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Protein synthesis - Biology-Online Dictionary

Antoun A, Pavlov MY, Lovmar M and Ehrenberg M (2006a) How initiation factors tune the rate of initiation of protein synthesis in bacteria. EMBO Journal 25: 2539–2550.

Antoun A, Pavlov MY, Lovmar M and Ehrenberg M (2006b) How initiation factors maximize the accuracy of tRNA selection in initiation of bacterial protein synthesis. Molecular Cell 23: 183–193.

Protein folding in the endoplasmic reticulum Protein synthesis

Ribosomes - Protein Synthesis - Cronodon

The initial interaction of mRNA with the protein synthesis machinery presumably involves recognition of the 5′-cap (m7GpppN), although it is not clear at the present time whether this recognition is by eIF-4E or eIF-4F. This process has been studied by direct fluorescence titration experiments. The equilibrium constants for the formation of the binary protein:m7GpppG, protein:mRNA, and protein:protein complexes as well as well as the ternary mRNA:eIF-4E:eIF-4A complexes were measured. These studies show, for the first time, direct evidence for an eIF-4A:eIF-4E interaction. In contrast to earlier studies, we show that the affinity of eIF-4E and eIF-4F for globin mRNA is similar. Furthermore, the relative affinities of mRNA analogs (capped oligonucleotides) for these initiation factors indicate that the cap is the predominant feature recognized for binding, but other features also contribute to the eIF-4E:mRNA interaction.

N2 - The initial interaction of mRNA with the protein synthesis machinery presumably involves recognition of the 5′-cap (m7GpppN), although it is not clear at the present time whether this recognition is by eIF-4E or eIF-4F. This process has been studied by direct fluorescence titration experiments. The equilibrium constants for the formation of the binary protein:m7GpppG, protein:mRNA, and protein:protein complexes as well as well as the ternary mRNA:eIF-4E:eIF-4A complexes were measured. These studies show, for the first time, direct evidence for an eIF-4A:eIF-4E interaction. In contrast to earlier studies, we show that the affinity of eIF-4E and eIF-4F for globin mRNA is similar. Furthermore, the relative affinities of mRNA analogs (capped oligonucleotides) for these initiation factors indicate that the cap is the predominant feature recognized for binding, but other features also contribute to the eIF-4E:mRNA interaction.

Animation of Protein Synthesis (Translation) in Prokaryotes

The major mechanism of translation initiation in eukaryotes involves recognition of the cap structure at the 5′ end of the mRNA by the cap‐binding protein eIF4E. Internal ribosome entry sites (IRES) are specialised RNA sequences that are capable of recruiting ribosomes to an internal position of an mRNA in a cap‐independent manner. Many viruses have evolved this alternative pathway to initiate translation. Viral IRESs bind ribosomes by several mechanisms that require different sets of canonical initiation factors. In addition, IRES activity is modulated by IRES trans‐acting factors (ITAFs). Some cellular mRNAs are suggested to contain IRESs, as they function in cells under stress and other conditions when cap‐dependent initiation is inhibited. However, solid evidence for internal ribosome entry onto many of these mRNAs is lacking.

AB - The initial interaction of mRNA with the protein synthesis machinery presumably involves recognition of the 5′-cap (m7GpppN), although it is not clear at the present time whether this recognition is by eIF-4E or eIF-4F. This process has been studied by direct fluorescence titration experiments. The equilibrium constants for the formation of the binary protein:m7GpppG, protein:mRNA, and protein:protein complexes as well as well as the ternary mRNA:eIF-4E:eIF-4A complexes were measured. These studies show, for the first time, direct evidence for an eIF-4A:eIF-4E interaction. In contrast to earlier studies, we show that the affinity of eIF-4E and eIF-4F for globin mRNA is similar. Furthermore, the relative affinities of mRNA analogs (capped oligonucleotides) for these initiation factors indicate that the cap is the predominant feature recognized for binding, but other features also contribute to the eIF-4E:mRNA interaction.

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Protein Synthesis Initiation in Bacteria


Protein Synthesis - D - N - A - Google Sites

Since the early pioneering work of Nirenberg and Matthaei in 1961 (1), which demonstrated in vitro protein translation using cell extracts, cell-free protein synthesis has become an important tool for molecular biologists by playing a centn Dr. Takuya Ueda’s lab at the University of Tokyo. This became known as the “PURE” system, which stands for “Protein synthesisral role in a wide variety of applications (2). In the post-genomic era, cell-free protein synthesis has the potential to become one of the most important high throughput technologies for functional genomics and proteomics.

Protein synthesis generally occurs in two major steps: ..

The biggest advantage, compared to protein production in living cells, is that cell-free protein synthesis is the quickest way to obtain an expressed phenotype (protein) from a genotype (gene). Starting with a PCR or plasmid template, in vitro protein synthesis and functional assays can be carried out in a few hours. Moreover, it is independent of host cells. Proteins which are toxic or prone to proteolytic degradation can be readily prepared in vitro.

Protein Synthesis Initiation in Eukaryotes: …

Commercially available cell-free protein synthesis systems are typically derived from cell extracts of Escherichia coli S30, rabbit reticulocytes or wheat germ. The drawback of extract-based systems is that they often contain nonspecific nucleases and proteases that adversely affect protein synthesis. In addition, the cell extract is like a “black box” in which numerous uncharacterized activities may modify or interfere with subsequent downstream assays.

Protein Synthesis - MCAT Review

Initiation factors 1, 2 and 3 are essential proteins that promote the binding of the initiator tRNA to the 30S subunit P site and the joining of the 50S subunit.

Molecular Biology Protein Synthesis MCAT Review and MCAT Prep

PURExpress™ from NEB is based on the PURESYSTEM® from PGI, and improves on the original “Classic II” Kit by optimizing components to increase yield of protein synthesis. For more information please .

Protein synthesis is the process in ..

Lopez‐Lastra M, Rivas A and Barria MI (2005) Protein synthesis in eukaryotes: the growing biological relevance of cap‐independent translation initiation. Biological Research 38: 121–146.

Protein Synthesis - Translation Flashcards | Quizlet

The PURE system is more robust and convenient than most extract-based systems for many in vitro applications. The immediate advantage is the significantly reduced level of all contaminating activities. It can be used to express a wide range of protein targets and has the capacity for a yield of more than 100 μg/ml. The activity of the synthesized protein can often be directly assayed without purification due to the low background activity of the translation mixture. All recombinant protein factors inside the PURE system are His-tagged, in some cases allowing the synthesized protein to be “reverse-purified” (Figure 1,2)(3). The purity of this system allows it to withstand more than five freeze-thaw cycles without losing its efficiency, further extending its shelf life (Figure 3)(Cantor, E., unpublished observation).

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