Base Excision DNA Repair
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Base Excision DNA Repair
Base excision repair (BER) is a cellular mechanism, studied in the fields of biochemistry and genetics, that repairs damaged DNA throughout the cell cycle. It is responsible primarily for removing small, non-helix-distorting base lesions from the genome. The related nucleotide excision repair pathway repairs bulky helix-distorting lesions. BER is important for removing damaged bases that could otherwise cause mutations by mispairing or lead to breaks in DNA during replication. BER is initiated by DNA glycosylases, which recognize and remove specific damaged or inappropriate bases, forming AP sites. These are then cleaved by an AP endonuclease. The resulting single-strand break can then be processed by either short-patch (where a single nucleotide is replaced) or long-patch BER (where 2–10 new nucleotides are synthesized). Lesions processed by BER Single bases in DNA can be chemically damaged by a variety of mechanisms, the most common ones being deamination, oxidation, ...
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BER Basic Pathway
BER may refer to: Science and technology Biology and medicine * Basal electrical rhythm, spontaneous rhythmic slow action potentials that some smooth muscles of the GI tract display * Base excision repair, a DNA repair pathway * Benign early repolarization, a heart arrhythmia * Blossom end rot, a plant disorder Computing * Basic Encoding Rules, a set of rules for encoding data * Bit error rate, the ratio between the number of incorrect bits transmitted to the total Places * Bermuda (IOC and UNDP code), a British overseas territory * Bohai Economic Rim, the economic region surrounding Tianjin, China Transport * Air Berlin (ICAO code: BER), a defunct German airline * Berlin Brandenburg Airport (IATA code: BER), Germany * Berlin station (Connecticut) (Amtrak code: BER), United States Other uses * Beyond economic repair, a rating of a damaged item * Block Exemption Regulation, published by the European Commission regarding European Union competition law * Building the Education Revol ...
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Thymidine
Thymidine (nucleoside#List of nucleosides and corresponding nucleobases, symbol dT or dThd), also known as deoxythymidine, deoxyribosylthymine, or thymine deoxyriboside, is a pyrimidine nucleoside, deoxynucleoside. Deoxythymidine is the DNA nucleoside T, which pairs with deoxyadenosine (A) in double-stranded DNA. In cell biology it is used to cell synchronization, synchronize the cells in G1/early S phase. The prefix deoxy- is often left out since there are no precursors of thymine nucleotides involved in RNA synthesis. Before the boom in thymidine use caused by the need for thymidine in the production of the antiretroviral drug Zidovudine, azidothymidine (AZT), much of the world's thymidine production came from herring sperm. Thymidine occurs almost exclusively in DNA but it also occurs in the T arm, T-loop of tRNA. Structure and properties In its composition, deoxythymidine is a nucleoside composed of deoxyribose (a pentose sugar) joined to the pyrimidine base thymine. De ...
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Uracil-DNA Glycosylase
Uracil-DNA glycosylase (also known as UNG or UDG) is an enzyme. Its most important function is to prevent mutagenesis by eliminating uracil from DNA molecules by cleaving the N-glycosidic bond and initiating the base-excision repair (BER) pathway. Function The human gene encodes one of several uracil-DNA glycosylases. Alternative promoter usage and splicing of this gene leads to two different isoforms: the mitochondrial UNG1 and the nuclear UNG2. One important function of uracil-DNA glycosylases is to prevent mutagenesis by eliminating uracil from DNA molecules by cleaving the N-glycosidic bond and initiating the base-excision repair (BER) pathway. Uracil bases occur from cytosine deamination or misincorporation of dUMP residues. After a mutation occurs, the mutagenic threat of uracil propagates through any subsequent DNA replication steps. Once unzipped, mismatched guanine and uracil pairs are separated, and DNA polymerase inserts complementary bases to form a guanine-cytosine ...
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DNA-3-methyladenine Glycosylase
DNA-3-methyladenine glycosylase also known as 3-alkyladenine DNA glycosylase (AAG) or N-methylpurine DNA glycosylase (MPG) is an enzyme that in humans is encoded by the ''MPG'' gene. Alkyladenine DNA glycosylase is a specific type of DNA glycosylase. This subfamily of monofunctional glycosylases is involved in the recognition of a variety of base lesions, including alkylated and deaminated purines, and initiating their repair via the base excision repair pathway. To date, the human AAG (hAAG) is the only glycosylase identified that excises alkylation-damaged purine bases in human cells. Function DNA bases are subject to a large number of anomalies: spontaneous alkylation or oxidative deamination. It is estimated that 104 mutations appear in a typical human cell per day. Albeit it seems to be an insignificant amount considering the extension of the DNA (1010 nucleotides), these mutations lead to changes in the structure and coding potential of the DNA, affecting processes of DN ...
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Oxoguanine Glycosylase
8-Oxoguanine glycosylase, also known as OGG1, is a DNA glycosylase enzyme that, in humans, is encoded by the ''OGG1'' gene. It is involved in base excision repair. It is found in bacterial, archaeal and eukaryotic species. Function OGG1 is the primary enzyme responsible for the excision of 8-oxoguanine (8-oxoG), a mutagenic base byproduct that occurs as a result of exposure to reactive oxygen species (ROS). OGG1 is a bifunctional glycosylase, as it is able to both cleave the glycosidic bond of the mutagenic lesion and cause a strand break in the DNA backbone. Alternative splicing of the C-terminal region of this gene classifies splice variants into two major groups, type 1 and type 2, depending on the last exon of the sequence. Type 1 alternative splice variants end with exon 7 and type 2 end with exon 8. One set of spliced forms are designated 1a, 1b, 2a to 2e. All variants have the N-terminal region in common. Many alternative splice variants for this gene have been ...
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AP Lyase
The enzyme DNA-(apurinic or apyrimidinic site) lyase, also referred to as DNA-(apurinic or apyrimidinic site) 5'-phosphomonoester-lyase (systematic name) or DNA AP lyase (EC 4.2.99.18) catalyzes the cleavage of the C-O-P bond 3' from the apurinic or apyrimidinic site in DNA via β-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. In the 1970s, this class of enzyme was found to repair at apurinic or apyrimidinic DNA sites in ''E. coli'' and in mammalian cells. The major active enzyme of this class in bacteria, and specifically, ''E. coli'' is endonuclease type III. This enzyme is part of a family of lyases that cleave carbon-oxygen bonds. Other names for DNA AP lyase include: AP lyase; AP endonuclease class I; endodeoxyribonuclease (apurinic or apyrimidinic); deoxyribonuclease (apurinic or apyrimidinic); E. coli endonuclease III; phage-T4 UV endonuclease; Micrococcus luteus UV endonuclease; AP site-DNA 5'-phosphomonoester-lyas ...
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DNA Base Flipping
DNA base flipping, or nucleotide flipping, is a mechanism in which a single nucleotide base, or nucleobase, is rotated outside the nucleic acid double helix. This occurs when a nucleic acid-processing enzyme needs access to the base to perform work on it, such as its excision for replacement with another base during Base excision repair, DNA repair. It was first observed in 1994 using X-ray crystallography in a methyltransferase enzyme catalyzing methylation of a cytosine base in DNA. Since then, it has been shown to be used by different enzymes in many biological processes such as DNA methylation, various DNA repair mechanisms, and DNA replication. It can also occur in RNA double helices or in the DNA:RNA intermediates formed during RNA transcription. DNA base flipping occurs by breaking the Hydrogen bonds#Hydrogen bonds in DNA and proteins, hydrogen bonds between the bases and unstacking the base from its neighbors. This could occur through an active process, where an enzyme bi ...
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