Functional Identification of an 8-Oxoguanine Specific Endonuclease from Thermotoga maritima

Im, Eui; Hong, Chang Hyung; Back, Jinwook; Han, Ye; Chung, Ji Hyung

doi:10.5483/bmbrep.2005.38.6.676

Cited by 8 publications

(14 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…17 Ogg2 glycosylases comprise two domains separated by the HhH motif and, in contrast to Ogg1, are less variable in size (± 207 amino acids). 18; 19; 20; 21 Ogg2 enzymes also display a less stringent opposite base specificity than Ogg1. 19; 21 Finally, members of the third family, AGOG, share a similar two-domain architecture with Ogg2.…”

Section: Introductionmentioning

confidence: 99%

The C-terminal Lysine of Ogg2 DNA Glycosylases is a Major Molecular Determinant for Guanine/8-Oxoguanine Distinction

Faucher

Wallace

Doublié

2010

Journal of Molecular Biology

View full text Add to dashboard Cite

7,8-dihydro-8-oxoguanine (8-oxoG) is a major oxidative lesion found in DNA. The 8-oxoguanine DNA glycosylases (Ogg) responsible for the removal of 8-oxoG are divided into three families: Ogg1, Ogg2 and AGOG. Since Ogg2 members are devoid of the recognition loop used by Ogg1 to discriminate between 8-oxoG and guanine it was unclear until recently how Ogg2 enzymes recognize the oxidized base. We present here the first crystallographic structure of an Ogg2 member, Methanocaldococcus janischii Ogg, in complex with a DNA duplex containing the 8-oxoG lesion. This structure highlights the critical role of the C-terminal lysine, strictly conserved in Ogg2, in the recognition of 8-oxoG. The structure also reveals that, similarly to Ogg1 glycosylases, Ogg2 undergoes a conformational change upon DNA binding. Furthermore, this work provides a structural rationale for the lack of opposite base specificity in this family of enzymes.

show abstract

Section: Introductionmentioning

confidence: 99%

The C-terminal Lysine of Ogg2 DNA Glycosylases is a Major Molecular Determinant for Guanine/8-Oxoguanine Distinction

Faucher

Wallace

Doublié

2010

Journal of Molecular Biology

View full text Add to dashboard Cite

show abstract

“…Members of this family, mostly from archaea, show a reduced specificity for the base opposite the lesion compared to hOGG1 2122; 23 A third class of Ogg, AGOG (archaeal GO glycosylase),24; 25 was described and the crystal structure of one of its representatives, Pa-AGOG from Pyrobaculum aerophilum , was reported recently 26. Enzymes of this class efficiently remove 8-oxoG from single- and double-stranded DNA substrates and demonstrate no opposite base specificity.…”

Section: Introductionmentioning

confidence: 99%

Structural Characterization of Clostridium acetobutylicum 8-Oxoguanine DNA Glycosylase in Its Apo Form and in Complex with 8-Oxodeoxyguanosine

Faucher

Robey-Bond

Wallace

et al. 2009

Journal of Molecular Biology

View full text Add to dashboard Cite

SummaryDNA is subject to a multitude of oxidative damages generated by oxidizing agents from metabolism, from exogenous sources and by ionizing radiation. Guanine is particularly vulnerable to oxidation and the most common oxidative product, 8-oxoguanine (8-oxoG), is the most prevalent lesion observed in DNA molecules. 8-oxoG can form a normal Watson-Crick pair with cytosine (8-oxoG:C), but it can also form a stable Hoogsteen pair with adenine (8-oxoG:A) leading to a G:C →T:A transversion after replication. Fortunately, 8-oxoG is recognized and excised by either of two DNA glycosylases of the base excision repair (BER) pathway, formamidopyrimidine-DNA glycosylase (Fpg) and 8-oxoguanine DNA glycosylase (Ogg). While Clostridium acetobutylicum Ogg DNA glycosylase can specifically recognize and remove 8-oxoG it displays little preference for the base opposite the lesion, which is unusual for a member of the Ogg1 family. This paper describes the crystal structures of CacOgg in its apo-form and in complex with 8-oxo-2'-deoxyguanosine. A structural comparison between the apo and liganded forms of the enzyme reveals a structural reorganization of the C-terminal domain upon binding of 8-oxoG similar to that reported for hOGG1. A structural comparison of CacOgg with hOGG1 in complex with 8-oxoG containing DNA provides a structural rationale for the lack of opposite base specificity displayed by CacOgg.

