Marine unicellular Cyanobacteria of the Synechococcus group occupy an important position at the base of the marine food web. They are abundant in the world's oceans and as a result are major primary producers on a global scale and one of the most numerous genomes on earth Synechococcus is the main source of primary productin in oligotrophic, pelagic waters. Many genera of Cyanobacteria thrive in nutrient-rich, eutrophic environments, and are, as such considered indicators of eutrophication, which currently troubles many aquatic ecosystems. Synechococcus sp. strain WH8102 is a motile strain that can be grown in both natural and artificial seawater liquid media as well as on plates and is amenable to biochemical and genetic manipulation. It dwells in the most[..]

Marine unicellular Cyanobacteria of the Synechococcus group occupy an important position at the base of the marine food web. They are abundant in the world's oceans and as a result are major primary producers on a global scale and one of the most numerous genomes on earth. They have the ability to acquire major nutrients and trace metals at the submicromolar concentrations found in the oligotrophic open seas, and their light-harvesting apparatus is uniquely adapted to the spectral quality of light in the ocean (Ref.1). Glutathione metabolism in Synechococcus sp. involves both the synthesis of Glutathione and its catabolism. Glutathione is a small molecule found in almost every cell. It cannot enter most cells directly and therefore must be made available inside the[..]

Glutathione is a sulfhydryl (-SH) antioxidant, antitoxin, and enzyme cofactor. It is ubiquitous in animals, plants, and microorganisms, and being water soluble is found mainly in the cell cytosol and other aqueous phases of the living system. It has been assigned several cellular functions, including protection against oxidative damage, maintenance of a reducing cellular thiol-disulfide balance, electron donation for a number of enzymes, protection of protein sulfhydryls from irreversible oxidation, and detoxification of foreign compounds. Glutathione is synthesized enzymatically from its constituent amino acids in two consecutive reactions. GSA1 (Glutathione Synthetase or GSH2) catalyzes the second step and it occurs in two different forms in Schizosaccharomyces[..]

Vibrio vulnificus is an etiologic agent for severe human infection acquired through wounds or contaminated seafood. This is a lactose-fermenting, halophilic, Gram-negative, opportunistic pathogen, is found in estuarine environments and is associated with various marine species such as plankton, shellfish (Oysters, Clams, and Crabs), and finfish (Ref.1). V. vulnificus belong to the Gamma-group of Proteobacteria, and it shares morphological and biochemical characteristics with other human Vibrio pathogens, including Vibrio cholerae and Vibrio parahaemolyticus. It is divided into three biotypes according to its different biochemical and biological properties. The genome of Biotype-1 strain, V. vulnificus YJ016, contains two chromosomes (Ref.2).Glutathione is a tripeptide,[..]

Glutathione is a sulfhydryl (-SH) antioxidant, antitoxin, and enzyme cofactor. It is ubiquitous in animals, plants, and microorganisms, and being water soluble is found mainly in the cell cytosol and other aqueous phases of the living system. It cannot enter most cells directly and therefore must be made available inside the cell from its three constituent amino acids: Glycine, Glutamate and Cysteine. The rate at which glutathione can be made depends on the availability of Cysteine, which is relatively scarce in foodstuffs. It often attains millimolar levels inside cells, which makes it one of the most highly concentrated intracellular antioxidants. Glutathione exists in two forms. The antioxidant "reduced Glutathione" tripeptide is conventionally called[..]

Glutathione is a sulfhydryl (-SH) antioxidant, antitoxin, and enzyme cofactor. It is ubiquitous in animals, plants, and microorganisms, and being water soluble is found mainly in the cell cytosol and other aqueous phases of the living system. Glutathione is a tripeptide composed of Glutamate, Cysteine and Glycine that has numerous important functions within cells. It is homeostatically controlled, both inside the cell and outside and often attains millimolar levels inside cells, which makes it one of the most highly concentrated intracellular antioxidants. Glutathione exists in two forms. The antioxidant "reduced Glutathione" tripeptide is conventionally called Glutathione and abbreviated Gsh; the oxidized form is a sulfur-sulfur linked compound, known as[..]

