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Protein synthesis is the process of producing proteins using the information encoded by the DNA located in the nucleus of the cell. Two processes take place to convert the information in DNA into proteins by cells.

Forms Part Of The Protein Synthesis Site In The Cytoplasm

First, in a process called transcription, the coding region of a gene is copied into a single-stranded ribonucleic acid (RNA) version of double-stranded DNA. This is done by RNA polymerase, a large enzyme that catalyzes the addition of nucleotides to the RNA chain. RNA is processed into messenger RNA (mRNA) before being transported to the cytoplasm.

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After processing, the mRNA is translocated through nuclear pores to the cytoplasm, where the translation machinery (i.e., the ribosome, eukaryotic initiation factors eIF4E and eIF4G, and poly(A)-binding protein) carries out the second process, translation. in which ribosomes. Assemble the amino acids in the order specified by the mRNA sequence.

Protein synthesis is an important cellular process in prokaryotes and eukaryotes. This is done by the ribosome, an evolutionarily conserved ribonucleoprotein complex, and many other proteins and RNA molecules help. Together, they synthesize all proteins necessary for various biological functions. Protein synthesis can be divided into 3 stages: initiation, elongation and termination. Each step has different protein and RNA molecules that play a role in efficient catalysis. The ribosome also has three main sites: an acceptor site (A site), a peptidyl transfer site (P site), and an exit site (E site) where tRNA facilitates catalysis.

Initiation begins with the 30S subunit, which binds to factor 3 (IF-3). IF-3 binding prevents premature binding of the 50S unit and also plays a role in mRNA strand control. mRNA binds to this complex using the Shine-Dalgarno sequence. This sequence is a sequence of 9 nucleotide bases upstream of the AUG start codon in the mRNA. It is complementary to the sequence in the 16S rRNA of the 30S subunit and helps align the mRNA with 30S. Next, IF-1 binds to the A site on 30S, where all charged tRNAs first bind. IF-1 effectively blocks early binding of tRNA at the A site before the ribosome is fully assembled.

IF-2 delivers the first tRNA to the P site, where peptidyl transfer reactions occur. In bacteria, the first tRNA is always an N-formyl-modified methionine encoded by the start codon AUG. As more amino acids are added to the nascent peptide chain, the formyl group is removed downstream. At this stage, the 30S initiation complex is fully assembled, attracting the 50S subunit to self-assemble with it. IF-2 is a GTP-binding protein whose GTP hydrolysis releases all initiation factors from the newly assembled initiation complex. The 70S-mRNA-f-met tRNA complex is now ready for protein synthesis.

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After the 70S complex assembles with the initiator tRNA at the P site, the ribosome begins scanning the mRNA sequence. Each codon corresponds to a specific amino acid, which is delivered to the ribosome by elongation factor thermostable (EF-Tu). EF-Tu forms a complex with a charged tRNA molecule, inserts it into mRNA, and is released from 70S by GTP hydrolysis.

The GTP-bound state of EF-Tu is essential for efficient delivery of tRNA, so the cell has evolved a mechanism to recycle EF-Tu using another protein called elongation factor thermostable (EF-Ts). EF-Ts act as a guanine nucleotide exchange factor, effectively releasing GDP from EF-Tu so that a new molecule of GTP can bind. When EF-Tu binds another GTP molecule, it can again form a tRNA-EF-Tu-GTP complex and continue the process of tRNA delivery. Once the A site and the P site are both charged tRNAs, a peptide bond is formed between the two amino acids by nucleophilic attack of the A amino acid on the P site amino acid. At this stage, the A site contains tRNA with a growing peptide chain, and the P site contains empty tRNA.

Another GTP-binding protein, elongation factor G (EF-G), catalyzes the movement of tRNAs along the assembly line. This is called translocation and frees the A site for further peptidyl transfer reactions. After EF-G binds to the ribosome, GTP hydrolysis causes a conformational shift of the ribosome so that the tRNAs move down from the A and P site to the P and E site. Site E is the exit site, where free tRNAs diffuse into the cytosol where they are recharged by tRNA synthetases. After EF-G translocates, the A site is ready to accept the new tRNA. Thus, the elongation cycle continues to supply the growing new peptide until it encounters a stop codon.

Once a stop codon is reached on the mRNA strand, there are no more tRNA molecules to complement the base pair with the mRNA. Instead, release factors 1 and 2 (RF-1/RF-2) recognize stop codons and bind to 70S. This triggers hydrolysis of the peptide chain at the P-site and releases the peptide into the cytosol for further processing and folding. RF-3, a GTP-binding protein, binds to 70S and triggers the release of RF-1/RF-2 through GTP hydrolysis. At this stage, the 70S ribosome is bound to mRNA and free tRNA. In this case, 70S cannot carry out protein synthesis and must therefore be recycled. This function is carried out by ribosome processing factor (RRF) and EF-G, which bind to the ribosome and cause its dissociation through GTP hydrolysis. Once the 30S and 50S subunits are released, IF-3 rebinds 30S to prevent premature 70S formation and the initiation cycle can begin again.

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The structural complexity of the ribosome, along with its central biological function, makes it a prime target for inhibition. Given the difference between prokaryotic 70S ribosomes and eukaryotic 80S ribosomes, organisms have developed small molecules that selectively target 70S ribosomes and 80S ribosomes to selectively kill their target. These inhibitors target almost every step of protein synthesis, and modern X-ray crystallography allows us to fully understand their binding modes and mechanisms of action. Many 70S inhibitors serve as powerful antibiotics in the clinic because they have a selective toxic effect on bacterial cells. It should be noted that many inhibitors inhibit several stages of protein synthesis, increasing their antimicrobial activity. Some of the major inhibitors of protein synthesis in prokaryotes are discussed below. Protein synthesis is the process of converting the information in the DNA code into proteins. Some of these proteins form part of the cell structure. Others are enzymes that control the production of all the other materials that make up a cell or an entire organism.

Protein synthesis is a continuous process, but we break it down into steps to help you understand what happens and where it happens in the cell.

For many years, scientists thought that each gene coded for a single protein. We now know that DNA itself or the mRNA produced in the nucleus are affected by various factors. As a result, a single gene can encode many different proteins depending on the internal and external environment of the cell.

Transcription factors can affect the transcription of DNA in different ways

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Primary mRNA is the transcription of all DNA, including introns or non-coding regions of DNA. It must be modified before it can be transferred to ribosomes for translation. Introns are removed by enzymes called spliceosomes. Sometimes, spliceosomes attach to certain exons or coding regions in different sequences, so that the same region of DNA can give rise to several different types of mRNA.

Epigenetics is a relatively new method of studying the effect of the environment on the genome. It describes how different chemicals bound to DNA or RNA can affect the way the genetic code is read. Such external control of the genome can be achieved by:

Some proteins are produced in an inactive form. Post-translational modifications as a result of second messengers such as cyclic AMP (cAMP) in the cell or specific enzymes in the body modify and activate proteins, changing the molecule produced. Examples are the production of fibrin from fibrinogen in the coagulation cascade and the production of pepsin from pepsinogen in the digestive system.

Explore epigenetics and make a poster for your peers explaining an example of this rapidly growing field of research.

Messenger Rna (mrna)

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As mentioned earlier, the sequence of nucleotides represents the genetic information that makes us unique and the blueprint for who and what we are and how we function. Part of this genetic information is devoted to the synthesis of proteins that are necessary for our body and used in various ways. Proteins are created from templates

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