Ogg1 Glycosylase
Ogg1 Glycosylase - Related Videos
14:27
Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
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Cited by 26 •
2013
Time courses for the glycosylase activity of 8-oxoguanine DNA glycosylase are biphasic exhibiting a burst of product formation and a linear steady-state phase. Utilizing quench-flow techniques, the burst and the steady-state rates can be measured, which correspond to excision of 8-oxoguanine and release of the glycosylase from the product DNA, respectively.
12:19
Uracil-DNA Glycosylase Assay by Matrix-assisted Laser Desorption/Ionization Time-of-flight Mass Spectrometry Analysis
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2022
A non-labeled, non-radio-isotopic method to assay uracil-DNA glycosylase activity was developed using MALDI-TOF mass spectrometry for direct apurinic/apyrimidinic site-containing product analysis. The assay proved to be quite simple, specific, rapid, and easy to use for DNA glycosylase measurement.
01:54
Base Excision Repair
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2020
One of the common DNA damages is the chemical alteration of single bases by alkylation, oxidation, or deamination. The altered bases cause mispairing and strand breakage during replication. This type of damage causes minimal change to the DNA double helix structure and can be repaired by the base excision repair (BER) pathways. BER corrects damaged DNA sequences by removing the damaged base and restoring the original base sequence using the complementary strand as a template. The first step of...
10:44
Laser Microirradiation to Study In Vivo Cellular Responses to Simple and Complex DNA Damage
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Cited by 12 •
2018
The goal of this protocol is to describe how to use laser microirradiation to induce different types of DNA damage, including relatively simple strand breaks and complex damage, to study DNA damage signaling and repair factor assembly at damage sites in vivo.
10:41
Wild-type Blocking PCR Combined with Direct Sequencing as a Highly Sensitive Method for Detection of Low-Frequency Somatic Mutations
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Cited by 5 •
2017
Wild-type blocking PCR followed by direct sequencing offers a highly sensitive method of detection for low frequency somatic mutations in a variety of sample types.
FAQs
Ogg1 glycosylase recognizes 8-oxoguanine in the context of the DNA helix and flips the damaged base out of that structure. This lesion-flipping step positions 8-oxoguanine for enzymatic inspection and subsequent bond cleavage. By acting on a specific oxidative lesion rather than repairing DNA indiscriminately, Ogg1 directs base excision repair toward a defined source of genetic damage.
Base flipping makes the damaged nucleotide accessible to the enzyme’s catalytic machinery. Once 8-oxoguanine is moved from the helix, Ogg1 can act on the N-glycosidic bond that connects the base to its sugar. This structural rearrangement links lesion recognition to chemical initiation of repair and helps explain how a DNA-bound enzyme targets a specific damaged base.
Ogg1 cleaves the N-glycosidic bond between 8-oxoguanine and its sugar in the DNA backbone. That reaction removes the damaged base while leaving an abasic site, meaning a site lacking its normal base. The newly created intermediate is not the final repair product; it must be processed by downstream enzymes in the base excision repair pathway.
Reactive oxygen species can damage DNA, and unrepaired oxidative lesions can contribute to changes in genetic information. Ogg1 helps limit this threat by recognizing and removing 8-oxoguanine, thereby initiating repair before the lesion can contribute to oxidative mutagenesis. Its activity therefore connects lesion removal with genome stability under conditions that generate oxidative damage.
Examining Ogg1 activity provides a way to investigate how cells respond to oxidative DNA damage and how base excision repair is initiated. Researchers can use this enzyme-centered perspective to study lesion recognition, creation of abasic repair intermediates, and the handoff to downstream repair processes. These observations help characterize cellular strategies for maintaining genetic information.
Environmental or metabolic conditions can generate reactive oxygen species, which in turn can damage DNA. Studying Ogg1 in this context helps connect those sources of oxidative stress with the cellular repair response directed at 8-oxoguanine. The enzyme therefore serves as a useful focus for examining how biological systems protect genome stability when oxidative damage increases.
Ogg1 is relevant because oxidative DNA damage and its repair are connected to the preservation of genetic information. Investigating its activity can help researchers examine whether damage recognition and repair responses are functioning in contexts where genomic instability is associated with disease. This work also places individual repair events within broader studies of DNA damage and cellular genome maintenance.