pubmed-article:8332499 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8332499 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
pubmed-article:8332499 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
pubmed-article:8332499 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:8332499 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
pubmed-article:8332499 | lifeskim:mentions | umls-concept:C1883559 | lld:lifeskim |
pubmed-article:8332499 | lifeskim:mentions | umls-concept:C2263803 | lld:lifeskim |
pubmed-article:8332499 | lifeskim:mentions | umls-concept:C0332256 | lld:lifeskim |
pubmed-article:8332499 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
pubmed-article:8332499 | lifeskim:mentions | umls-concept:C0684192 | lld:lifeskim |
pubmed-article:8332499 | lifeskim:mentions | umls-concept:C0167195 | lld:lifeskim |
pubmed-article:8332499 | pubmed:issue | 12 | lld:pubmed |
pubmed-article:8332499 | pubmed:dateCreated | 1993-8-17 | lld:pubmed |
pubmed-article:8332499 | pubmed:abstractText | A 34-mer oligonucleotide containing a single 7,8-dihydro-8-oxoguanine (8-OxoG) residue was used to study the enzymatic and DNA binding properties of the Fpg protein from E. coli. The highest rates of incision of the 8-OxoG containing strand by the Fpg protein were observed for duplexes where 8-OxoG was opposite C (*G/C) or T (*G/T). In contrast, the rates of incision of duplexes containing 8-OxoG opposite G (*G/G) and A (*G/A) were 5-fold and 200-fold slower. Gel retardation studies showed that the Fpg protein had a strong affinity for duplexes where the 8-OxoG was opposite pyrimidines and less affinity for duplexes where the 8-OxoG was opposite purines. KDapp values were 0.6 nM (*G/C), 1.0 nM (*G/T), 6.0 nM (*G/G) and 16.0 nM (*G/A). The Fpg protein also binds to unmodified (G/C) duplex and a KDapp of 90 nM was measured. The cleavage and binding of the (*G/C) duplex were also studied using bacterial crude lysates. Wild type E. coli crude extract incised the 8-OxoG containing strand and formed a specific retardation complex with the (*G/C) duplex. These two reactions were mediated by the Fpg protein, since they were not observed with a crude extract from a bacterial strain whose fpg gene was inactivated. Furthermore, we have studied the properties of 6 mutant Fpg proteins with Cys-->Gly mutations. The results showed that the 2 Fpg proteins with Cys-->Gly mutations outside the zinc finger sequence cleaved the 8-OxoG containing strand, formed complexes with the (*G/C) duplex and suppressed the mutator phenotype of the fpg-1 mutant. In contrast, the 4 Fpg proteins with Cys-->Gly mutations within the zinc finger motif neither cleave nor bind the (*G/C) duplex, nor do these proteins suppress the fpg-1 mutator phenotype. | lld:pubmed |
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pubmed-article:8332499 | pubmed:language | eng | lld:pubmed |
pubmed-article:8332499 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8332499 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8332499 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:8332499 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8332499 | pubmed:month | Jun | lld:pubmed |
pubmed-article:8332499 | pubmed:issn | 0305-1048 | lld:pubmed |
pubmed-article:8332499 | pubmed:author | pubmed-author:GeigerAA | lld:pubmed |
pubmed-article:8332499 | pubmed:author | pubmed-author:NehlsPP | lld:pubmed |
pubmed-article:8332499 | pubmed:author | pubmed-author:LavalJJ | lld:pubmed |
pubmed-article:8332499 | pubmed:author | pubmed-author:BoiteuxSS | lld:pubmed |
pubmed-article:8332499 | pubmed:author | pubmed-author:ZelwerCC | lld:pubmed |
pubmed-article:8332499 | pubmed:author | pubmed-author:SeligerHH | lld:pubmed |
pubmed-article:8332499 | pubmed:author | pubmed-author:CastaingBB | lld:pubmed |
pubmed-article:8332499 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8332499 | pubmed:day | 25 | lld:pubmed |
pubmed-article:8332499 | pubmed:volume | 21 | lld:pubmed |
pubmed-article:8332499 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8332499 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8332499 | pubmed:pagination | 2899-905 | lld:pubmed |
pubmed-article:8332499 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:8332499 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8332499 | pubmed:articleTitle | Cleavage and binding of a DNA fragment containing a single 8-oxoguanine by wild type and mutant FPG proteins. | lld:pubmed |