|
BlyA Holin Family
The BlyA Holin FamilyTC# 1.E.17 is a group of holin proteins that are approximately 55-70 amino acyl residues (aas) in length and exhibit one transmembrane segment (TMS). A representative list of the proteins belonging to the BlyA holin family can be found in thTransporter Classification Database BlyAB The BlyA membrane protein and the BlyB soluble accessory protein are encoded on the conserved cp32 plasmid of ''Borrelia burgdorferi,'' which can be packaged into a bacteriophage particle. These two proteins had previously been proposed to comprise a hemolysis system, but Damman et al. (2000) provided evidence that BlyAB functions as a prophage-encoded holin system. BlyA promotes endolysin-dependent lysis of an induced lambda lysogen that is defective for the lambda holin S gene. The holin pores are generally stable and nonspecific, allowing endolysin access to the peptidoglycan. Introduction of the ''Borrelia burgdorferi'' ''blyAB'' locus into ''Escherichia coli ''Escheric ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Borrelia Burgdorferi
''Borrelia burgdorferi'' is a bacterial species of the spirochete class in the genus ''Borrelia'', and is one of the causative agents of Lyme disease in humans. Along with a few similar genospecies, some of which also cause Lyme disease, it makes up the species complex of ''Borrelia burgdorferi'' sensu lato. The complex currently comprises 20 accepted and 3 proposed genospecies. ''B. burgdorferi'' sensu stricto exists in North America and Eurasia and until 2016 was the only known cause of Lyme disease in North America. ''Borrelia'' species are Gram-negative. Microbiology ''Borrelia burgdorferi'' is named after the researcher Willy Burgdorfer, who first isolated the bacterium in 1982. ''Borrelia burgdorferi'' is a microaerophile, requiring small amounts of oxygen in order to undergo glycolysis and survive. Like all other ''Borrelia'' sps., this bacterium is also gram-negative and a spirochete. Borrelia colonies are often smaller, rounded, and white with an elevated center. ''B. b ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bacteriophage
A bacteriophage (), also known informally as a ''phage'' (), is a duplodnaviria virus that infects and replicates within bacteria and archaea. The term was derived from "bacteria" and the Greek φαγεῖν ('), meaning "to devour". Bacteriophages are composed of proteins that encapsulate a DNA or RNA genome, and may have structures that are either simple or elaborate. Their genomes may encode as few as four genes (e.g. MS2) and as many as hundreds of genes. Phages replicate within the bacterium following the injection of their genome into its cytoplasm. Bacteriophages are among the most common and diverse entities in the biosphere. Bacteriophages are ubiquitous viruses, found wherever bacteria exist. It is estimated there are more than 1031 bacteriophages on the planet, more than every other organism on Earth, including bacteria, combined. Viruses are the most abundant biological entity in the water column of the world's oceans, and the second largest component of biom ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hemolysis (microbiology)
Hemolysis (from Greek αιμόλυση, meaning 'blood breakdown') is the breakdown of red blood cells. The ability of bacterial colonies to induce hemolysis when grown on blood agar is used to classify certain microorganisms. This is particularly useful in classifying streptococcal species. A substance that causes hemolysis is a ''hemolysin''. Types Alpha-hemolysis When alpha-hemolysis (α-hemolysis) is present, the agar under the colony is light and greenish. ''Streptococcus pneumoniae'' and a group of oral streptococci ( ''Streptococcus'' viridans or viridans streptococci) display alpha hemolysis. This is sometimes called ''green hemolysis'' because of the color change in the agar. Other synonymous terms are ''incomplete hemolysis'' and ''partial hemolysis''. Alpha hemolysis is caused by hydrogen peroxide produced by the bacterium, oxidizing hemoglobin producing the green oxidized derivative methemoglobin. Beta-hemolysis Beta-hemolysis (β-hemolysis), sometimes called ''comp ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lambda Holin Family
The Lambda Holin S (λ Holin) FamilyTC# 1.E.2 is a group of integral membrane transporter proteins belonging to the Holin Superfamily III. Members of this family generally consist of the characteristic three transmembrane segments (TMSs) and are of 110 amino acyl residues (aas) in length, on average. A representative list of members belonging to this family can be found in the Transporter Classification Database. Lambda Holin S Lambda holin S (Lysis protein S of phage lambda, holin S105TC# 1.E.2.1.1 is the prototype for class I holins. It has 3 TMSs with the N-terminus in the periplasm and the C-terminus in the cytoplasm. Its 107 codon sequence encodes two proteins with opposing functions, the holin, S105, and the holin inhibitor, S107. The latter protein, S107, is a 2-amino acid extension of the former protein, S105, due to a different translational initiation start site (M1-K2-M3 vs. M3). A cationic amino acid at position 2 is largely responsible for the inhibiting effect of S1 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peptidoglycan
Peptidoglycan or murein is a unique large macromolecule, a polysaccharide, consisting of sugars and amino acids that forms a mesh-like peptidoglycan layer outside the plasma membrane, the rigid cell wall (murein sacculus) characteristic of most bacteria (domain ''Bacteria''). The sugar component consists of alternating residues of β-(1,4) linked ''N''-acetylglucosamine (NAG) and ''N''-acetylmuramic acid (NAM). Attached to the ''N''-acetylmuramic acid is a oligopeptide chain made of three to five amino acids. The peptide chain can be cross-linked to the peptide chain of another strand forming the 3D mesh-like layer. Peptidoglycan serves a structural role in the bacterial cell wall, giving structural strength, as well as counteracting the osmotic pressure of the cytoplasm. This repetitive linking results in a dense peptidoglycan layer which is critical for maintaining cell form and withstanding high osmotic pressures, and it is regularly replaced by peptidoglycan production. Pep ... [...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] |
Protein Families
