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Replication Terminator Tus Family
Tus (terminus utilization substance), also known as a ter-binding protein, is a protein that binds to terminator sequences and acts as a counter-helicase when it comes in contact with an advancing helicase. The bound Tus protein effectively halts DNA polymerase movement. Tus helps end DNA replication in prokaryotes.Slonczewski, Joan, and John Watkins. Foster. Microbiology: An Evolving Science. New York: W.W. Norton &, 2009. Print. They function by binding to DNA replication terminator sequences, thus preventing the passage of replication forks. The termination efficiency is affected by the affinity of a particular protein for the terminator sequence. In ''E. coli'' (), Tus binds to 10 closely related sites encoded in the chromosome, although only 6 are likely to be involved in replication termination. Each site is 23 base pairs. The sites are called Ter sites, and are designated ''TerA'', ''TerB'', ..., ''TerG''. These binding sites are asymmetric, such that when a Tus-Ter com ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bacillus Subtilis
''Bacillus subtilis'' (), known also as the hay bacillus or grass bacillus, is a gram-positive, catalase-positive bacterium, found in soil and the gastrointestinal tract of ruminants, humans and marine sponges. As a member of the genus ''Bacillus'', ''B. subtilis'' is rod-shaped, and can form a tough, protective endospore, allowing it to tolerate extreme environmental conditions. ''B. subtilis'' has historically been classified as an obligate aerobe, though evidence exists that it is a facultative anaerobe. ''B. subtilis'' is considered the best studied Gram-positive bacterium and a model organism to study bacterial chromosome replication and cell differentiation. It is one of the bacterial champions in secreted enzyme production and used on an industrial scale by biotechnology companies. Description ''Bacillus subtilis'' is a Gram-positive bacterium, rod-shaped and catalase-positive. It was originally named ''Vibrio subtilis'' by Christian Gottfried Ehrenberg, an ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tus (biology)
Tus (terminus utilization substance), also known as a ter-binding protein, is a protein that binds to terminator sequences and acts as a counter-helicase when it comes in contact with an advancing helicase. The bound Tus protein effectively halts DNA polymerase movement. Tus helps end DNA replication in prokaryotes.Slonczewski, Joan, and John Watkins. Foster. Microbiology: An Evolving Science. New York: W.W. Norton &, 2009. Print. They function by binding to DNA replication terminator sequences, thus preventing the passage of replication forks. The termination efficiency is affected by the affinity of a particular protein for the terminator sequence. In ''E. coli'' (), Tus binds to 10 closely related sites encoded in the chromosome, although only 6 are likely to be involved in replication termination. Each site is 23 base pairs. The sites are called Ter sites, and are designated ''TerA'', ''TerB'', ..., ''TerG''. These binding sites are asymmetric, such that when a Tus-Ter com ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Replication Fork
In molecular biology, DNA replication is the biological process of producing two identical replicas of DNA from one original DNA molecule. DNA replication occurs in all living organisms, acting as the most essential part of biological inheritance. This is essential for cell division during growth and repair of damaged tissues, while it also ensures that each of the new cells receives its own copy of the DNA. The cell possesses the distinctive property of division, which makes replication of DNA essential. DNA is made up of a double helix of two complementary strands. DNA is often called double helix. The double helix describes the appearance of a double-stranded DNA which is composed of two linear strands that run opposite to each other and twist together. During replication, these strands are separated. Each strand of the original DNA molecule then serves as a template for the production of its counterpart, a process referred to as semiconservative replication. As a result, th ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CATH
Cath may refer to: __NOTOC__ People * Cath Bishop (born 1971), British former rower and 2003 world champion * Cath Carroll (born 1960), British musician and music journalist * Cath Coffey (), one of the earliest members of British rap band Stereo MCs * Cath Crowley (born 1971), Australian young adult fiction author * Cath Kidston (born 1958), English fashion designer, businesswoman and author * Cath Mayo, New Zealand short story writer, novelist and musician * Cath Rae (born 1985), Scottish field hockey goalkeeper * Cath Vautier (1902–1989), New Zealand netball player, teacher and sports administrator * Cath Wallace (born 1952), New Zealand environmentalist and academic In mythology * Catha (mythology) or Cath, an Etruscan deity * Cath Palug, a feline creature in Welsh mythology Songs *" Cath...", a Death Cab for Cutie song *"Cath", a hit song by The Bluebells Other uses *Cath., abbreviation for Catholic *Catheter or catheterization * CATH, protein structure classificat ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Beta Sheet
The beta sheet (β-sheet, also β-pleated sheet) is a common motif of the regular protein secondary structure. Beta sheets consist of beta strands (β-strands) connected laterally by at least two or three backbone hydrogen bonds, forming a generally twisted, pleated sheet. A β-strand is a stretch of polypeptide chain typically 3 to 10 amino acids long with backbone in an extended conformation. The supramolecular association of β-sheets has been implicated in the formation of the fibrils and protein aggregates observed in amyloidosis, Alzheimer's disease and other proteinopathies. History The first β-sheet structure was proposed by William Astbury in the 1930s. He proposed the idea of hydrogen bonding between the peptide bonds of parallel or antiparallel extended β-strands. However, Astbury did not have the necessary data on the bond geometry of the amino acids in order to build accurate models, especially since he did not then know that the peptide bond was planar. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alpha Helix
