Unknown

Dataset Information

0

Structural basis for the lack of opposite base specificity of Clostridium acetobutylicum 8-oxoguanine DNA glycosylase.


ABSTRACT: 7,8-Dihydro-8-oxoguanine (8-oxoG) is the major oxidative product of guanine and the most prevalent base lesion observed in DNA molecules. Because 8-oxoG has the capability to form a Hoogsteen pair with adenine (8-oxoG:A) in addition to a normal Watson-Crick pair with cytosine (8-oxoG:C), this lesion can lead to a G:C-->T:A transversion after replication. However, 8-oxoG is recognized and excised by the 8-oxoguanine DNA glycosylase (Ogg) of the base excision repair pathway. Members of the Ogg1 family usually display a strong preference for a C opposite the lesion. In contrast, the atypical Ogg1 from Clostridium actetobutylicum (CacOgg) can excise 8-oxoG when paired with either one of the four bases, albeit with a preference for C and A. Here we describe the first high-resolution crystal structures of CacOgg in complex with duplex DNA containing the 8-oxoG lesion paired to cytosine and to adenine. A structural comparison with human OGG1 provides a rationale for the lack of opposite base specificity displayed by the bacterial Ogg.

SUBMITTER: Faucher F 

PROVIDER: S-EPMC2779579 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structural basis for the lack of opposite base specificity of Clostridium acetobutylicum 8-oxoguanine DNA glycosylase.

Faucher Frédérick F   Wallace Susan S SS   Doublié Sylvie S  

DNA repair 20090910 11


7,8-Dihydro-8-oxoguanine (8-oxoG) is the major oxidative product of guanine and the most prevalent base lesion observed in DNA molecules. Because 8-oxoG has the capability to form a Hoogsteen pair with adenine (8-oxoG:A) in addition to a normal Watson-Crick pair with cytosine (8-oxoG:C), this lesion can lead to a G:C-->T:A transversion after replication. However, 8-oxoG is recognized and excised by the 8-oxoguanine DNA glycosylase (Ogg) of the base excision repair pathway. Members of the Ogg1 fa  ...[more]

Similar Datasets

| S-EPMC2574669 | biostudies-literature
| S-EPMC2678946 | biostudies-literature
| S-EPMC8241999 | biostudies-literature
| S-EPMC4364697 | biostudies-literature
| S-EPMC3113562 | biostudies-literature
| S-EPMC3797267 | biostudies-literature
| S-EPMC4976190 | biostudies-literature
| S-EPMC4207560 | biostudies-literature
| S-EPMC2746928 | biostudies-literature
| S-EPMC147981 | biostudies-other