A protein family is a group of evolutionarily related proteins. In many cases, a protein family has a corresponding gene family, in which each gene encodes a corresponding protein with a 1:1 relationship. The term "protein family" should not be confused with family as it is used in taxonomy. Proteins in a family descend from a common ancestor and typically have similar three-dimensional structures, functions, and significant sequence similarity. The most important of these is sequence similarity (usually amino-acid sequence), since it is the strictest indicator of homology and therefore the clearest indicator of common ancestry. A fairly well developed framework exists for evaluating the significance of similarity between a group of sequences using sequence alignment methods. Proteins that do not share a common ancestor are very unlikely to show statistically significant sequence similarity, making sequence alignment a powerful tool for identifying the members of protein familie ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Membrane Proteins
Membrane proteins are common proteins that are part of, or interact with, biological membranes. Membrane proteins fall into several broad categories depending on their location. Integral membrane proteins are a permanent part of a cell membrane and can either penetrate the membrane (transmembrane) or associate with one or the other side of a membrane ( integral monotopic). Peripheral membrane proteins are transiently associated with the cell membrane. Membrane proteins are common, and medically important—about a third of all human proteins are membrane proteins, and these are targets for more than half of all drugs. Nonetheless, compared to other classes of proteins, determining membrane protein structures remains a challenge in large part due to the difficulty in establishing experimental conditions that can preserve the correct conformation of the protein in isolation from its native environment. Function Membrane proteins perform a variety of functions vital to the surv ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Transmembrane Proteins
A transmembrane protein (TP) is a type of integral membrane protein that spans the entirety of the cell membrane. Many transmembrane proteins function as gateways to permit the transport of specific substances across the membrane. They frequently undergo significant conformational changes to move a substance through the membrane. They are usually highly hydrophobic and aggregate and precipitate in water. They require detergents or nonpolar solvents for extraction, although some of them (beta-barrels) can be also extracted using denaturing agents. The peptide sequence that spans the membrane, or the transmembrane segment, is largely hydrophobic and can be visualized using the hydropathy plot. Depending on the number of transmembrane segments, transmembrane proteins can be classified as single-span (or bitopic) or multi-span (polytopic). Some other integral membrane proteins are called monotopic, meaning that they are also permanently attached to the membrane, but do not pass t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Transmembrane Transporters
A transmembrane protein (TP) is a type of integral membrane protein that spans the entirety of the cell membrane. Many transmembrane proteins function as gateways to permit the transport of specific substances across the membrane. They frequently undergo significant conformational changes to move a substance through the membrane. They are usually highly hydrophobic and aggregate and precipitate in water. They require detergents or nonpolar solvents for extraction, although some of them (beta-barrels) can be also extracted using denaturing agents. The peptide sequence that spans the membrane, or the transmembrane segment, is largely hydrophobic and can be visualized using the hydropathy plot. Depending on the number of transmembrane segments, transmembrane proteins can be classified as single-span (or bitopic) or multi-span (polytopic). Some other integral membrane proteins are called monotopic, meaning that they are also permanently attached to the membrane, but do not pass t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Transport Proteins
A transport protein (variously referred to as a transmembrane pump, transporter, escort protein, acid transport protein, cation transport protein, or anion transport protein) is a protein that serves the function of moving other materials within an organism. Transport proteins are vital to the growth and life of all living things. There are several different kinds of transport proteins. Carrier proteins are proteins involved in the movement of ions, small molecules, or macromolecules, such as another protein, across a biological membrane. Carrier proteins are integral membrane proteins; that is, they exist within and span the membrane across which they transport substances. The proteins may assist in the movement of substances by facilitated diffusion (i.e., passive transport) or active transport. These mechanisms of movement are known as carrier-mediated transport. Each carrier protein is designed to recognize only one substance or one group of very similar substances. Research ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Integral Membrane Proteins
An integral, or intrinsic, membrane protein (IMP) is a type of membrane protein that is permanently attached to the biological membrane. All ''transmembrane proteins'' are IMPs, but not all IMPs are transmembrane proteins. IMPs comprise a significant fraction of the proteins encoded in an organism's genome. Proteins that cross the membrane are surrounded by annular lipids, which are defined as lipids that are in direct contact with a membrane protein. Such proteins can only be separated from the membranes by using detergents, nonpolar solvents, or sometimes denaturing agents. Structure Three-dimensional structures of ~160 different integral membrane proteins have been determined at atomic resolution by X-ray crystallography or nuclear magnetic resonance spectroscopy. They are challenging subjects for study owing to the difficulties associated with extraction and crystallization. In addition, structures of many water-soluble protein domains of IMPs are available in the Prote ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