Zymomonas mobilis is an ethanologenic microorganism used for the production of fuel ethanol (Ref.1). Glutathione metabolism in Z. mobilis involves both the synthesis of Glutathione and its catabolism. Glutathione is a small molecule found in almost every cell. It cannot enter most cells directly and therefore must be made available inside the cell from its three constituent amino acids: Glycine, Glutamate and Cysteine. The rate at which Glutathione can be made depends on the availability of Cysteine, which is relatively scarce in foodstuffs. Furthermore, the Cysteine molecule has a sulfur-containing portion which gives the whole Glutathione molecule its ‘biochemical activity’, i.e. its ability to carry out the vitally important functions. Cysteine can also[..]

Glutathione is a sulfhydryl (-SH) antioxidant, antitoxin, and enzyme cofactor. It is ubiquitous in animals, plants, and microorganisms, and being water soluble is found mainly in the cell cytosol and other aqueous phases of the living system. It cannot enter most cells directly and therefore must be made available inside the cell from its three constituent amino acids: Glycine, Glutamate and Cysteine. The rate at which glutathione can be made depends on the availability of Cysteine, which is relatively scarce in foodstuffs. Furthermore, the Cysteine molecule has a sulfur-containing portion which gives the whole Glutathione molecule its ‘biochemical activity’. Cysteine can also enter the Glutathione metabolism through several other metabolic pathways like[..]

Simple eukaryotes such as yeasts and molds encode multiple PAKs (p21-Activated Kinases) that, like their orthologs in other systems, act downstream of Rho-family GTPases. All PAKs contain an N-terminal PBD (p21 GTPase-Binding-Domain), which confers binding to small GTPases such as CDC42 (Cell Division Cycle-42) or Rac, and a C-terminal protein kinase domain, but they do not bind to Rho, Ras, or other small G-proteins. CDC42 and Rac bind in a GTP-dependent fashion to a highly conserved sequence, referred to as the CRIB (CDC42 and Rac Interactive Binding) domain, found in the N-terminal regulatory domains of all characterized PAKs (Ref.1).The fission yeast Schizosaccharomyces pombe encodes two PAK kinases–Pak1/Shk1 and Pak2/Shk2–both of which, like their[..]

Glutathione is a sulfhydryl (-SH) antioxidant, antitoxin, and enzyme cofactor. It is ubiquitous in animals, plants, and microorganisms, and being water soluble is found mainly in the cell cytosol and other aqueous phases of the living system. It is composed of Glutamate, Cysteine and Glycine that has numerous important functions within cells. Glutathione is homeostatically controlled, both inside the cell and outside. It often attains millimolar levels inside cells, which makes it one of the most highly concentrated intracellular antioxidants. Glutathione exists in two forms. The antioxidant "reduced Glutathione" tripeptide is conventionally called Glutathione and abbreviated Gsh; the oxidized form is a sulfur-sulfur linked compound, known as Glutathione[..]

Axon regeneration is arrested in the injured CNS (Central Nervous System) by axon growth-inhibitory ligands expressed in oligodendrocytes/myelin and reactive astrocytes in the lesion and by fibroblasts in scar tissue. Growth cone receptors bind inhibitory ligands, activating a Rho-family GTPase intracellular signaling pathway that disrupts the actin cytoskeleton inducing growth cone collapse/repulsion. The known inhibitory ligands include Eph (Ephrins) expressed on astrocyte/fibroblast membranes; the myelin/oligodendrocyte-derived growth inhibitors Nogo, MAG (Myelin-Associated Glycoprotein), and OMGP (Oligodendrocyte Myelin Glycoprotein); and membrane-bound Sema (Semaphorins) produced by meningeal fibroblasts invading the scar (Ref.1).Myelin-associated inhibitory[..]

Glutathione is a sulfhydryl (-SH) antioxidant, antitoxin, and enzyme cofactor. It is ubiquitous in animals, plants, and microorganisms, and being water soluble is found mainly in the cell cytosol and other aqueous phases of the living system. Glutathione is a tripeptide composed of Glutamate, Cysteine and Glycine that has numerous important functions within cells. Glutathione is homeostatically controlled, both inside the cell and outside. It often attains millimolar levels inside cells, which makes it one of the most highly concentrated intracellular antioxidants. Glutathione exists in two forms. The antioxidant "reduced Glutathione" tripeptide is conventionally called Glutathione. The oxidized form is a sulfur-sulfur linked compound, known as Glutathione[..]