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Halorhodopsin
Halorhodopsin is a light-gated ion pump, specific for chloride ions, found in archaea, known as halobacteria. It is a seven-transmembrane retinylidene protein from microbial rhodopsin family. It is similar in tertiary structure (but not primary sequence structure) to vertebrate rhodopsins, the pigments that sense light in the retina. Halorhodopsin also shares sequence similarity to channelrhodopsin, another light-driven ion channel. Halorhodopsin contains the essential light-isomerizable vitamin A derivative all-trans-retinal. Due to the intense attention on solving the structure and function of this molecule, halorhodopsin is one of the few membrane proteins whose crystal structure is known. Halorhodopsin uses the energy of green/yellow light to move chloride ions into the cell, overcoming the membrane potential. Beside chlorides it transports other halides and nitrates into the cell. Potassium chloride uptake by cells helps to maintain osmotic balance during cell growth. By ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Optogenetics
Optogenetics is a biological technique to control the activity of neurons or other cell types with light. This is achieved by expression of light-sensitive ion channels, pumps or enzymes specifically in the target cells. On the level of individual cells, light-activated enzymes and transcription factors allow precise control of biochemical signaling pathways. In systems neuroscience, the ability to control the activity of a genetically defined set of neurons has been used to understand their contribution to decision making, learning, fear memory, mating, addiction, feeding, and locomotion. In a first medical application of optogenetic technology, vision was partially restored in a blind patient. Optogenetic techniques have also been introduced to map the functional connectivity of the brain''.'' By altering the activity of genetically labelled neurons with light and using imaging and electrophysiology techniques to record the activity of other cells, researchers can identi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Microbial Rhodopsin
Microbial rhodopsins, also known as bacterial rhodopsins are retinal-binding proteins that provide light-dependent ion transport and sensory functions in halophilic and other bacteria. They are integral membrane proteins with seven transmembrane helices, the last of which contains the attachment point (a conserved lysine) for retinal. This protein family includes light-driven proton pumps, ion pumps and ion channels, as well as light sensors. For example, the proteins from halobacteria include bacteriorhodopsin and archaerhodopsin, which are light-driven proton pumps; halorhodopsin, a light-driven chloride pump; and sensory rhodopsin, which mediates both photoattractant (in the red) and photophobic (in the ultra-violet) responses. Proteins from other bacteria include proteorhodopsin. Contrary to their name, microbial rhodopsins are found not only in Archaea and Bacteria, but also in Eukaryota (such as algae) and viruses; although they are rare in complex multicellular organi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Retinylidene Protein
Retinylidene proteins, are proteins that use retinal as a chromophore for light reception. They are the molecular basis for a variety of light-sensing systems from phototaxis in flagellates to eyesight in animals. Retinylidene proteins include all forms of opsin and rhodopsin (in the broad sense). While rhodopsin in the narrow sense refers to a dim-light visual pigment found in vertebrates, usually on rod cells, ''rhodopsin'' in the broad sense (as used here) refers to any molecule consisting of an opsin and a retinal chromophore in the ground state. When activated by light, the chromophore is isomerized, at which point the molecule as a whole is no longer rhodopsin, but a related molecule such as metarhodopsin. However, it remains a retinylidene protein. The chromophore then separates from the opsin, at which point the bare opsin is a retinylidene protein. Thus, the molecule remains a retinylidene protein throughout the phototransduction cycle. Structure All rhodopsins consi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Retinal
Retinal (also known as retinaldehyde) is a polyene chromophore. Retinal, bound to proteins called opsins, is the chemical basis of visual phototransduction, the light-detection stage of visual perception (vision). Some microorganisms use retinal to convert light into metabolic energy. In fact, a recent study suggests most living organisms on our planet ~3 billion years ago used retinal to convert sunlight into energy rather than chlorophyll. Since retinal absorbs mostly green light and transmits purple light, this gave rise to the Purple Earth Hypothesis. There are many forms of vitamin A — all of which are converted to retinal, which cannot be made without them. Retinal itself is considered to be a form of vitamin A when eaten by an animal. The number of different molecules that can be converted to retinal varies from species to species. Retinal was originally called retinene, and was renamed after it was discovered to be vitamin A aldehyde. Vertebrate animals ingest r ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Archaea
Archaea ( ; singular archaeon ) is a domain of single-celled organisms. These microorganisms lack cell nuclei and are therefore prokaryotes. Archaea were initially classified as bacteria, receiving the name archaebacteria (in the Archaebacteria kingdom), but this term has fallen out of use. Archaeal cells have unique properties separating them from the other two domains, Bacteria and Eukaryota. Archaea are further divided into multiple recognized phyla. Classification is difficult because most have not been isolated in a laboratory and have been detected only by their gene sequences in environmental samples. Archaea and bacteria are generally similar in size and shape, although a few archaea have very different shapes, such as the flat, square cells of '' Haloquadratum walsbyi''. Despite this morphological similarity to bacteria, archaea possess genes and several metabolic pathways that are more closely related to those of eukaryotes, notably for the enzymes invo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Halobacteria
