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Planarian Secretory Cell Nidovirus
Planarian secretory cell nidovirus (PSCNV) is a virus of the species ''Planidovirus 1'', a nidovirus notable for its extremely large genome. At 41.1 kilobases, it is the largest known genome of an RNA virus. It was discovered by inspecting the transcriptomes of the planarian flatworm '' Schmidtea mediterranea'' and is the first known RNA virus infecting planarians. It was first described in 2018. Genome and expression The PSCNV genome is 41.1 kilobases long, the largest known genome in an RNA virus. It is substantially larger than coronaviruses, another group of nidoviruses known for large genomes, which are typically in the 27-32kb range. PSCNV has an unusual genomic organization consisting of a single extremely large open reading frame (ORF) which encodes a polyprotein of 13,556 amino acids - the largest protein known to be encoded by an RNA virus. Bioinformatics analysis of the genome suggests it is organized similarly to canonical nidovirus genomes, in which ORF1a and ORF ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nidovirus
''Nidovirales'' is an order of enveloped, positive-strand RNA viruses which infect vertebrates and invertebrates. Host organisms include mammals, birds, reptiles, amphibians, fish, arthropods, molluscs, and helminths. The order includes the families ''Coronaviridae'', ''Arteriviridae, Roniviridae,'' and ''Mesoniviridae''. Member viruses have a viral envelope and a positive-sense, single-stranded RNA genome which is capped and polyadenylated. Nidoviruses are named for the Latin ''nidus'', meaning nest, as all viruses in this order produce a 3' co-terminal nested set of subgenomic mRNAs during infection. Virology Structure Nidoviruses have a viral envelope and a positive-sense, single-stranded RNA genome which is capped and polyadenylated. The group expresses structural proteins separately from the nonstructural ones. The structural proteins are encoded at the 3’ region of the genome and are expressed from a set of subgenomic mRNAs. Member viruses encode one main p ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
3' End
Directionality, in molecular biology and biochemistry, is the end-to-end chemical orientation of a single strand of nucleic acid. In a single strand of DNA or RNA, the chemical convention of naming carbon atoms in the nucleotide pentose-sugar-ring means that there will be a 5′ end (usually pronounced "five-prime end"), which frequently contains a phosphate group attached to the 5′ carbon of the ribose ring, and a 3′ end (usually pronounced "three-prime end"), which typically is unmodified from the ribose -OH substituent. In a DNA double helix, the strands run in opposite directions to permit base pairing between them, which is essential for replication or transcription of the encoded information. Nucleic acids can only be synthesized in vivo in the 5′-to-3′ direction, as the polymerases that assemble various types of new strands generally rely on the energy produced by breaking nucleoside triphosphate bonds to attach new nucleoside monophosphates to the 3′- ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
RNA-dependent RNA Polymerase
RNA-dependent RNA polymerase (RdRp) or RNA replicase is an enzyme that catalyzes the replication of RNA from an RNA template. Specifically, it catalyzes synthesis of the RNA strand complementary to a given RNA template. This is in contrast to typical DNA-dependent RNA polymerases, which all organisms use to catalyze the transcription of RNA from a DNA template. RdRp is an essential protein encoded in the genomes of most RNA-containing viruses with no DNA stage including SARS-CoV-2. Some eukaryotes also contain RdRps, which are involved in RNA interference and differ structurally from viral RdRps. History Viral RdRps were discovered in the early 1960s from studies on mengovirus and polio virus when it was observed that these viruses were not sensitive to actinomycin D, a drug that inhibits cellular DNA-directed RNA synthesis. This lack of sensitivity suggested that there is a virus-specific enzyme that could copy RNA from an RNA template and not from a DNA template. Distr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
NiRAN
Na'aran ( he, נערן), formerly known as Niran () is an Israeli settlement organized as a kibbutz in the West Bank. Located in Area C of the Jordan Valley near Jericho,Niran Bik'at HaYarden Regional Council it falls under the jurisdiction of . In it had a population of . The international community considers Israeli settlements in the West Bank illegal under international law, but the Israeli government disputes this. Etymology The settlement was originally named Nira ...[...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nucleotidyltransferase
Nucleotidyltransferases are transferase enzymes of phosphorus-containing groups, e.g., substituents of nucleotidylic acids or simply nucleoside monophosphates. The general reaction of transferring a nucleoside monophosphate moiety from A to B, can be written as: :A-P-N + B \rightleftharpoons A + B-P-N For example, in the case of polymerases, A is pyrophosphate and B is the nascent polynucleotide. They are classified under EC number 2.7.7 and they can be categorised into: #Uridylyltransferases, which transfer uridylyl- groups # Adenylyltransferases, which transfer adenylyl- groups #Guanylyltransferases, which transfer guanylyl- groups # Cytitidylyltransferases, which transfer cytidylyl- groups # Thymidylyltransferases, which transfer thymidylyl- groups Role in metabolism Many metabolic enzymes are modified by nucleotidyltransferases. The attachment of an AMP (adenylylation) or UMP (uridylylation) can activate or inactivate an enzyme or change its specificity (see figure). Thes ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Transmembrane Domain
