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Protein synthesis is the process of making proteins using the information encoded by DNA, located in the nucleus of a cell. Cells use two processes to convert information in DNA into proteins.

The Site Of Protein Synthesis Is Called

First, in a process called transcription, the coding part of a gene is copied into a single-stranded ribonucleic acid (RNA) version of the double-stranded DNA. This is accomplished by RNA polymerase, a large enzyme that synthesizes the chain of nucleotides in an RNA chain using DNA as a template. The RNA is further processed into messenger RNA (mRNA) before being transported to the cytoplasm.

Cell Free Protein Synthesis From Genomically Recoded Bacteria Enables Multisite Incorporation Of Noncanonical Amino Acids

After processing, the mRNA is transported to the nuclear pores in the cytoplasm, where translation machinery (such as the ribosome, eukaryotic initiation factors eIF4E and eIF4G, and poly(A)-binding protein) is used to make ate the second process, translation, during the ribosomes. assemble amino acids in the order dictated by the mRNA sequence.

Protein synthesis is an important cellular process in both prokaryotes and eukaryotes. This is done by the ribosome, a complex ribonucleoprotein complex, and assisted by many other protein and RNA molecules. Together, they synthesize all the proteins needed for specific functions. Protein synthesis can be divided into 3 phases: initiation, elongation, and termination. Each step has different proteins and RNA molecules that play a role in effective catalysis. The ribosome also has three main sites: the acceptance site (A site), the peptidyl-transfer site (P site) and the exit site (E site) where the tRNA is attached, facilitating its use.

The initiation starts with the 30S subunit that has initiation factor 3 (IF-3) bound to it. The binding of IF-3 prevents the immediate binding of the 50S unit, and also has a role in regulating the mRNA strand. mRNA binds to this complex, assisted by the Shine-Dalgarno sequence. This sequence is a 9 nucleotide string based on the start codon AUG on the mRNA. It adds a sequence to the 16S rRNA of the 30S subunit and helps bind the mRNA to the 30S. In turn, IF-1 binds to the A site on the 30S which is the first binding site for all tRNAs. IF-1 effectively blocks the early binding of a tRNA to the A site before the ribosome is fully assembled.

IF-2 delivers the first tRNA to the P site, where peptidyl translation occurs. In bacteria, the first tRNA is usually N-formyl modified methionine, marked by the AUG start codon. The formyl group is removed in water when other amino acids are added to the new peptide chain. At this point, the 30S pre-initiation complex is fully assembled which attracts the 50S subunit to assemble with it. IF-2 is a GTP-binding protein, and hydrolysis of GTP releases all the initiators from the new initiation complex. The 70S-mRNA-f-met tRNA complex is now ready for protein synthesis.

B1 Protein Synthesis

After 70S pairs with the starting tRNA at the P site, the ribosome begins to search for the mRNA sequence. Each codon corresponds to a specific amino acid, and is transported to the ribosome by the elongation factor thermo unstable (EF-Tu). EF-Tu forms a complex with a charged tRNA molecule, places it on the mRNA and then dissociates it from the 70S by GTP hydrolysis.

The GTP bound state of EF-Tu is required for efficient delivery of tRNA, so the cell develops a mechanism to recycle EF-Tu to by using another protein called elongation factor thermo stable (EF-Ts). EF-Ts act as guanine nucleotide exchange factors, efficiently releasing GDP from EF-Tu so that it can bind a molecule of GTP. When EF-Tu binds another molecule of GTP, a tRNA-EF-Tu-GTP complex can be formed and the process of tRNA delivery continues. Once both the A and P sites have charged the tRNA present, a peptide bond is formed between the two amino acids through a nucleophilic attack of the amino acid A site i on the P site amino acids. In this step, the A site contains the tRNA and the resulting peptide chain and the P site contains an empty tRNA.

Another GTP-binding protein, elongation factor G (EF-G), promotes the movement of tRNAs along the assembly line. This is called translation, and leaves the A site up for further peptidyl translation activity. Once EF-G binds to the ribosome, GTP hydrolysis causes the ribosome to shift so that the tRNA moves from the A and P sites to the P and E sites. site E is the exit site and empty tRNAs diffuse back into the cytosol where they are regenerated by tRNA synthetases. After EF-G has made a translation, the site is ready to accept a new tRNA. Thus, the elongation cycle continues to produce an increasing number of peptides, until a stop codon is found.

