|
Translational Regulation
Translational regulation refers to the control of the levels of protein synthesized from its mRNA. This regulation is vastly important to the cellular response to stressors, growth cues, and differentiation. In comparison to transcriptional regulation, it results in much more immediate cellular adjustment through direct regulation of protein concentration. The corresponding mechanisms are primarily targeted on the control of ribosome recruitment on the initiation codon, but can also involve modulation of peptide elongation, termination of protein synthesis, or ribosome biogenesis. While these general concepts are widely conserved, some of the finer details in this sort of regulation have been proven to differ between prokaryotic and eukaryotic organisms. In prokaryotes Initiation Initiation of translation is regulated by the accessibility of ribosomes to the Shine-Dalgarno sequence. This stretch of four to nine purine residues are located upstream the initiation codon and ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Regulation Of Gene Expression
Regulation of gene expression, or gene regulation, includes a wide range of mechanisms that are used by cells to increase or decrease the production of specific gene products (protein or RNA). Sophisticated programs of gene expression are widely observed in biology, for example to trigger developmental pathways, respond to environmental stimuli, or adapt to new food sources. Virtually any step of gene expression can be modulated, from Transcriptional regulation, transcriptional initiation, to RNA processing, and to the post-translational modification of a protein. Often, one gene regulator controls another, and so on, in a gene regulatory network. Gene regulation is essential for viruses, prokaryotes and eukaryotes as it increases the versatility and adaptability of an organism by allowing the cell to express protein when needed. Although as early as 1951, Barbara McClintock showed interaction between two genetic loci, Activator (''Ac'') and Dissociator (''Ds''), in the color f ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Irreversible Process
In thermodynamics, an irreversible process is a thermodynamic processes, process that cannot be undone. All complex natural processes are irreversible, although a phase transition at the coexistence temperature (e.g. melting of ice cubes in water) is well approximated as reversible. A change in the thermodynamic state of a system and all of its surroundings cannot be precisely restored to its initial state by infinitesimal changes in some property of the system without expenditure of energy. A system that undergoes an irreversible process may still be capable of returning to its initial state. Because entropy is a state function, the change in entropy of the system is the same whether the process is reversible or irreversible. However, the impossibility occurs in restoring the Environment (systems), environment to its own initial conditions. An irreversible process increases the total entropy of the system and its surroundings. The second law of thermodynamics can be used to dete ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
EEF2
Eukaryotic elongation factor 2 is a protein that in humans is encoded by the ''EEF2'' gene. It is the archaeal and eukaryotic counterpart of bacterial EF-G. This gene encodes a member of the GTP-binding translation elongation factor family. This protein is an essential factor for protein synthesis. It promotes the GTP-dependent translocation of the ribosome. This protein is completely inactivated by EF-2 kinase phosphorylation. aEF2/eEF2 found in most archaea and eukaryotes, including humans, contains a post translationally modified histidine diphthamide. It is the target of diphtheria toxin (from ''Corynebacterium diphtheriae''), and exotoxin A (from ''Pseudomonas aeruginosa ''Pseudomonas aeruginosa'' is a common Bacterial capsule, encapsulated, Gram-negative bacteria, Gram-negative, Aerobic organism, aerobic–facultative anaerobe, facultatively anaerobic, Bacillus (shape), rod-shaped bacteria, bacterium that can c ...''). The inactivation of EF-2 by toxins inhibits pr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nuclear Membrane
The nuclear envelope, also known as the nuclear membrane, is made up of two lipid bilayer polar membrane, membranes that in eukaryotic cells surround the Cell nucleus, nucleus, which encloses the genome, genetic material. The nuclear envelope consists of two lipid bilayer membranes: an inner nuclear membrane and an outer nuclear membrane. The space between the membranes is called the perinuclear space. It is usually about 10–50 Nanometre, nm wide. The outer nuclear membrane is continuous with the endoplasmic reticulum membrane. The nuclear envelope has many nuclear pores that allow materials to move between the cytosol and the nucleus. Intermediate filament proteins called lamins form a structure called the nuclear lamina on the inner aspect of the inner nuclear membrane and give structural support to the nucleus. Structure The nuclear envelope is made up of two lipid bilayer membranes, an inner nuclear membrane and an outer nuclear membrane. These membranes are connected t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Gcn2
GCN2 (general control nonderepressible 2) is a serine/threonine-protein kinase that senses amino acid deficiency through binding to uncharged transfer RNA (tRNA). It plays a key role in modulating amino acid metabolism as a response to nutrient deprivation. Introduction GCN2 is the only known eukaryotic initiation factor 2α kinase (eIF2α) in ''Saccharomyces cerevisiae''. It inactivates eIF2α by phosphorylation at Serine 51 under conditions of amino acid deprivation, resulting in repression of general protein synthesis whilst allowing selected mRNA, such as the transcription factor GCN4, to be translated due to regions upstream of the coding sequence. Elevated levels of GCN4 stimulate the expression of amino acid biosynthetic genes, which code for enzymes required to synthesize all 20 major amino acids. Structure Protein kinase GCN2 is a multidomain protein and its C-terminus contains a region homologous to histidyl-tRNA synthetase (HisRS) next to the kinase catalytic moi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Kinase
