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SMUG1
Single-strand selective monofunctional uracil DNA glycosylase is an enzyme that in humans is encoded by the ''SMUG1'' gene. SMUG1 is a glycosylase that removes uracil from single- and double-stranded DNA in nuclear chromatin, thus contributing to base excision repair. Function SMUG1 is an important Uracil-DNA glycosylase, uracil-DNA glycosylases that process uracil in DNA. SMUG1 function is to remove U or its derivatives from DNA. SMUG1 is able to excise uracil from both single- and doubledstranded DNA. Other DNA glycosylases linked to U removal are Uracil-DNA glycosylase, UNG, Thymine-DNA glycosylase, TDG and MBD4. Uracil-DNA repair is essential to protect against mutations. Current evidence suggests that UNG and SMUG1 are the major enzymes responsible for the repair of the U:G mispairs. Uracil is also introduced into DNA as part of antibody gene diversification and its removal is critical to antibody diversification. UNG is known to be the major player in uracil removal but wh ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
RBPMS
RNA-binding protein with multiple splicing is a protein that in humans is encoded by the ''RBPMS'' gene. Function This gene encodes a member of the RRM family of RNA-binding proteins. The RRM domain is between 80-100 amino acids in length and family members contain one to four copies of the domain. The RRM domain consists of two short stretches of conserved sequence called RNP1 and RNP2, as well as a few highly conserved hydrophobic residues. The protein encoded by this gene has a single, putative RRM domain in its N-terminus. Alternative splicing results in multiple transcript variants encoding different isoforms. It is uniquely expressed in retinal ganglion cells in the mammalian retina, for reasons unknown. Interactions RBPMS has been shown to Protein-protein interaction, interact with SMUG1. References Further reading * * * * {{gene-8-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Base Excision 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, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enzyme
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts are catalytic RNA molecules, called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the react ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Gene
In biology, the word gene (from , ; "... Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''generation'' or ''birth'' or ''gender'') can have several different meanings. The Mendelian gene is a basic unit of heredity and the molecular gene is a sequence of nucleotides in DNA that is transcribed to produce a functional RNA. There are two types of molecular genes: protein-coding genes and noncoding genes. During gene expression, the DNA is first copied into RNA. The RNA can be directly functional or be the intermediate template for a protein that performs a function. The transmission of genes to an organism's offspring is the basis of the inheritance of phenotypic traits. These genes make up different DNA sequences called genotypes. Genotypes along with environmental and developmental factors determine what the phenotypes will be. Most biological traits are under the influence of polygenes (many different genes) as well as ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Gregory L
Gregory may refer to: People and fictional characters * Gregory (given name), including a list of people and fictional characters with the given name * Gregory (surname), a surname Places Australia * Gregory, Queensland, a town in the Shire of Burke **Electoral district of Gregory, Queensland, Australia * Gregory, Western Australia. United States * Gregory, South Dakota * Gregory, Tennessee * Gregory, Texas Outer space * Gregory (lunar crater) *Gregory (crater on Venus) Grimke is a crater on Venus at latitude 7.1, longitude 95.8. It is 18 km in diameter and is named after Isabella Augusta Gregory Isabella Augusta, Lady Gregory (''née'' Persse; 15 March 1852 – 22 May 1932) was an Irish dramatist, folklo ... Other uses * "Gregory" (''The Americans''), the third episode of the first season of the television series ''The Americans'' See also * Greg (other) * Greggory * Gregoire (other) * Gregor (other) * Gregores (disambiguation ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Uracil
Uracil () (symbol U or Ura) is one of the four nucleobases in the nucleic acid RNA. The others are adenine (A), cytosine (C), and guanine (G). In RNA, uracil binds to adenine via two hydrogen bonds. In DNA, the uracil nucleobase is replaced by thymine (T). Uracil is a demethylated form of thymine. Uracil is a common and naturally occurring pyrimidine derivative. The name "uracil" was coined in 1885 by the German chemist Robert Behrend, who was attempting to synthesize derivatives of uric acid. Originally discovered in 1900 by Alberto Ascoli, it was isolated by hydrolysis of yeast nuclein; it was also found in bovine thymus and spleen, herring sperm, and wheat germ. It is a planar, unsaturated compound that has the ability to absorb light. Based on 12C/13C isotopic ratios of organic compounds found in the Murchison meteorite, it is believed that uracil, xanthine, and related molecules can also be formed extraterrestrially. Data from the Cassini mission, orbiting in th ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Uracil-DNA Glycosylase
Uracil-DNA glycosylase is also known as UNG or UDG. 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 (GC) pair in ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycosylase
Glycosylases ( EC 3.2) are enzymes that hydrolyze glycosyl compounds. They are a type of hydrolase (EC 3). In turn, glycosylases are divided into two groups: glycosidase Glycoside hydrolases (also called glycosidases or glycosyl hydrolases) catalyze the hydrolysis of glycosidic bonds in complex sugars. They are extremely common enzymes with roles in nature including degradation of biomass such as cellulose (c ...s—enzymes that hydrolyze O- and S-glycosyl compounds (EC 3.2.1) -- and enzymes that hydrolyze N-glycosyl compounds (EC 3.2.2). References {{Portal bar, Biology, border=no EC 3.2 Enzymes ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thymine-DNA Glycosylase
G/T mismatch-specific thymine DNA glycosylase is an enzyme that in humans is encoded by the TDG gene. Several bacterial proteins have strong sequence homology with this protein. Function The protein encoded by this gene belongs to the TDG/mug DNA glycosylase family. Thymine-DNA glycosylase (TDG) removes thymine moieties from G/T mismatches by hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of DNA and the mispaired thymine. With lower activity, this enzyme also removes thymine from C/T and T/T mispairings. TDG can also remove uracil and 5-bromouracil from mispairings with guanine. TDG knockout mouse models showed no increase in mispairing frequency suggesting that other enzymes, like the functional homologue MBD4, may provide functional redundancy. This gene may have a pseudogene in the p arm of chromosome 12. Additionally, in 2011, the human thymine DNA glycosylase (hTDG) was reported to efficiently excise 5-formylcytosine (5fC) and 5-carboxylcytosin ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
MBD4
Methyl-CpG-binding domain protein 4 is a protein that in humans is encoded by the ''MBD4'' gene. Structure Human MBD4 protein has 580 amino acids with a methyl-CpG-binding domain at amino acids 82–147 and a C-terminal DNA glycosylase domain at amino acids 426–580. These domains are separated by an intervening region that interacts with UHRF1, an E3 ubiquitin ligase, and USP7, a de-ubiquinating enzyme. Function DNA methylation is the major modification of eukaryotic genomes and plays an essential role in mammalian development. Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 (this gene) comprise a family of nuclear proteins related by the presence in each of a methyl-CpG-binding domain (MBD). Each of these proteins, with the exception of MBD3, is capable of binding specifically to methylated DNA. MBD4 may function to mediate the biological consequences of the methylation signal. In addition, MBD4 has protein sequence similarity to bacterial DNA repair enzymes and thus ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
