EIF4A
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EIF4A
The eukaryotic initiation factor-4A (eIF4A) family consists of 3 closely related proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. Background The mechanisms governing the basic subsistence of eukaryotic cells are immensely complex; it is therefore unsurprising that regulation occurs at a number of stages of protein synthesis – the regulation of translation has become a well-studied field. Human translational control is of increasing research interest as it has connotations in a range of diseases. Orthologs of many of the factors involved in human translation are shared by a range of eukaryotic organisms; some of which are used as model systems for the investigation of translation initiation and elongation, for example: sea urchin eggs upon fertilization, rodent brain and rabbit reticulocytes. Monod and Jacob were among the f ...
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EIF4A2
Eukaryotic initiation factor 4A-II is a protein that in humans is encoded by the ''EIF4A2'' gene In biology, the word gene (from , ; "...Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''generation'' or ''birth'' or ''gender'') can have several different meanings. The Mendelian gene is a ba .... References Further reading * * * * * * * * * * External links

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EIF4A1
Eukaryotic initiation factor 4A-I (also known as eIF4A1 or DDX2A) is a 46 kDa cytosolic protein that, in humans, is encoded by the ''EIF4A1'' gene, which is located on chromosome 17. It is the most prevalent member of the eIF4A family of ATP-dependant RNA helicases, and plays a critical role in the initiation of cap-dependent eukaryotic protein translation as a component of the eIF4F translation initiation complex. eIF4A1 unwinds the secondary structure of RNA within the 5'-UTR of mRNA, a critical step necessary for the recruitment of the 43S preinitiation complex, and thus the translation of protein in eukaryotes. It was first characterized in 1982 by Grifo, ''et al.'', who purified it from rabbit reticulocyte lysate. Background The regulation of the translation of mRNA transcripts into protein is one of the best ways that a cell can alter its response to its environment, as changes to the transcription of genes often takes considerably more time to be enacted. Protein trans ...
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DEAD Box
Death is the irreversible cessation of all biological functions that sustain an organism. For organisms with a brain, death can also be defined as the irreversible cessation of functioning of the whole brain, including brainstem, and brain death is sometimes used as a legal definition of death. The remains of a former organism normally begin to decompose shortly after death. Death is an inevitable process that eventually occurs in almost all organisms. Death is generally applied to whole organisms; the similar process seen in individual components of an organism, such as cells or tissues, is necrosis. Something that is not considered an organism, such as a virus, can be physically destroyed but is not said to die. As of the early 21st century, over 150,000 humans die each day, with ageing being by far the most common cause of death. Many cultures and religions have the idea of an afterlife, and also may hold the idea of judgement of good and bad deeds in one's life (heaven, ...
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Juri Rappsilber
Juri Rappsilber (born 1971) is a German chemist in the area of mass spectrometry and proteomics. Career Rappsilber studied chemistry at the Technical University of Berlin, University of Strathclyde, and with Tom Rapoport, Harvard Medical School. In 2001, he earned his Ph.D. in Proteomics jointly from EMBL Heidelberg and the Goethe University Frankfurt working in the laboratory of Matthias Mann on the mass spectrometric analysis of protein complexes, externally supervised by Michael Karas. He followed Mann to the University of Southern Denmark and completed a postdoctoral fellowship before starting his independent career at IFOM - FIRC Institute for Molecular Oncology, Milan in 2003. In 2006, he joined the Wellcome Trust Centre for Cell Biology in the Institute of Cell Biology at the University of Edinburgh. In 2009, he became a senior research fellow of the Wellcome Trust, in 2010 he was appointed Professor of Proteomics in Edinburgh. Since 2011, he has been Full Professor ...
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Start Codon
The start codon is the first codon of a messenger RNA (mRNA) transcript translated by a ribosome. The start codon always codes for methionine in eukaryotes and Archaea and a N-formylmethionine (fMet) in bacteria, mitochondria and plastids. The most common start codon is AUG (i.e., ATG in the corresponding DNA sequence). The start codon is often preceded by a 5' untranslated region ( 5' UTR). In prokaryotes this includes the ribosome binding site. Alternative start codons Alternative start codons are different from the standard AUG codon and are found in both prokaryotes (bacteria and archaea) and eukaryotes. Alternate start codons are still translated as Met when they are at the start of a protein (even if the codon encodes a different amino acid otherwise). This is because a separate transfer RNA (tRNA) is used for initiation. Eukaryotes Alternate start codons (non-AUG) are very rare in eukaryotic genomes. However, naturally occurring non-AUG start codons have been rep ...
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Cereal Germ
Cereal germ or Wheat germ: The germ of a cereal is the reproductive part that germinates to grow into a plant; it is the embryo of the seed. Along with bran, germ is often a by-product of the milling that produces refined grain products. Cereal grains and their components, such as wheat germ oil, rice bran oil, and maize bran, may be used as a source from which vegetable oil is extracted, or used directly as a food ingredient. The germ is retained as an integral part of whole-grain foods. Non-whole grain methods of milling are intended to isolate the endosperm, which is ground into flour, with removal of both the husk (bran) and the germ. Removal of bran is aimed at producing a flour with a white rather than a brown color, and eliminating fiber, which reduces nutrition. The germ is rich in polyunsaturated fats (which have a tendency to oxidize and become rancid on storage) and so germ removal improves the storage qualities of flour. Wheat germ Wheat germ or wheatgerm is a co ...
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EIF4H
Eukaryotic translation initiation factor 4H is a protein that in humans is encoded by the ''EIF4H'' gene. This gene encodes one of the translation initiation factors, which function to stimulate the initiation of protein synthesis at the level of mRNA utilization. This gene is deleted in Williams syndrome, a multisystem developmental disorder caused by the deletion of contiguous genes at 7q11.23. Alternative splicing of this gene generates 2 transcript variants. EIF4H appears analogous to drr-2 in C. elegans which regulates the mTOR pathway The mammalian target of rapamycin (mTOR), also referred to as the mechanistic target of rapamycin, and sometimes called FK506-binding protein 12-rapamycin-associated protein 1 (FRAP1), is a kinase that in humans is encoded by the ''MTOR'' gene. ... and affects longevity. References Further reading * * * * * * * * * * * * * * * External links

