Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1993-8-17
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.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-1378443, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-1392536, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-1408745, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-1417833, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-1649454, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-1650738, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-1710617, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-1730583, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-1731864, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-1741272, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-1991121, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-1992344, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-2052552, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-2155406, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-2206282, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-2223758, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-2233814, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-2303467, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-2430946, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-2453510, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-2501784, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-2651883, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-2664776, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-2676225, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-2679549, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-2914925, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-2982160, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-3319582, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-3574469, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-3769133, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-386277, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-3894348, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-6275366, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-6371006, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-6382026, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-6382167, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-6383204, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-6462910, http://linkedlifedata.com/resource/pubmed/commentcorrection/8332499-8437588
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0305-1048
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2899-905
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Cleavage and binding of a DNA fragment containing a single 8-oxoguanine by wild type and mutant FPG proteins.
More...