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DnaQ
''dnaQ'' is the gene encoding the ε subunit of DNA polymerase III in ''Escherichia coli''. The ε subunit is one of three core proteins in the DNA polymerase complex. It functions as a 3’→5’ DNA directed proofreading exonuclease that removes incorrectly incorporated bases during replication. ''dnaQ'' may also be referred to as ''mutD''. Biological role Missense mutations in the ''dnaQ'' gene lead to the induction of the SOS DNA repair mechanism. Mutating the essential amino acid in the catalytic center of the ε subunit leads to complete loss of function. Overexpression of the ε subunit decreases the incidence of mutations with exposure to UV, proving that the epsilon subunit has an essential function in DNA editing and preventing the initiation of SOS DNA repair. The ε subunit has also been proven to have some impact on the growth rate of E. coli. Silencing of the ''dnaQ'' gene is correlated to significantly reduced growth. Interactions The ε subunit is stabilize ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
DNA Polymerase III
DNA polymerase III holoenzyme is the primary enzyme complex involved in prokaryotic DNA replication. It was discovered by Thomas Kornberg (son of Arthur Kornberg) and Malcolm Gefter in 1970. The complex has high processivity (i.e. the number of nucleotides added per binding event) and, specifically referring to the replication of the ''E.coli'' genome, works in conjunction with four other DNA polymerases (Pol I, Pol II, Pol IV, and Pol V). Being the primary holoenzyme involved in replication activity, the DNA Pol III holoenzyme also has proofreading capabilities that corrects replication mistakes by means of exonuclease activity reading 3'→5' and synthesizing 5'→3'. DNA Pol III is a component of the replisome, which is located at the replication fork. Components The replisome is composed of the following: *2 DNA Pol III enzymes, each comprising α, ε and θ subunits. (It has been proven that there is a third copy of Pol III at the replisome.) **the α subunit (encoded ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Escherichia Coli
''Escherichia coli'' (),Wells, J. C. (2000) Longman Pronunciation Dictionary. Harlow ngland Pearson Education Ltd. also known as ''E. coli'' (), is a Gram-negative, facultative anaerobic, rod-shaped, coliform bacterium of the genus ''Escherichia'' that is commonly found in the lower intestine of warm-blooded organisms. Most ''E. coli'' strains are harmless, but some serotypes ( EPEC, ETEC etc.) can cause serious food poisoning in their hosts, and are occasionally responsible for food contamination incidents that prompt product recalls. Most strains do not cause disease in humans and are part of the normal microbiota of the gut; such strains are harmless or even beneficial to humans (although these strains tend to be less studied than the pathogenic ones). For example, some strains of ''E. coli'' benefit their hosts by producing vitamin K2 or by preventing the colonization of the intestine by pathogenic bacteria. These mutually beneficial relationships between ''E. col ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Proofreading (biology)
The term proofreading is used in genetics to refer to the error-correcting processes, first proposed by John Hopfield and Jacques Ninio, involved in DNA replication, immune system specificity, enzyme-substrate recognition among many other processes that require enhanced specificity. The proofreading mechanisms of Hopfield and Ninio are non-equilibrium active processes that consume ATP to enhance specificity of various biochemical reactions. In bacteria, all three DNA polymerases (I, II and III) have the ability to proofread, using 3’ → 5’ exonuclease activity. When an incorrect base pair is recognized, DNA polymerase reverses its direction by one base pair of DNA and excises the mismatched base. Following base excision, the polymerase can re-insert the correct base and replication can continue. In eukaryotes, only the polymerases that deal with the elongation (delta and epsilon) have proofreading ability (3’ → 5’ exonuclease activity). Proofreading also occurs in mRNA ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Exonuclease
Exonucleases are enzymes that work by cleaving nucleotides one at a time from the end (exo) of a polynucleotide chain. A hydrolyzing reaction that breaks phosphodiester bonds at either the 3′ or the 5′ end occurs. Its close relative is the endonuclease, which cleaves phosphodiester bonds in the middle (endo) of a polynucleotide chain. Eukaryotes and prokaryotes have three types of exonucleases involved in the normal turnover of mRNA: 5′ to 3′ exonuclease (Xrn1), which is a dependent decapping protein; 3′ to 5′ exonuclease, an independent protein; and poly(A)-specific 3′ to 5′ exonuclease. In both archaea and eukaryotes, one of the main routes of RNA degradation is performed by the multi-protein exosome complex, which consists largely of 3′ to 5′ exoribonucleases. Significance to polymerase RNA polymerase II is known to be in effect during transcriptional termination; it works with a 5' exonuclease (human gene Xrn2) to degrade the newly formed transcript ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SOS Response
