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Streptomyces Coelicolor
''Streptomyces albidoflavus'' is a bacterium species from the genus of ''Streptomyces'' which has been isolated from soil from Poland. ''Streptomyces albidoflavus'' produces dibutyl phthalate and streptothricins. Small noncoding RNA Bacterial small RNAs are involved in post-transcriptional regulation. Using deep sequencing ''S. albidoflavus'' transcriptome was analysed at the end of exponential growth. 63 small RNAs were identified. Expression of 11 of them was confirmed by Northern blot. The sRNAs were shown to be only present in ''Streptomyces'' species. sRNA scr4677 (''Streptomyces coelicolor'' sRNA 4677) is located in the intergenic region between anti-sigma factor ''SCO4677'' gene and a putative regulatory protein gene ''SCO4676''. ''scr4677'' expression requires the ''SCO4677'' activity and ''scr4677'' sRNA itself seem to affect the levels of the ''SCO4676''-associated transcripts. Targets of two of ''S. albidoflavus'' noncoding RNAs have been identified. Noncoding ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Deutsche Sammlung Von Mikroorganismen Und Zellkulturen
The Leibniz Institute DSMZ - German Collection of Microorganisms and Cell Cultures GmbH (German: ''Leibniz-Institut DSMZ-Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH''), located in Braunschweig, is a research infrastructure in the Leibniz Association. Also the DSMZ is the world's most diverse collection of bioresources (status 2021: 75,000 bioresources). These include microorganisms (including more than 32,000 bacterial strains, 690 archaeal strains, 7,000 strains of yeasts and fungi) as well as more than 840 human and animal cell cultures, over 1. 500 plant viruses, over 940 bacteriophages, and 250 plasmids (status 2021). Since 2010, the scientific director of the Leibniz Institute DSMZ has been Jörg Overmann, a microbiologist with a PhD. He holds a professorship in microbiology at the Technical University of Braunschweig. Since August 2018, he has led the institute in a dual leadership with Bettina Fischer as administrative director. History Stru ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Methylenomycin A
Methylenomycin A is a cyclopentanone derived antibiotic produced by ''Streptomyces coelicolor'' A3(2) that is effective against both Gram-negative and Gram-positive In bacteriology, gram-positive bacteria are bacteria that give a positive result in the Gram stain test, which is traditionally used to quickly classify bacteria into two broad categories according to their type of cell wall. Gram-positive bact ... bacteria. Methylenomycins are naturally produced in two variants: A and B. See also * Methylenomycin B References Antibiotics Epoxides Enones Carboxylic acids Oxygen heterocycles Vinylidene compounds {{Antibiotic-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ligase
In biochemistry, a ligase is an enzyme that can catalyze the joining (ligation) of two large molecules by forming a new chemical bond. This is typically via hydrolysis of a small pendant chemical group on one of the larger molecules or the enzyme catalyzing the linking together of two compounds, e.g., enzymes that catalyze joining of C-O, C-S, C-N, etc. In general, a ligase catalyzes the following reaction: :Ab + C → A–C + b or sometimes :Ab + cD → A–D + b + c + d + e + f where the lowercase letters can signify the small, dependent groups. Ligase can join two complementary fragments of nucleic acid and repair single stranded breaks that arise in double stranded DNA during replication. Nomenclature The common names of ligases often include the word "ligase", such as DNA ligase, an enzyme commonly used in molecular biology laboratories to join together DNA fragments. Other common names for ligases include the word "synthetase", because they are used to synthes ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nuclease
A nuclease (also archaically known as nucleodepolymerase or polynucleotidase) is an enzyme capable of cleaving the phosphodiester bonds between nucleotides of nucleic acids. Nucleases variously effect single and double stranded breaks in their target molecules. In living organisms, they are essential machinery for many aspects of DNA repair. Defects in certain nucleases can cause genetic instability or immunodeficiency. Nucleases are also extensively used in molecular cloning. There are two primary classifications based on the locus of activity. Exonucleases digest nucleic acids from the ends. Endonucleases act on regions in the ''middle'' of target molecules. They are further subcategorized as deoxyribonucleases and ribonucleases. The former acts on DNA, the latter on RNA. History In the late 1960s, scientists Stuart Linn and Werner Arber isolated examples of the two types of enzymes responsible for phage growth restriction in Escherichia coli ( E. coli) bacteria. One