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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] |
DNA Replication
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 life, living organisms, acting as the most essential part of heredity, 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 nucleic acid double helix, double helix of two Complementary DNA, complementary DNA strand, 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, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bacillus
''Bacillus'', from Latin "bacillus", meaning "little staff, wand", is a genus of Gram-positive, rod-shaped bacteria, a member of the phylum ''Bacillota'', with 266 named species. The term is also used to describe the shape (rod) of other so-shaped bacteria; and the plural ''Bacilli'' is the name of the class of bacteria to which this genus belongs. ''Bacillus'' species can be either obligate aerobes which are dependent on oxygen, or facultative anaerobes which can survive in the absence of oxygen. Cultured ''Bacillus'' species test positive for the enzyme catalase if oxygen has been used or is present. ''Bacillus'' can reduce themselves to oval endospores and can remain in this dormant state for years. The endospore of one species from Morocco is reported to have survived being heated to 420 °C. Endospore formation is usually triggered by a lack of nutrients: the bacterium divides within its cell wall, and one side then engulfs the other. They are not true spores (i.e. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Winged-helix Transcription Factors
Consisting of about 110 amino acids, the domain in winged-helix transcription factors (see Regulation of gene expression) has four helices and a two-strand beta-sheet. These proteins are classified into 19 families called FoxA-FoxS. Mutations in FoxP proteins are implicated in human autoimmune diseases. See also * FOX proteins FOX (forkhead box) proteins are a family of transcription factors that play important roles in regulating the expression of genes involved in cell growth, proliferation, Cellular differentiation, differentiation, and longevity. Many FOX proteins a ... External links * Transcription factors {{Transcription factors, g3 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Homodimer
In biochemistry, a protein dimer is a macromolecular complex or protein multimer, multimer formed by two protein monomers, or single proteins, which are usually Non-covalent interaction, non-covalently bound. Many macromolecules, such as proteins or nucleic acids, form dimers. The word ''dimer'' has roots meaning "two parts", ''wikt:di-#Prefix, di-'' + ''wikt:-mer#Suffix, -mer''. A protein dimer is a type of protein quaternary structure. A protein homodimer is formed by two identical proteins while a protein heterodimer is formed by two different proteins. Most protein dimers in biochemistry are not connected by covalent bonds. An example of a non-covalent heterodimer is the enzyme reverse transcriptase, which is composed of two different amino acid chains. An exception is dimers that are linked by disulfide bridges such as the homodimeric protein IKBKG, NEMO. Some proteins contain specialized domains to ensure dimerization (dimerization domains) and specificity. The G protein- ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Base Pair
A base pair (bp) is a fundamental unit of double-stranded nucleic acids consisting of two nucleobases bound to each other by hydrogen bonds. They form the building blocks of the DNA double helix and contribute to the folded structure of both DNA and RNA. Dictated by specific hydrogen bonding patterns, "Watson–Crick" (or "Watson–Crick–Franklin") base pairs (guanine–cytosine and adenine–thymine) allow the DNA helix to maintain a regular helical structure that is subtly dependent on its nucleotide sequence. The Complementarity (molecular biology), complementary nature of this based-paired structure provides a Redundancy (information theory), redundant copy of the genetic information encoded within each strand of DNA. The regular structure and data redundancy provided by the DNA double helix make DNA well suited to the storage of genetic information, while base-pairing between DNA and incoming nucleotides provides the mechanism through which DNA polymerase replicates DNA and ... [...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] |
Proteopedia
Proteopedia is a wiki, 3D encyclopedia of proteins and other molecules. Website The site contains a page for all of the entries in the Protein Data Bank (PDB), as well as pages that are more descriptive of protein structures in general such as acetylcholinesterase, hemoglobin, and the photosystem II with a Jmol view that highlights functional sites and ligands. It employs a scene-authoring tool so that users do not have to learn JSmol script language to create customized molecular scenes. Custom scenes are easily attached to "green links" in descriptive text that display those scenes in JSmol. A web browser is all that is needed to access the site and the 3D information; no viewers are required to be installed. Proteopedia was the winner of the 2010 award for the best website by '' The Scientist'' magazine. Licensing terms All user-added content is free and covered by the GNU Free Documentation License. Proteopedia is hosted at the Israel Structural Proteomics Center at the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