Once a stop codon is reached on the mRNA strand, no tRNA molecules can re-pair the base with the mRNA. Instead, release factors 1 and 2 (RF-1/RF-2) recognize stop codons and bind to 70S. This triggers the oxidation 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 induces the release of RF-1/RF-2 through GTP hydrolysis. At this stage, the 70S ribosome contains empty mRNA and tRNA. In this state, 70S cannot perform protein synthesis and must be recycled. This function is carried out by the ribosome recycling factor (RRF) and EF-G, which binds to the ribosome and causes its disassembly by GTP hydrolysis. Once the 30S and 50S subunits are free, the IF-3 rebinds the 30S to prevent the rapid formation of the 70S and the initiation cycle begins again.

Protein Synthesis • Ibiology

The highly complex structure of the ribosome, together with its central function, has made it a prime target for inhibition. Because of the differences between the prokaryotic 70S ribosomes and the eukaryotic 80S ribosomes, organisms have evolved small organisms that can selectively target the 70S ribosomes and 80S ribosomes to destroy their target. These inhibitors target almost all stages of protein synthesis, with modern x-ray crystallography we have a complete understanding of their binding methods and mechanisms of action. Many 70S inhibitors have become a powerful drug in the clinic since they exhibit selective toxicity to bacterial cells. It should be noted that many inhibitors interfere with many steps of protein synthesis, increasing their antimicrobial activity. Some of the main mechanisms of protein synthesis in prokaryotes are discussed below. The ribosome is a cellular organelle made up of RNA (ribonucleic acid) and ribosomal proteins that serve as a site for protein synthesis in the cell. Ribosomes consist of two major parts: the small and large ribosomal subunits. Scientists like to call ribosomes, macromolecular machines, admire the beauty of the design of ribosomes!

The ribosome reads the messenger RNA (mRNA) sequence and, using the genetic code, translates the RNA sequence into a sequence of amino acids (a process called called Translation).

Ribosomes act as machines that translate the code sequence of mRNA into a protein. Scientists like to call ribosomes, the molecular micro-machines, to admire the beautiful design of ribosomes!

The ribosome is a complex but beautiful “micro-machine” for producing proteins. Ribosomes are made of ribosomal proteins and ribosomal RNA (rRNA). In prokaryotes, ribosomes are composed of about 40 percent protein and 60 percent rRNA. The eukaryotic ribosome consists of three or four rRNA molecules and about 80 different proteins. Its molecular mass is about 4, 200, 000 Da. About two-thirds of this system is ribosomal RNA, and one-third of that is various ribosomal proteins. Ribosomes are not membrane-bound organelles.

Ribosomal Rna (rrna)

Each ribosome consists of two subunits, a large subunit and a small subunit; both are RNA-protein complexes. The large subunit has the transcriptional activity, while the smaller subunit acts as a sorting mechanism.

The name of the subunits is based on the sedimentation rate, which means how quickly it can settle down when mixing the lysis cells in a centrifuge. This ratio is measured in Svedberg (S) units rather than size. This is why subunit names are not added: for example, bacterial 70S ribosomes are composed of a large 50S subunit and a small 30S subunit, while human 80S ribosomes have subgroups 60S and 40S.

[In this picture] The combination of prokaryotic ribosome rRNA and eukaryotic ribosome rRNA. LSU is a very small group and SSU is a very small group.

Ribosomal ribonucleic acid (rRNA) is the first part of ribosomes and carries our proteins together like an enzyme; this is why it is called a ribozyme. Unlike messenger RNA, rRNA does not carry structural information. Therefore, they do not identify RNA. Ribosomal RNA is transcribed from ribosomal DNA (rDNA).

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RRNA is not a linear RNA molecule. In fact, it folds into a special 3-D structure with buttons and buttons. The strands of short double-stranded RNA are formed by base pairing (A=U, G≡C). The signals are non-duplicated RNAs. This image is a secondary structure of 16S rRNA. The higher order rRNA will fold this structure onto a complex of proteins. The complete sequence of the 16S rRNA gene is about 1500 bases

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