Partial complementation of the UV sensitivity of Deinococcus radiodurans excision repair mutants by the cloned denV gene of bacteriophage T4
Autor: | Pablo D. Gutman, Hanlong Yao, Kenneth W. Minton |
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Rok vydání: | 1991 |
Předmět: |
DNA Repair
Genes Viral Ultraviolet Rays Mutant Gene Expression Gram-Positive Bacteria Toxicology Chromosomes DNA Glycosylases Endonuclease Transformation Genetic Genetics Cloning Molecular N-Glycosyl Hydrolases Molecular Biology biology Genetic Complementation Test Mutagenesis Genetic transfer Deinococcus radiodurans biology.organism_classification Molecular biology Complementation DNA glycosylase Mutation biology.protein T-Phages Nucleotide excision repair |
Zdroj: | Mutation Research/DNA Repair. 254:207-215 |
ISSN: | 0921-8777 |
DOI: | 10.1016/0921-8777(91)90058-w |
Popis: | Deinococcus radiodurans has 2 endonucleases that incise UV-irradiated DNA. UV endonuclease-alpha and UV endonuclease-beta, that are believed to functionally overlap. Both endonucleases must be mutationally inactivated to yield an incisionless, markedly UV-sensitive phenotype. denV, the bacteriophage T4 gene encoding pyrimidine dimer-DNA glycosylase (PD-glycosylase), was introduced and expressed via duplication insertion in D. radiodurans wild-type, and single and double UV endonuclease mutants. The strain deficient in UV endonuclease-alpha has wild-type UV resistance, and the expression of PD-glycosylase exerted no survival effect on this strain or wild-type. Expression of denV increased survival of both the markedly UV-sensitive double mutant and the moderately UV-sensitive strain deficient only in UV endonuclease-beta. In endonuclease-beta-deficient cells phenotypic complementation by denV was almost complete in restoring UV resistance to wild-type levels. These results suggest that UV endonuclease-alpha (which is present in the endonuclease-beta-deficient cells) does not recognize one or more types of cyclobutane dimer incised by the PD-glycosylase or UV endonuclease-beta. |
Databáze: | OpenAIRE |
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