An alpha helix (or α-helix) is a sequence of amino acids in a protein that are twisted into a coil (a helix). The alpha helix is the most common structural arrangement in the Protein secondary structure, secondary structure of proteins. It is also the most extreme type of local structure, and it is the local structure that is most easily predicted from a sequence of amino acids. The alpha helix has a right-handed helix conformation in which every backbone amino, N−H group hydrogen bonds to the backbone carbonyl, C=O group of the amino acid that is four residue (biochemistry), residues earlier in the protein sequence. Other names The alpha helix is also commonly called a: * Pauling–Corey–Branson α-helix (from the names of three scientists who described its structure) * 3.613-helix because there are 3.6 amino acids in one ring, with 13 atoms being involved in the ring formed by the hydrogen bond (starting with amidic hydrogen and ending with carbonyl oxygen) Discovery ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Replication Terminator Protein
The replication terminator protein (RTP) is a DNA-binding protein that helps terminate DNA replication in ''Bacillus''. It has a winged-helix structure and forms a homodimer via hydrogen bonds. The dimer is symmetric when it is not bound to DNA, but becomes asymmetrical when it is bound. Its termination activity is polar: it stops the replication fork from continuing in one direction, but a fork going the other direction is allowed to proceed. Binding site Each RTP dimer binds to a binding site 20 bp long. A ''ter'' site on the actual bacterial chromosome consists of two dimer-binding sites "A" and "B", with 3 bp of overlap. The "A" site matches the preference of RTP better and hence has higher affinity. Binding of the "A" site with an RTP dimer changes the shape of the "B" site such that it is easier to bind to another RTP dimer. Mechanism Before 2006, it was assumed that RTP simply terminates DNA replication by clamping onto the DNA and physically blocking the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ter Site
Tus (terminus utilization substance), also known as a ter-binding protein, is a protein that binds to terminator sequences and acts as a counter-helicase when it comes in contact with an advancing helicase. The bound Tus protein effectively halts DNA polymerase movement. Tus helps end DNA replication in prokaryotes.Slonczewski, Joan, and John Watkins. Foster. Microbiology: An Evolving Science. New York: W.W. Norton &, 2009. Print. They function by binding to DNA replication terminator sequences, thus preventing the passage of replication forks. The termination efficiency is affected by the affinity of a particular protein for the terminator sequence. In ''E. coli'' (), Tus binds to 10 closely related sites encoded in the chromosome, although only 6 are likely to be involved in replication termination. Each site is 23 base pairs. The sites are called Ter sites, and are designated ''TerA'', ''TerB'', ..., ''TerG''. These binding sites are asymmetric, such that when a Tus-Ter com ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
DnaB Helicase
DnaB helicase is an enzyme in bacteria which opens the replication fork during DNA replication. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerisation of the N-terminal domain has been observed and may occur during the enzymatic cycle. Initially when DnaB binds to dnaA, it is associated with dnaC, a negative regulator. After DnaC dissociates, DnaB binds dnaG. The N-terminal has a multi-helical structure that forms an orthogonal bundle. The C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis. In eukaryotes, helicase function is provided by the MCM ( Minichromosome maintenance) complex. The DnaB helicase is the product of the ''dnaB'' gene. DnaB is expressed as a monomer and oligomerises into hexamer through N-terminal interactions. Replicative helicases have a central ring and that ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Chromosome
A chromosome is a package of DNA containing part or all of the genetic material of an organism. In most chromosomes, the very long thin DNA fibers are coated with nucleosome-forming packaging proteins; in eukaryotic cells, the most important of these proteins are the histones. Aided by chaperone proteins, the histones bind to and condense the DNA molecule to maintain its integrity. These eukaryotic chromosomes display a complex three-dimensional structure that has a significant role in transcriptional regulation. Normally, chromosomes are visible under a light microscope only during the metaphase of cell division, where all chromosomes are aligned in the center of the cell in their condensed form. Before this stage occurs, each chromosome is duplicated ( S phase), and the two copies are joined by a centromere—resulting in either an X-shaped structure if the centromere is located equatorially, or a two-armed structure if the centromere is located distally; the jo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sequence (biology)
A sequence in biology is the one-dimensional ordering of monomers, covalently linked within a biopolymer; it is also referred to as the primary structure of a biological macromolecule. While it can refer to many different molecules, the term sequence is most often used to refer to a DNA sequence or a protein sequence.https://www.nobelprize.org/uploads/2018/06/sanger-lecture.pdf See also * Dot plot (bioinformatics) * Sequence analysis In bioinformatics, sequence analysis is the process of subjecting a DNA, RNA or peptide sequence to any of a wide range of analytical methods to understand its features, function, structure, or evolution. It can be performed on the entire genome ... References Molecular biology {{molecular-biology-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
