MersV1, Main, Curation, bibRecord, 003647

Purification and characterization of a novel UV lesion-specific DNA glycosylase/AP lyase from Bacillus sphaericus

Identifieur interne : 003647 ( Main/Curation ); précédent : 003646; suivant : 003648

Purification and characterization of a novel UV lesion-specific DNA glycosylase/AP lyase from Bacillus sphaericus

Auteurs : Debra A. Vasquez [États-Unis] ; Simon G. Nyaga [États-Unis] ; R. Stephen Lloyd [États-Unis]

Source :

Mutation Research-DNA Repair [ 0921-8777 ] ; 2000.

RBID : ISTEX:01BD75235FC3754532BE2B8FBF749B63687B6469

English descriptors

Teeft :
- Amino, Bacillus sphaericus, Base excision repair, Biochemical characterization, Biol, Catalytic mechanism, Chem, Covalent, Cyclobutane, Cyclobutane pyrimidine dimer, Cyclobutane pyrimidine dimers, Dewar, Dewar photoproducts, Dimer, Duplex, Edta, Endonuclease, England biolabs, Ethylene glycol, Excision, Glycosylase, Glycosylaserap, Glycosylaserap lyase, Heparin, Heparin sepharose chromatography, Imino, Linear gradient, Lyase, Lyase activity, Micrococcus luteus, Mismatch, Mutation, Mutation research, Nabh, Nicking, Nicking activity, Oligonucleotide, Oligonucleotides, Photoproduct, Photoproducts, Purification, Purification scheme, Pyrimidine, Pyrimidine dimer, Pyrimidine nicking activity, Reaction products, Sepharose, Silver staining, Sodium borohydride, Sphaericus, Thymine, Vasquez.

Abstract

Abstract: The purification and characterization of a pyrimidine dimer-specific glycosylase/AP lyase from Bacillus sphaericus (Bsp-pdg) are reported. Bsp-pdg is highly specific for DNA containing the cis–syn cyclobutane pyrimidine dimer, displaying no detectable activity on oligonucleotides with trans–syn I, trans–syn II, (6–4), or Dewar photoproducts. Like other glycosylase/AP lyases that sequentially cleave the Nglycosyl bond of the 5′ pyrimidine of a cyclobutane pyrimidine dimer, and the phosphodiester backbone, this enzyme appears to utilize a primary amine as the attacking nucleophile. The formation of a covalent enzyme–DNA imino intermediate is evidenced by the ability to trap this protein–DNA complex by reduction with sodium borohydride. Also consistent with its AP lyase activity, Bsp-pdg was shown to incise an AP site-containing oligonucleotide, yielding β- and δ-elimination products. N-terminal amino acid sequence analysis of this 26 kDa protein revealed little amino acid homology to any previously reported protein. This is the first report of a glycosylase/AP lyase enzyme from Bacillus sphaericus that is specific for cis–syn pyrimidine dimers.

Url:

https://api.istex.fr/ark:/67375/6H6-M9SSV5TP-F/fulltext.pdf

DOI: 10.1016/S0921-8777(00)00009-4

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<term>Biochemical characterization</term>
<term>Biol</term>
<term>Catalytic mechanism</term>
<term>Chem</term>
<term>Covalent</term>
<term>Cyclobutane</term>
<term>Cyclobutane pyrimidine dimer</term>
<term>Cyclobutane pyrimidine dimers</term>
<term>Dewar</term>
<term>Dewar photoproducts</term>
<term>Dimer</term>
<term>Duplex</term>
<term>Edta</term>
<term>Endonuclease</term>
<term>England biolabs</term>
<term>Ethylene glycol</term>
<term>Excision</term>
<term>Glycosylase</term>
<term>Glycosylaserap</term>
<term>Glycosylaserap lyase</term>
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<term>Heparin sepharose chromatography</term>
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<term>Mutation</term>
<term>Mutation research</term>
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<term>Nicking</term>
<term>Nicking activity</term>
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<term>Oligonucleotides</term>
<term>Photoproduct</term>
<term>Photoproducts</term>
<term>Purification</term>
<term>Purification scheme</term>
<term>Pyrimidine</term>
<term>Pyrimidine dimer</term>
<term>Pyrimidine nicking activity</term>
<term>Reaction products</term>
<term>Sepharose</term>
<term>Silver staining</term>
<term>Sodium borohydride</term>
<term>Sphaericus</term>
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<term>Vasquez</term>
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<front><div type="abstract" xml:lang="en">Abstract: The purification and characterization of a pyrimidine dimer-specific glycosylase/AP lyase from Bacillus sphaericus (Bsp-pdg) are reported. Bsp-pdg is highly specific for DNA containing the cis–syn cyclobutane pyrimidine dimer, displaying no detectable activity on oligonucleotides with trans–syn I, trans–syn II, (6–4), or Dewar photoproducts. Like other glycosylase/AP lyases that sequentially cleave the Nglycosyl bond of the 5′ pyrimidine of a cyclobutane pyrimidine dimer, and the phosphodiester backbone, this enzyme appears to utilize a primary amine as the attacking nucleophile. The formation of a covalent enzyme–DNA imino intermediate is evidenced by the ability to trap this protein–DNA complex by reduction with sodium borohydride. Also consistent with its AP lyase activity, Bsp-pdg was shown to incise an AP site-containing oligonucleotide, yielding β- and δ-elimination products. N-terminal amino acid sequence analysis of this 26 kDa protein revealed little amino acid homology to any previously reported protein. This is the first report of a glycosylase/AP lyase enzyme from Bacillus sphaericus that is specific for cis–syn pyrimidine dimers.</div>
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Purification and characterization of a novel UV lesion-specific DNA glycosylase/AP lyase from Bacillus sphaericus

Purification and characterization of a novel UV lesion-specific DNA glycosylase/AP lyase from Bacillus sphaericus

Source :

English descriptors

Abstract

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Links to Exploration step

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