene was inducible by visible light. The phr1 expression was also detected in presence of alpha-tomatine, a glycoalkaloid from tomato damaging cell membranes, suggesting that phr1 is induced by this cellular stress.
...
PMID:The photolyase gene from the plant pathogen Fusarium oxysporum f. sp. lycopersici is induced by visible light and alpha-tomatine from tomato plant. 1451 68


<< Previous 1 2 3 Next >>

---