A protein kinase is a kinase which selectively modifies other proteins by covalently adding phosphates to them ( phosphorylation) as opposed to kinases which modify lipids, carbohydrates, or other molecules. Phosphorylation usually results in a functional change of the target protein ( substrate) by changing enzyme activity, cellular location, or association with other proteins. The human genome contains about 500 protein kinase genes and they constitute about 2% of all human genes. There are two main types of protein kinase. The great majority are serine/threonine kinases, which phosphorylate the hydroxyl groups of serines and threonines in their targets. Most of the others are tyrosine kinases, although additional types exist. Protein kinases are also found in bacteria and plants. Up to 30% of all human proteins may be modified by kinase activity, and kinases are known to regulate the majority of cellular pathways, especially those involved in signal transduction. Chemical ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phosphorylation
In biochemistry, phosphorylation is described as the "transfer of a phosphate group" from a donor to an acceptor. A common phosphorylating agent (phosphate donor) is ATP and a common family of acceptor are alcohols: : This equation can be written in several ways that are nearly equivalent that describe the behaviors of various protonated states of ATP, ADP, and the phosphorylated product. As is clear from the equation, a phosphate group per se is not transferred, but a phosphoryl group (PO3-). Phosphoryl is an electrophile. This process and its inverse, dephosphorylation, are common in biology. Text was copied from this source, which is available under a Creative Commons Attribution 4.0 International License. Protein phosphorylation often activates (or deactivates) many enzymes. During respiration Phosphorylation is essential to the processes of both anaerobic and aerobic respiration, which involve the production of adenosine triphosphate (ATP), the "high-energy" exc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
EIF2
Eukaryotic Initiation Factor 2 (eIF2) is a eukaryotic initiation factor. It is required for most forms of eukaryotic translation initiation. eIF2 mediates the binding of tRNAiMet to the ribosome in a GTP-dependent manner. eIF2 is a heterotrimer consisting of an alpha (also called subunit 1, EIF2S1), a beta (subunit 2, EIF2S2), and a gamma (subunit 3, EIF2S3) subunit. Once the initiation phase has completed, eIF2 is released from the ribosome bound to GDP as an inactive binary complex. To participate in another round of translation initiation, this GDP must be exchanged for GTP. Function eIF2 is an essential factor for protein synthesis that forms a ternary complex (TC) with GTP and the initiator Met- tRNAiMet. After its formation, the TC binds the 40S ribosomal subunit to form the 43S preinitiation complex (43S PIC). 43S PIC assembly is believed to be stimulated by the initiation factors eIF1, eIF1A, and the eIF3 complex according to ''in vitro'' experiments. The 43 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
5' Cap
In molecular biology, the five-prime cap (5′ cap) is a specially altered nucleotide on the 5′ end of some primary transcripts such as precursor messenger RNA. This process, known as mRNA capping, is highly regulated and vital in the creation of stable and mature messenger RNA able to undergo translation during protein synthesis. Mitochondrial mRNA and chloroplastic mRNA are not capped. Structure In eukaryotes, the 5′ cap (cap-0), found on the 5′ end of an mRNA molecule, consists of a guanine nucleotide connected to mRNA via an unusual 5′ to 5′ triphosphate linkage. This guanosine is methylated on the 7 position directly after capping ''in vivo'' by a methyltransferase. It is referred to as a 7-methylguanylate cap, abbreviated m7G. The Cap-0 is the base cap structure, however, the first and second transcribed nucleotides can also be 2' O-methylated, leading to the Cap-1 and Cap-2 structures, respectively. This is more common in higher eukaryotes an ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
EIF4E
Eukaryotic translation initiation factor 4E, also known as eIF4E, is a protein in humans encoded by the ''EIF4E'' gene. eIF4E plays a central role in translation initiation and is involved in regulating protein synthesis. Its activity influences a range of biological processes and disease states, making it an important target for therapeutic development, particularly in disorders characterized by aberrant protein production. Discovery eIF4E was discovered as a cytoplasmic cap binding protein functioning in translation by Witold Filipowicz at al. In 1976. Two years later, in 1978, Sonenberg et al. confirmed Filipowicz et al.’s findings by repeating the same experiments and adding a crosslinking chemical to increase the stability of the mRNA-protein complex. This has been confirmed by numerous scientists in their published articles such as Katherine L. B. Borden, Michael J. Osborne and Katherine L.B. Borden. Structure Most eukaryote, eukaryotic cellular Messenger RNA, mRNAs ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cap-dependent Initiation
Eukaryotic translation is the biological process by which messenger RNA is translated into proteins in eukaryotes. It consists of four phases: initiation, elongation, termination, and recapping. Initiation Translation initiation is the process by which the ribosome and its associated factors bind to an mRNA and are assembled at the start codon. This process is defined as either cap-dependent, in which the ribosome binds initially at the 5' cap and then travels to the stop codon, or as cap-independent, where the ribosome does not initially bind the 5' cap. Cap-dependent initiation Initiation of translation usually involves the interaction of certain key proteins, the initiation factors, with a special tag bound to the 5'-end of an mRNA molecule, the 5' cap, as well as with the 5' UTR. These proteins bind the small (40S) ribosomal subunit and hold the mRNA in place. eIF3 is associated with the 40S ribosomal subunit and plays a role in keeping the large (60S) ribosomal subunit fr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Eukaryotic Initiation Factor
Eukaryotic initiation factors (eIFs) are proteins or protein complexes involved in the initiation phase of eukaryotic translation. These proteins help stabilize the formation of ribosomal preinitiation complexes around the start codon and are an important input for post-transcription gene regulation. Several initiation factors form a complex with the small 40S ribosomal subunit and Met- tRNAiMet called the 43S preinitiation complex (43S PIC). Additional factors of the eIF4F complex (eIF4A, E, and G) recruit the 43S PIC to the five-prime cap structure of the mRNA, from which the 43S particle scans 5'-->3' along the mRNA to reach an AUG start codon. Recognition of the start codon by the Met-tRNAiMet promotes gated phosphate and eIF1 release to form the 48S preinitiation complex (48S PIC), followed by large 60S ribosomal subunit recruitment to form the 80S ribosome. There exist many more eukaryotic initiation factors than prokaryotic initiation factors, reflecting the gre ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