The SOS response is a global response to DNA damage in which the cell cycle is arrested and DNA repair and mutagenesis is induced. The system involves the RecA protein ( Rad51 in eukaryotes). The RecA protein, stimulated by single-stranded DNA, is involved in the inactivation of the repressor (LexA) of SOS response genes thereby inducing the response. It is an error-prone repair system that contributes significantly to DNA changes observed in a wide range of species. Discovery The SOS response was discovered and named by Miroslav Radman in 1975. Mechanism During normal growth, the SOS genes are negatively regulated by LexA repressor protein dimers. Under normal conditions, LexA binds to a 20-bp consensus sequence (the SOS box) in the operator region for those genes. Some of these SOS genes are expressed at certain levels even in the repressed state, according to the affinity of LexA for their SOS box. Activation of the SOS genes occurs after DNA damage by the accumulation of s ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Histidinol-phosphatase
The enzyme histidinol-phosphatase (EC 3.1.3.15) catalysis, catalyzes the reaction :L-histidinol phosphate + H2O \rightleftharpoons L-histidinol + phosphate This enzyme participates in histidine metabolism. Nomenclature This enzyme belongs to the family of hydrolases, to be specific, those acting on phosphoric ester, monoester bonds. The List of enzymes, systematic name is L-histidinol-phosphate phosphohydrolase. Other names in common use include histidinol phosphate phosphatase, L-histidinol phosphate phosphatase, histidinolphosphate phosphatase, HPpase, and histidinolphosphatase. ''E. coli'' In ''E. coli'' the enzyme encoded by the gene ''hisB'' is a fused imidazoleglycerol-phosphate dehydratase and histidinol-phosphatase. References Further reading * EC 3.1.3 Enzymes of known structure {{3.1-enzyme-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
TREX1
Three prime repair exonuclease 1 is an enzyme that in humans is encoded by the ''TREX1'' gene. Function This gene encodes the major 3'->5' DNA exonuclease in human cells. The protein is a non-processive exonuclease that may serve a proofreading function for a human DNA polymerase. It is also a component of the SET complex, and acts to rapidly degrade 3' ends of nicked DNA during granzyme A-mediated cell death. Mutations in this gene result in Aicardi-Goutieres syndrome, chilblain lupus, RVCL (Retinal Vasculopathy with Cerebral Leukodystrophy), and Cree encephalitis. Multiple transcript variants encoding different isoforms have been found for this gene. Clinical relevance Mutations within the ''TREX1'' gene cause familial chilblain lupus. The ''TREX1'' polymorphisms confer susceptibility to systemic lupus erythematosus. Missense mutations of the ''TREX1'' gene significantly downregulate its exonucleolytic capacity and result in the accumulation of nucleic acids. The build- ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
DNA Polymerase Epsilon
DNA polymerase epsilon is a member of the DNA polymerase family of enzymes found in eukaryotes. It is composed of the following four subunits: POLE (central catalytic unit), POLE2 (subunit 2), POLE3 (subunit 3), and POLE4 (subunit 4). Recent evidence suggests that it plays a major role in leading strand DNA synthesis and nucleotide and base excision repair. Research had conducted to study nucleotide excision repair DNA synthesis by DNA polymerase epsilon in the presence of PCNA (proliferating cell nuclear antigen), RFC (replication factor C) and RPA (replication protein A). Either DNA polymerase epsilon or DNA polymerase delta along with DNA ligase DNA ligase is a specific type of enzyme, a ligase, () that facilitates the joining of DNA strands together by catalyzing the formation of a phosphodiester bond. It plays a role in repairing single-strand breaks in duplex DNA in living organ ... can be used to repair UV-damaged DNA. However, it is found that DNA polymerase del ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Retroelements
Retrotransposons (also called Class I transposable elements or transposons via RNA intermediates) are a type of genetic component that copy and paste themselves into different genomic locations (transposon) by converting RNA back into DNA through the reverse transcription process using an RNA transposition intermediate. Through reverse transcription, retrotransposons amplify themselves quickly to become abundant in eukaryotic genomes such as maize (49–78%) and humans (42%). They are only present in eukaryotes but share features with retroviruses such as HIV, for example, discontinuous reverse transcriptase-mediated extrachromosomal recombination. These retrotransposons are regulated by a family of short non-coding RNAs termed as PIWI -element induced wimpy testisinteracting RNAs (piRNAs). piRNA is a recently discovered class of ncRNAs, which are in the length range of ~24-32 nucleotides. Initially, piRNAs were described as repeat-associated siRNAs (rasiRNAs) because of their ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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