show abstract

“…Characterization of the gene product revealed this protein to be an 8-oxoguanine DNA glycosylase (Gogos and Clarke, 1999). Similar Oggs were subsequently identified in archaea such as Sulfolobus solfataricus (Brock, et al, 1972, She, et al, 2001) and Archeoglobus fulgidus (Chung, et al, 2001) and eubacteria such as Thermotoga maritima (Im, et al, 2005, Nelson, et al, 1999). …”

Section: Introductionmentioning

confidence: 67%

“…A) Sequence alignment of the C-terminal region of MjaOgg, SsoOgg, AfuOgg ( Archaeoglobus fulgidus ) (Chung, et al, 2001) and TmaOgg ( Thermotoga maritima ) (Im, et al, 2005), showing the conserved “stacking” tryptophan and the C-terminal lysine of Ogg2 (in red) B) Ribbon diagram showing a superposition of the C-terminal loop of MjaOgg (red), SsoOgg (pale yellow) and the αA-βB loop of hOGG1 (gray) (PDB ID code: 1EBM (Bruner, et al, 2000)). The superposition indicates that Trp198 of Ogg2 may be involved in a similar stacking interaction with 8-oxoG as Phe319 in hOGG1.…”

Section: Figures and Tablementioning

confidence: 99%

“…The Ogg1 family encompasses the largest number of members including human OGG1 (hOGG1) (Aburatani, et al, 1997, Arai, et al, 1997, Bjørås, et al, 1997, Nagashima, et al, 1997, Radicella, et al, 1997, Roldan-Arjona, et al, 1997, Rosenquist, et al, 1997) and bacterial Oggs such as Clostridium acetobutylicum Ogg (CacOgg) (Robey-Bond, et al, 2008). The Ogg2 family comprises archaeal species such as M. jannaschii Ogg (MjaOgg) (Gogos and Clarke, 1999), S. solfataricus Ogg (SsoOgg), A. fulgidus Ogg (AfuOgg) (Chung, et al, 2001) and eubacteria, e.g., T. maritima Ogg (Tm 1821) (Im, et al, 2005). Ogg2 enzymes lack the A domain of Ogg1 family members, share a very low sequence identity with hOGG1 (13–19%) and display a reduced specificity for the base opposite the lesion.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Crystal Structures of Two Archaeal 8-Oxoguanine DNA Glycosylases Provide Structural Insight into Guanine/8-Oxoguanine Distinction

et al. 2009

View full text Add to dashboard Cite

Summary Among the four DNA bases, guanine is particularly vulnerable to oxidative damage and the most common oxidative product, 7,8 dihydro-8-oxoguanine (8-oxoG), is the most prevalent lesion observed in DNA molecules. Fortunately, 8-oxoG is recognized and excised by the 8-oxoguanine DNA glycosylase (Ogg) of the base excision repair pathway. Ogg enzymes are divided into three separate families, namely Ogg1, Ogg2, and AGOG. To date, structures of members of both Ogg1 and AGOG families are known but no structural information is available for members of Ogg2. Here we describe the first crystal structures of two archaeal Ogg2: Methanocaldococcus janischii Ogg (MjaOgg) and Sulfolobus solfataricus Ogg (SsoOgg). A structural comparison with OGG1 and AGOG suggested that the C-terminal lysine of Ogg2 may play a key role in discriminating between guanine and 8-oxoG. This prediction was substantiated by measuring the glycosylase/lyase activity of a C-terminal deletion mutant of MjaOgg.

show abstract

Functional Identification of an 8-Oxoguanine Specific Endonuclease from Thermotoga maritima

Cited by 8 publications

References 24 publications

The C-terminal Lysine of Ogg2 DNA Glycosylases is a Major Molecular Determinant for Guanine/8-Oxoguanine Distinction

The C-terminal Lysine of Ogg2 DNA Glycosylases is a Major Molecular Determinant for Guanine/8-Oxoguanine Distinction

Structural Characterization of Clostridium acetobutylicum 8-Oxoguanine DNA Glycosylase in Its Apo Form and in Complex with 8-Oxodeoxyguanosine

Crystal Structures of Two Archaeal 8-Oxoguanine DNA Glycosylases Provide Structural Insight into Guanine/8-Oxoguanine Distinction

Contact Info

Product

Resources

About