Haloarchaea (halophilic archaea, halophilic archaebacteria, halobacteria) are a class of the Euryarchaeota, found in water saturated or nearly saturated with salt. Halobacteria are now recognized as archaea rather than bacteria and are one of the largest groups. The name 'halobacteria' was assigned to this group of organisms before the existence of the domain Archaea was realized, and while valid according to taxonomic rules, should be updated. Halophilic archaea are generally referred to as haloarchaea to distinguish them from halophilic bacteria. These microorganisms are among the halophile organisms, that they require high salt concentrations to grow, with most species requiring more than 2.0M NaCl for growth and survival. They are a distinct evolutionary branch of the Archaea distinguished by the possession of ether-linked lipids and the absence of murein in their cell walls. Haloarchaea can grow aerobically or anaerobically. Parts of the membranes of haloarchaea are purpli ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Channelrhodopsin
Channelrhodopsins are a subfamily of retinylidene proteins (rhodopsins) that function as light-gated ion channels. They serve as sensory photoreceptors in unicellular green algae, controlling phototaxis: movement in response to light. Expressed in cells of other organisms, they enable light to control electrical excitability, intracellular acidity, calcium influx, and other cellular processes (see optogenetics). Channelrhodopsin-1 (ChR1) and Channelrhodopsin-2 (ChR2) from the model organism ''Chlamydomonas reinhardtii'' are the first discovered channelrhodopsins. Variants that are sensitive to different colors of light or selective for specific ions (ACRs, KCRs) have been cloned from other species of algae and protists. History Phototaxis and photoorientation of microalgae have been studied over more than hundred years in many laboratories worldwide. In 1980, Ken Foster developed the first consistent theory about the functionality of algal eyes. He also analyzed published acti ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Channelrhodopsin-2
Channelrhodopsins are a subfamily of retinylidene proteins (rhodopsins) that function as light-gated ion channels. They serve as sensory photoreceptors in unicellular green algae, controlling phototaxis: movement in response to light. Expressed in cells of other organisms, they enable light to control electrical excitability, intracellular acidity, calcium influx, and other cellular processes (see optogenetics). Channelrhodopsin-1 (ChR1) and Channelrhodopsin-2 (ChR2) from the model organism ''Chlamydomonas reinhardtii'' are the first discovered channelrhodopsins. Variants that are sensitive to different colors of light or selective for specific ions (ACRs, KCRs) have been cloned from other species of algae and protists. History Phototaxis and photoorientation of microalgae have been studied over more than hundred years in many laboratories worldwide. In 1980, Ken Foster developed the first consistent theory about the functionality of algal eyes. He also analyzed published action s ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Endoplasmic Reticulum
The endoplasmic reticulum (ER) is, in essence, the transportation system of the eukaryotic cell, and has many other important functions such as protein folding. It is a type of organelle made up of two subunits – rough endoplasmic reticulum (RER), and smooth endoplasmic reticulum (SER). The endoplasmic reticulum is found in most eukaryotic cells and forms an interconnected network of flattened, membrane-enclosed sacs known as cisternae (in the RER), and tubular structures in the SER. The membranes of the ER are continuous with the outer nuclear membrane. The endoplasmic reticulum is not found in red blood cells, or spermatozoa. The two types of ER share many of the same proteins and engage in certain common activities such as the synthesis of certain lipids and cholesterol. Different types of cells contain different ratios of the two types of ER depending on the activities of the cell. RER is found mainly toward the nucleus of cell and SER towards the cell membrane or pl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Muscle Cell
A muscle cell is also known as a myocyte when referring to either a cardiac muscle cell (cardiomyocyte), or a smooth muscle cell as these are both small cells. A skeletal muscle cell is long and threadlike with many nuclei and is called a muscle fiber. Muscle cells (including myocytes and muscle fibers) develop from embryonic precursor cells called myoblasts. Myoblasts fuse to form multinucleated skeletal muscle cells known as syncytia in a process known as myogenesis. Skeletal muscle cells and cardiac muscle cells both contain myofibrils and sarcomeres and form a striated muscle tissue. Cardiac muscle cells form the cardiac muscle in the walls of the heart chambers, and have a single central nucleus. Cardiac muscle cells are joined to neighboring cells by intercalated discs, and when joined in a visible unit they are described as a ''cardiac muscle fiber''. Smooth muscle cells control involuntary movements such as the peristalsis contractions in the esophagus ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Natronomonas
''Natronomonas'' (common abbreviation ''Nmn.''). is a genus of the Halobacteriaceae.See the NCBIbr>webpage on Natronomonas Data extracted from the Description and significance ''Natronomonas pharaonis'' is an aerobic, extremely haloalkaliphilic archaeon that grows optimally in 3.5M sodium chloride and at pH 8.5, but is sensitive to high magnesium concentrations. Genome structure The genome of ''Natronomonas pharaonis'' consists of three circular replicons, the chromosome which is 2,595,221 bp in length, a typical haloarchaeal 131-kb plasmid, and a unique multicopy 23-kb plasmid. Its chromosome has a high G + C content (63.4%). Also, a high proportion of acidic amino acids (average 19.3%) is found in the proteins of ''N. pharaonis'' which results in low isoelectric points (average pI 4.6). This is considered to be one of the adaptive features of haloarchaea, which are known to apply the salt-in strategy (high internal salt concentrations) in order to survive in their ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Action Potential
An action potential occurs when the membrane potential of a specific cell location rapidly rises and falls. This depolarization then causes adjacent locations to similarly depolarize. Action potentials occur in several types of animal cells, called excitable cells, which include neurons, muscle cells, and in some plant cells. Certain endocrine cells such as pancreatic beta cells, and certain cells of the anterior pituitary gland are also excitable cells. In neurons, action potentials play a central role in cell-cell communication by providing for—or with regard to saltatory conduction, assisting—the propagation of signals along the neuron's axon toward synaptic boutons situated at the ends of an axon; these signals can then connect with other neurons at synapses, or to motor cells or glands. In other types of cells, their main function is to activate intracellular processes. In muscle cells, for example, an action potential is the first step in the chain of event ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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