NDLI: UV endonuclease of Micrococcus luteus, a cyclobutane pyrimidine dimer-DNA glycosylase/abasic lyase: cloning and characterization of the gene.

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UV endonuclease of Micrococcus luteus, a cyclobutane pyrimidine dimer-DNA glycosylase/abasic lyase: cloning and characterization of the gene.

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UV endonuclease of Micrococcus luteus, a cyclobutane pyrimidine dimer-DNA glycosylase/abasic lyase: cloning and characterization of the gene.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Nakayama, H. Shiota, S.
Description	Author Affiliation: Shiota S ( Department of Microbiology, Faculty of Dentistry, Kyushu University, Fukuoka, Japan.);
Abstract	The gene of Micrococcus luteus UV endonuclease (cyclobutane pyrimidine dimer-DNA glycosylase/ abasic lyase) was cloned and characterized. The cloned gene, whose product had a predicted molecular mass of 17,120 Da, was found to be capable of complementing the Escherichia coli uvrA6 mutation in vivo with respect to resistance to acetonemediated molecular photosensitization, a treatment producing exclusively cyclobutane pyrimidine dimers in DNA. It also generated a nicking activity specific for photosensitization-treated DNA by in vitro transcription/translation. When expressed in E. coli cells, the gene produced a protein structurally identical with UV endonuclease and possessing an activity consistent with cyclobutane pyrimidine dimer-DNA glycosylase/abasic lyase with respect to the effect of inhibitors and the site of the DNA backbone scission. Furthermore, the UV endonuclease-deficient mutant DB7 was shown to regain the enzyme through transformation with the cloned gene. The deduced amino acid sequence of the gene product was at best 27% identical with that of endonuclease V of phage T4, an enzyme strikingly similar to UV endonuclease in molecular and catalytic properties. Despite this marginal overall similarity in amino acid sequence, four of the seven amino acid residues reported to be functionally important in the T4 enzyme were found to be conserved in the M. luteus enzyme. We propose that the gene be called uveA.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	2
Volume Number	94
Language	English
Publisher	National Academy of Sciences
Publisher Date	1997-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	DNA Repair Endodeoxyribonucleases Genetics Escherichia Coli Proteins Genes, Bacterial Micrococcus Luteus Multienzyme Complexes N-Glycosyl Hydrolases Adenosine Triphosphatases Bacterial Proteins Cloning, Molecular DNA Damage DNA-Binding Proteins Deoxyribonuclease (Pyrimidine Dimer) Chemistry Genetic Complementation Test Enzymology Molecular Sequence Data Pyrimidine Dimers Sequence Alignment Sequence Homology, Amino Acid Structure-Activity Relationship Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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