of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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 organisms, but some forms (such as DNA ligase IV) may specifically repair double-strand breaks (i.e. a break in both complementary strands of DNA). Single-strand breaks are repaired by DNA ligase using the complementary strand of the double helix as a template, with DNA ligase creating the final phosphodiester bond to fully repair the DNA. DNA ligase is used in both DNA repair and DNA replication (see '' Mammalian ligases''). In addition, DNA ligase has extensive use in molecular biology laboratories for recombinant DNA experiments (see '' Research applications''). Purified DNA ligase is used in gene cloning to join DNA molecules together to form recombinant DNA. Enzymatic mechanism The mechanism of DNA ligase is to form two covalent p ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
C-terminus
The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein or polypeptide), terminated by a free carboxyl group (-COOH). When the protein is translated from messenger RNA, it is created from N-terminus to C-terminus. The convention for writing peptide sequences is to put the C-terminal end on the right and write the sequence from N- to C-terminus. Chemistry Each amino acid has a carboxyl group and an amine group. Amino acids link to one another to form a chain by a dehydration reaction which joins the amine group of one amino acid to the carboxyl group of the next. Thus polypeptide chains have an end with an unbound carboxyl group, the C-terminus, and an end with an unbound amine group, the N-terminus. Proteins are naturally synthesized starting from the N-terminus and ending at the C-terminus. Function C-terminal retention signals While the N-terminus of a protein often ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Shrimp Alkaline Phosphatase
The enzyme alkaline phosphatase (EC 3.1.3.1, alkaline phosphomonoesterase; phosphomonoesterase; glycerophosphatase; alkaline phosphohydrolase; alkaline phenyl phosphatase; orthophosphoric-monoester phosphohydrolase (alkaline optimum), systematic name phosphate-monoester phosphohydrolase (alkaline optimum)) catalyses the following reaction: : a phosphate monoester + H2O = an alcohol + phosphate Alkaline phosphatase has the physiological role of dephosphorylating compounds. The enzyme is found across a multitude of organisms, prokaryotes and eukaryotes alike, with the same general function but in different structural forms suitable to the environment they function in. Alkaline phosphatase is found in the periplasmic space of '' E. coli'' bacteria. This enzyme is heat stable and has its maximum activity at high pH. In humans, it is found in many forms depending on its origin within the body – it plays an integral role in metabolism within the liver and development withi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sequence Homology
Sequence homology is the biological homology between DNA, RNA, or protein sequences, defined in terms of shared ancestry in the evolutionary history of life. Two segments of DNA can have shared ancestry because of three phenomena: either a speciation event (orthologs), or a duplication event (paralogs), or else a horizontal (or lateral) gene transfer event (xenologs). Homology among DNA, RNA, or proteins is typically inferred from their nucleotide or amino acid sequence similarity. Significant similarity is strong evidence that two sequences are related by evolutionary changes from a common ancestral sequence. Alignments of multiple sequences are used to indicate which regions of each sequence are homologous. Identity, similarity, and conservation The term "percent homology" is often used to mean "sequence similarity”, that is the percentage of identical residues (''percent identity''), or the percentage of residues conserved with similar physicochemical properties ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ku (protein)
Ku is a dimeric protein complex that binds to DNA double-strand break ends and is required for the non-homologous end joining (NHEJ) pathway of DNA repair. Ku is evolutionarily conserved from bacteria to humans. The ancestral bacterial Ku is a homodimer (two copies of the same protein bound to each other). Eukaryotic Ku is a heterodimer of two polypeptides, Ku70 (XRCC6) and Ku80 (XRCC5), so named because the molecular weight of the human Ku proteins is around 70 kDa and 80 kDa. The two Ku subunits form a basket-shaped structure that threads onto the DNA end. Once bound, Ku can slide down the DNA strand, allowing more Ku molecules to thread onto the end. In higher eukaryotes, Ku forms a complex with the DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to form the full DNA-dependent protein kinase, DNA-PK. Ku is thought to function as a molecular scaffold to which other proteins involved in NHEJ can bind, orienting the double-strand break for ligation. The Ku70 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
