Ras2
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Ras2
Ras2 is a ''Saccharomyces cerevisiae'' guanine nucleotide-binding protein (encoded by the RAS2 gene) which becomes activated by binding GTP when glucose is present in the environment. It affects growth regulation and starvation response. Modifications Ras2 becomes post-translationally modified in two ways, both being necessary for its activity: Upon activation, palmitoylation at its C terminus takes place and causes attachment from the cytoplasm to the plasma membrane. Farnesylation allows for efficient interaction with the downstream adenylate cyclase Cyr1p. In wild-type yeast deactivated Ras2 is transported to and degraded in the vacuole, a process for which Whi2 is essential. Disturbing this process leads to Ras2 accumulation at the mitochondrial membrane, a behavior that was not observed before. Ras2-cAMP-PKA pathway When activating the adenylate cyclase, Ras2 indirectly raises the cellular cAMP levels, thereby activating the PKA, by which in turn it is downregulated. Dow ...
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Saccharomyces Cerevisiae
''Saccharomyces cerevisiae'' () (brewer's yeast or baker's yeast) is a species of yeast (single-celled fungus microorganisms). The species has been instrumental in winemaking, baking, and brewing since ancient times. It is believed to have been originally isolated from the skin of grapes. It is one of the most intensively studied eukaryotic model organisms in molecular biology, molecular and cell biology, much like ''Escherichia coli'' as the model bacteria, bacterium. It is the microorganism behind the most common type of fermentation (biochemistry), fermentation. ''S. cerevisiae'' cells are round to ovoid, 5–10 micrometre, μm in diameter. It reproduces by budding. Many proteins important in human biology were first discovered by studying their Homology (biology), homologs in yeast; these proteins include cell cycle proteins, signaling proteins, and protein-processing enzymes. ''S. cerevisiae'' is currently the only yeast cell known to have Berkeley body, Berkeley bo ...
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Whi2
Whi2 or Whiskey 2 is a 55 kDa globular, cytoplasmatic scaffold protein in Saccharomyces cerevisiae, which plays an essential role in stress response pathways, apparently by passing input signals about nutrient availability on to stress responsive elements and autophagy/mitophagy mechanisms. It is encoded by a 1.46 kbp gene located on chromosome 15. Functional mechanism Upon complexing with plasma membrane associated phosphatase Psr1, Whi2 induces general stress response by dephosphorylating general stress response transcription factor Msn2. Whi2 is essential for Msn2 activity, moreover activation by Whi2 is dominant and independent of the PKA and TOR activation pathways. Additionally, experiments are suggesting Whi2 for playing a role in Ras2 Ras2 is a ''Saccharomyces cerevisiae'' guanine nucleotide-binding protein (encoded by the RAS2 gene) which becomes activated by binding GTP when glucose is present in the environment. It affects growth regulation and starvation response. M ...
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Guanosine Triphosphate
Guanosine-5'-triphosphate (GTP) is a purine nucleoside triphosphate. It is one of the building blocks needed for the synthesis of RNA during the transcription process. Its structure is similar to that of the guanosine nucleoside, the only difference being that nucleotides like GTP have phosphates on their ribose sugar. GTP has the guanine nucleobase attached to the 1' carbon of the ribose and it has the triphosphate moiety attached to ribose's 5' carbon. It also has the role of a source of energy or an activator of substrates in metabolic reactions, like that of ATP, but more specific. It is used as a source of energy for protein synthesis and gluconeogenesis. GTP is essential to signal transduction, in particular with G-proteins, in second-messenger mechanisms where it is converted to guanosine diphosphate (GDP) through the action of GTPases. Uses Energy transfer GTP is involved in energy transfer within the cell. For instance, a GTP molecule is generated by one of the enz ...
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Saccharomyces Genome Database
The ''Saccharomyces'' Genome Database (SGD) is a scientific database of the molecular biology and genetics of the yeast ''Saccharomyces cerevisiae'', which is commonly known as baker's or budding yeast. ''Saccharomyces'' Genome Database The SGD provides Internet access to the complete ''Saccharomyces cerevisiae'' genomic DNA sequence, its genes and their products, the phenotypes of its mutants, and the literature supporting these data. In the peer-reviewed literature report, experiment result on function and interaction of yeast genes are extracted by high-quality manual curation and integrated within a well-developed database. The data are combined with quality high-throughput results and post on Locus Summary pages which is a powerful query engine and rich genome browser. Based on the complexity of information collection, multiple bioinformatic tools are used to integrate information and allow productive discovery of new biological details. The gold standard for functional desc ...