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EIF4B
Eukaryotic translation initiation factor 4B is a protein that in humans is encoded by the ''EIF4B'' gene. Interactions eIF4B has been shown to interact with and stimulate the activity of eIF4A and bind to the eIF3 complex through the eIF3A subunit. This interaction results in the recruitment of the eukaryotic small ribosomal subunit (40S) to the mRNA which will in turn set the stage for the later steps leading to elongation. See also *Eukaryotic translation *eIF4F Eukaryotic initiation factor 4F (eIF4F) is a heterotrimeric protein complex that binds the 5' cap of messenger RNAs (mRNAs) to promote eukaryotic translation initiation. The eIF4F complex is composed of three non-identical subunits: the DEAD- ... References Further reading

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EIF4E
Eukaryotic translation initiation factor 4E, also known as eIF4E, is a protein that in humans is encoded by the ''EIF4E'' gene. Structure and function Most eukaryotic cellular mRNAs are blocked at their 5'-ends with the 7-methyl-guanosine five-prime cap structure, m7GpppX (where X is any nucleotide). This structure is involved in several cellular processes including enhanced translational efficiency, splicing, mRNA stability, and RNA nuclear export. eIF4E is a eukaryotic translation initiation factor involved in directing ribosomes to the cap structure of mRNAs. It is a 24-kD polypeptide that exists as both a free form and as part of the eIF4F pre-initiation complex. Almost all cellular mRNA require eIF4E in order to be translated into protein. The eIF4E polypeptide is the rate-limiting component of the eukaryotic translation apparatus and is involved in the mRNA-ribosome binding step of eukaryotic protein synthesis. The other subunits of eIF4F are a 47-kD polypeptide, terme ...
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EIF3
Eukaryotic initiation factor 3 (eIF3) is a multiprotein complex that functions during the initiation phase of eukaryotic translation. It is essential for most forms of Eukaryotic translation#Cap-dependent initiation, cap-dependent and Eukaryotic translation#cap-independent, cap-independent translation initiation. In humans, eIF3 consists of 13 nonidentical subunits (eIF3a-m) with a combined molecular weight of ~800 kDa, making it the largest Eukaryotic initiation factor, translation initiation factor. The eIF3 complex is broadly conserved across eukaryotes, but the conservation of individual subunits varies across organisms. For instance, while most mammalian eIF3 complexes are composed of 13 subunits, Saccharomyces cerevisiae, budding yeast's eIF3 has only six subunits (eIF3a, b, c, g, i, j). Function eIF3 stimulates nearly all steps of translation initiation. eIF3 also appears to participate in other phases of translation, such as recycling, where it promotes the splitting of ...
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EIF4F
Eukaryotic initiation factor 4F (eIF4F) is a heterotrimeric protein complex that binds the 5' cap of messenger RNAs (mRNAs) to promote eukaryotic translation initiation. The eIF4F complex is composed of three non-identical subunits: the DEAD-box RNA helicase eIF4A, the cap-binding protein eIF4E, and the large "scaffold" protein eIF4G. The mammalian eIF4F complex was first described in 1983, and has been a major area of study into the molecular mechanisms of cap-dependent translation initiation ever since. Function eIF4F is important for recruiting the small ribosomal subunit (40S) to the 5' cap of mRNAs during cap-dependent translation initiation. Components of the complex are also involved in cap-independent translation initiation; for instance, certain viral proteases cleave eIF4G to remove the eIF4E-binding region, thus inhibiting cap-dependent translation. Structure Structures of eIF4F components have been solved individually and as partial complexes by a variety ...
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Secondary Structure
Protein secondary structure is the three dimensional conformational isomerism, form of ''local segments'' of proteins. The two most common Protein structure#Secondary structure, secondary structural elements are alpha helix, alpha helices and beta sheets, though beta turns and omega loops occur as well. Secondary structure elements typically spontaneously form as an intermediate before the protein protein folding, folds into its three dimensional protein tertiary structure, tertiary structure. Secondary structure is formally defined by the pattern of hydrogen bonds between the Amine, amino hydrogen and carboxyl oxygen atoms in the peptide backbone chain, backbone. Secondary structure may alternatively be defined based on the regular pattern of backbone Dihedral angle#Dihedral angles of proteins, dihedral angles in a particular region of the Ramachandran plot regardless of whether it has the correct hydrogen bonds. The concept of secondary structure was first introduced by Kaj Ulrik ...
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