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  • 1
    Electronic Resource
    Electronic Resource
    UV-induced endonuclease III-sensitive sites at the mating type loci in Saccharomyces cerevisiae are repaired by nucleotide excision repair: RAD7 and RAD16 are not required for their removal from HMLα (1996)
    Springer
    Molecular genetics and genomics 250 (1996), S. 505-514 
    Details
    ISSN: 1617-4623
    Keywords: Key words DNA repair ; Nucleotide excision repair ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Ultraviolet irradiation of DNA induces cyclobutane pyrimidine dimers (CPDs), 6-4′-(pyrimidine 2′-one) pyrimidines and pyrimidine hydrates. The dimer is the major photoproduct, and is specifically recognized by endonuclease V of phage T4. Pyrimidine hydrates represent a small fraction of the total photoproducts, and are substrates for endonuclease III of Escherichia coli. We used these enzymes to follow the fate of their substrates in the mating type loci of Saccharomyces cerevisiae. In a RAD strain, CPDs in the transcriptionally active MATα locus are preferentially repaired relative to the inactive HMLα locus, whilst repair of endonuclease III-sensitive sites is not preferential. The rad1, 2, 3 and 4 mutants, which lack factors that are essential for the incision step of nucleotide excision repair (NER), repair neither CPDs nor endonuclease III-sensitive sites, clearly showing that these lesions are repaired by the NER pathway. Previously it had been shown that the products of the RAD7 and RAD16 genes are required for the NER of CPDs from the HMLα locus. We show that, in the same locus, these gene products are not needed for removal of endonuclease III-sensitive sites by the same mechanism. This indicates that the components required for NER differ depending on either the type of lesion encountered or on the specific location of the lesion within the genome.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02174039
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  • 2
    Electronic Resource
    Electronic Resource
    The levels of repair of endonuclease III-sensitive sites, 6-4 photoproducts and cyclobutane pyrimidine dimers differ in a point mutant for RAD14, the Saccharomyces cerevisiae homologue of the human gene defective in XPA patients (1996)
    Springer
    Molecular genetics and genomics 250 (1996), S. 515-522 
    Details
    ISSN: 1617-4623
    Keywords: Key words Saccharomyces cerevisiae ; Nucleotide excision repair ; RAD14 ; XPA homologue
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  In the accompanying paper we demonstrated that endonuclease III-sensitive sites in the MATα and HMLα loci of Saccharomyces cerevisiae are repaired by the Nucleotide Excision Repair (NER) pathway. In the current report we investigated the repair of endonuclease III sites, 6-4 photoproducts and cyclobutane pyrimidine dimers (CPDs) in a rad14-2 point mutant and in a rad14 deletion mutant. The RAD14 gene is the yeast homologue of the human gene that complements the defect in cells from xeroderma pigmentosum (XP) patients belonging to complementation group A. In the point mutant we observed normal repair of endonuclease III sites (i.e. as wild type), but no removal of CPDs at the MATα and HMLα loci. Similar experiments were undertaken using the recently created rad14 deletion mutant. Here, neither endonuclease III sites nor CPDs were repaired in MAT a or HMR a. Thus the point mutant appears to produce a gene product that permits the repair of endonuclease III sites, but prevents the repair of CPDs. Previously it was found that, in the genome overall, repair of 6-4 photoproducts was less impaired than repair of CPDs in the point mutant. The deletion mutant repairs neither CPDs nor 6-4 photoproducts in the genome overall. This finding is consistent with the RAD14 protein being involved in lesion recognition in yeast. A logical interpretation is that the rad14-2 point mutant produces a modified protein that enables the cell to repair endonuclease III sites and 6-4 photoproducts much more efficiently than CPDs. This modified protein may aid studies designed to elucidate the role of the RAD14 protein in lesion recognition.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02174040
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of the rad14-2 Mutant of Saccharomyces cerevisiae: Implications for the Recognition of UV Photoproducts by the Rad14 Protein (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 13 (1997), S. 31-36 
    Details
    ISSN: 0749-503X
    Keywords: RAD14 ; nucleotide excision repair ; Saccharomyces cerevisiae ; damage recognition ; XPA homologue ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The RAD14 gene of Saccharomyces cerevisiae is required for the incision step of the nucleotide excision repair process. The Rad14 protein can bind zinc, possesses a potential zinc finger DNA binding domain and has been shown to bind specifically to damaged DNA. Differences in UV sensitivity exist between a rad14 deletion strain and a putative rad14 point mutant, the point mutant being more resistant to UV than the deletion strain. Here, we confirm that the rad14 deletion strain repairs neither UV-induced cyclobutane pyrimidine dimers (CPDs) nor endonuclease III-sensitive damage sites, whereas the point mutant cannot repair the former but can repair the latter. From this it can be inferred that the point mutant produces an altered protein product allowing recognition of endonuclease III sensitive sites but not CPDs. To investigate this, the rad14 mutant allele was sequenced. It contained two GC-AT transition mutations when compared to the wild-type RAD14 gene sequence. When the rad14 point mutant sequence is translated, alterations within the putative zinc finger binding domain are observed, with one of the cysteine residues of the zinc binding motif being replaced by tyrosine. This suggests that alterations within the zinc finger binding domain of the Rad14 protein cause changes to the damage recognition properties of the protein. The use of the Rad14 protein from the point mutant should assist in experiments investigating the in vitro binding properties of the Rad14 protein to different types of DNA damage. © 1997 by John Wiley & Sons, Ltd.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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