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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 conta ...
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Adenylate Cyclase
Adenylate cyclase (EC 4.6.1.1, also commonly known as adenyl cyclase and adenylyl cyclase, abbreviated AC) is an enzyme with systematic name ATP diphosphate-lyase (cyclizing; 3′,5′-cyclic-AMP-forming). It catalyzes the following reaction: :ATP = 3′,5′-cyclic AMP + diphosphate It has key regulatory roles in essentially all cells. It is the most polyphyletic known enzyme: six distinct classes have been described, all catalyzing the same reaction but representing unrelated gene families with no known sequence or structural homology. The best known class of adenylyl cyclases is class III or AC-III (Roman numerals are used for classes). AC-III occurs widely in eukaryotes and has important roles in many human tissues. All classes of adenylyl cyclase catalyse the conversion of adenosine triphosphate (ATP) to 3',5'-cyclic AMP (cAMP) and pyrophosphate.Magnesium ions are generally required and appear to be closely involved in the enzymatic mechanism. The cAMP produced by AC t ...
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Cyclic Adenosine Monophosphate
Cyclic adenosine monophosphate (cAMP, cyclic AMP, or 3',5'-cyclic adenosine monophosphate) is a second messenger important in many biological processes. cAMP is a derivative of adenosine triphosphate (ATP) and used for intracellular signal transduction in many different organisms, conveying the cAMP-dependent pathway. History Earl Sutherland of Vanderbilt University won a Nobel Prize in Physiology or Medicine in 1971 "for his discoveries concerning the mechanisms of the action of hormones", especially epinephrine, via second messengers (such as cyclic adenosine monophosphate, cyclic AMP). Synthesis Cyclic adenosine monophosphate, AMP is synthesized from Adenosine triphosphate, ATP by adenylate cyclase located on the inner side of the plasma membrane and anchored at various locations in the interior of the cell. Adenylate cyclase is ''activated'' by a range of signaling molecules through the activation of adenylate cyclase stimulatory G (Gs alpha subunit, Gs)-protein-coupled recep ...
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Protein Kinase A
In cell biology, protein kinase A (PKA) is a family of enzymes whose activity is dependent on cellular levels of cyclic AMP (cAMP). PKA is also known as cAMP-dependent protein kinase (). PKA has several functions in the cell, including regulation of glycogen, sugar, and lipid metabolism. It should not be confused with 5'-AMP-activated protein kinase (AMP-activated protein kinase). History Protein kinase A, more precisely known as adenosine 3',5'-monophosphate (cyclic AMP)-dependent protein kinase, abbreviated to PKA, was discovered by chemists Edmond H. Fischer and Edwin G. Krebs in 1968. They won the Nobel Prize in Physiology or Medicine in 1992 for their work on phosphorylation and dephosphorylation and how it relates to PKA activity. PKA is one of the most widely researched protein kinases, in part because of its uniqueness; out of 540 different protein kinase genes that make up the human kinome, only one other protein kinase, casein kinase 2, is known to exist in a physio ...
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Msn2
MSN (meaning Microsoft Network) is a web portal and related collection of Internet services and apps for Windows and mobile devices, provided by Microsoft and launched on August 24, 1995, alongside the release of Windows 95. The Microsoft Network was initially a subscription-based dial-up online service that later became an Internet service provider named MSN Dial-up. At the same time, the company launched a new web portal named Microsoft Internet Start and set it as the first default home page of Internet Explorer, its web browser. In 1998, Microsoft renamed and moved this web portal to the domain name www.msn.com, where it has remained. In addition to its original MSN Dial-up service, Microsoft has used the 'MSN' brand name for a wide variety of products and services over the years, notably Hotmail (later Outlook.com), Messenger (which was once synonymous with 'MSN' in Internet slang and has now been replaced by Skype), and its web search engine, which is now Bing, and se ...
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Proteins
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residues ...
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