A transmembrane domain (TMD) is a membrane-spanning protein domain. TMDs generally adopt an alpha helix topological conformation, although some TMDs such as those in porins can adopt a different conformation. Because the interior of the lipid bilayer is hydrophobic, the amino acid residues in TMDs are often hydrophobic, although proteins such as membrane pumps and ion channels can contain polar residues. TMDs vary greatly in length, sequence, and hydrophobicity, adopting organelle-specific properties. Functions of transmembrane domains Transmembrane domains are known to perform a variety of functions. These include: * Anchoring transmembrane proteins to the membrane. *Facilitating molecular transport of molecules such as ions and proteins across biological membranes; usually hydrophilic residues and binding sites in the TMDs help in this process. *Signal transduction across the membrane; many transmembrane proteins, such as G protein-coupled receptors, receive extracellular ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Main Protease
The 3C-like protease (3CLpro) or main protease (Mpro), formally known as C30 endopeptidase or 3-chymotrypsin-like protease, is the main protease found in coronaviruses. It cleaves the coronavirus polyprotein at eleven conserved sites. It is a cysteine protease and a member of the PA clan of proteases. It has a cysteine-histidine catalytic dyad at its active site and cleaves a Gln–(Ser/Ala/Gly) peptide bond. The Enzyme Commission refers to this family as SARS coronavirus main proteinase (Mpro; ). The 3CL protease corresponds to coronavirus nonstructural protein 5 (nsp5). The "3C" in the common name refers to the 3C protease (3Cpro) which is a homologous protease found in picornaviruses. Function The 3C-like protease is able to catalytically cleave a peptide bond between a glutamine at position P1 and a small amino acid (serine, alanine, or glycine) at position P1'. The SARS coronavirus 3CLpro can for instance self-cleave the following peptides: The protease is i ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sequence Conservation
In evolutionary biology, conserved sequences are identical or similar sequences in nucleic acids ( DNA and RNA) or proteins across species ( orthologous sequences), or within a genome ( paralogous sequences), or between donor and receptor taxa ( xenologous sequences). Conservation indicates that a sequence has been maintained by natural selection. A highly conserved sequence is one that has remained relatively unchanged far back up the phylogenetic tree, and hence far back in geological time. Examples of highly conserved sequences include the RNA components of ribosomes present in all domains of life, the homeobox sequences widespread amongst Eukaryotes, and the tmRNA in Bacteria. The study of sequence conservation overlaps with the fields of genomics, proteomics, evolutionary biology, phylogenetics, bioinformatics and mathematics. History The discovery of the role of DNA in heredity, and observations by Frederick Sanger of variation between animal insulins in 1949, promp ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Domain
In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or disulfide bridges. Domains often form functional units, such as the calcium-binding EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimeric proteins. Background The concept of the domain was first proposed in 1973 by Wetlaufer aft ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Viral Replication
Viral replication is the formation of biological viruses during the infection process in the target host cells. Viruses must first get into the cell before viral replication can occur. Through the generation of abundant copies of its genome and packaging these copies, the virus continues infecting new hosts. Replication between viruses is greatly varied and depends on the type of genes involved in them. Most DNA viruses assemble in the nucleus while most RNA viruses develop solely in cytoplasm. Viral production / replication Viruses multiply only in living cells. The host cell must provide the energy and synthetic machinery and the low- molecular-weight precursors for the synthesis of viral proteins and nucleic acids. The virus replication occurs in seven stages, namely; # Attachment # Entry, # Uncoating, # Transcription / mRNA production, # Synthesis of virus components, # Virion assembly and # Release (Liberation Stage). Attachment It is the first step of viral replication ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Stoichiometry
Stoichiometry refers to the relationship between the quantities of reactants and products before, during, and following chemical reactions. Stoichiometry is founded on the law of conservation of mass where the total mass of the reactants equals the total mass of the products, leading to the insight that the relations among quantities of reactants and products typically form a ratio of positive integers. This means that if the amounts of the separate reactants are known, then the amount of the product can be calculated. Conversely, if one reactant has a known quantity and the quantity of the products can be empirically determined, then the amount of the other reactants can also be calculated. This is illustrated in the image here, where the balanced equation is: : Here, one molecule of methane reacts with two molecules of oxygen gas to yield one molecule of carbon dioxide and two molecules of water. This particular chemical equation is an example of complete combustion. St ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Programmed Ribosomal Frameshift
Ribosomal frameshifting, also known as translational frameshifting or translational recoding, is a biological phenomenon that occurs during translation that results in the production of multiple, unique proteins from a single mRNA. The process can be programmed by the nucleotide sequence of the mRNA and is sometimes affected by the secondary, 3-dimensional mRNA structure. It has been described mainly in viruses (especially retroviruses), retrotransposons and bacterial insertion elements, and also in some cellular genes. Process overview Proteins are translated by reading tri-nucleotides on the mRNA strand, also known as codons, from one end of the mRNA to the other (from the 5' to the 3' end) starting with the amino acid methionine as the start (initiation) codon AUG. Each codon is translated into a single amino acid. The code itself is considered degenerate, meaning that a particular amino acid can be specified by more than one codons. However, a shift of any number of nucleot ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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