Prokaryotic cells protein synthesis

Chloramphenicol an antibiotic, M, 323, from Streptomyces venezuelae. There are 4 stereoisomers, of which only D(-)-threo-C. (Fig.) is an antibiotic. C. inhibits protein synthesis on 70S ribosomes of prokaryotes, and on the mitochondrial ribosomes of eukaryotic cells. Protein synthesis on SOS eukaryotic ribosomes is not affected. C. inhibits peptide bond formation and peptidyl transferase activity on the 50S ribo-somal subunit, by specifically binding to one of the SOS ribosomal proteins involved in these reactions. The protein in question is probably localized in the acceptor-donor region of the ribosome. C. is used as a broad-spectrum antibiotic in the treatment, e.g. of typhoid fever, paratyphus, spotted fever, infectious hepatitis, dysentery, phtheiia and viral influenza . Because it inhibits protein synthesis in mitochondrial ribosomes, C. is relatively toxic. It is now produced entirely synthetically. 

Although the interior of a prokaryotic cell is not subdivided into compartments by internal membranes, the cell still shows some segregation of metabolism. For example, certain metabolic pathways, such as phospholipid synthesis and oxidative phosphorylation, are localized in the plasma membrane. Also, protein biosynthesis is carried out on ribosomes. 

Other antibiotics inhibit protein synthesis on all ribosomes (puromycin) or only on those of eukaryotic cells (cycloheximide). Puromycin (Figure 38—11) is a structural analog of tyrosinyl-tRNA. Puromycin is incorporated via the A site on the ribosome into the carboxyl terminal position of a peptide but causes the premature release of the polypeptide. Puromycin, as a tyrosinyl-tRNA analog, effectively inhibits protein synthesis in both prokaryotes and eukaryotes. Cycloheximide inhibits peptidyltransferase in the 60S ribosomal subunit in eukaryotes, presumably by binding to an rRNA component. 

The protein synthesis machinery reads the RNA template starting from the 5 end (the end made first) and makes proteins beginning with the amino terminus. These directionalities are set up so that in prokaryotes, protein synthesis can begin even before the RNA synthesis is complete. Simultaneous transcription-translation can t happen in eukaryotic cells because the nuclear membrane separates the ribosome from the nucleus. 

This drug has a direct amebicidal effect against trophozoites E. histolytica in tissues, and it is not active against cysts in either the lumen or intestinal walls, or in other organs. The mechanism of action of emetine consists of the blockage of protein synthesis in eukaryotic (but not in prokaryotic) cells. It inhibits the process of polypeptide chain formation. Protein synthesis is inhibited in parasite and mammalian cells, but not in bacteria. 

Although all tetracyclines have a similar mechanism of action, they have different chemical structures and are produced by different species of Streptomyces. In addition, structural analogues of these compounds have been synthesized to improve pharmacokinetic properties and antimicrobial activity. While several biological processes in the bacterial cells are modified by the tetracyclines, their primary mode of action is inhibition of protein synthesis. Tetracyclines bind to the SOS ribosome and thereby prevent the binding of aminoacyl transfer RNA (tRNA) to the A site (acceptor site) on the 50S ri-bosomal unit. The tetracyclines affect both eukaryotic and prokaryotic cells but are selectively toxic for bacteria, because they readily penetrate microbial membranes and accumulate in the cytoplasm through an energy-dependent tetracycline transport system that is absent from mammalian cells. 

Typical classes and examples within these categories as they apply to what is currently most prescribed on the U.S. market are summarized in Table 1.8. The targets in groups 1 and 4 are unique in bacteria and absent in humans and other animals, whereas groups 2, 3, and 5 have human counterparts that are structurally different between prokaryotes and eukaryotes. These differences in targets make the use of antibiotics selective for bacteria with little or no effect on eukaryotic cells from a therapeutic perspective. However, that does not mean that antimicrobial compounds are completely inert to eukaryotes. The mechanisms that block bacterial protein synthesis, block DNA replication, and those that disrupt membrane integrity affect membrane pores. 

Prokaryotic Bacterial cells infected with bacteriophage Transient expression Infected cells Viral (bacterial phage) promoter and other elements required to support viral protein synthesis... 

Ribosomal RNAs (rRNAs) are found in association with several proteins as components of the ribosomes—the complex structures that serve as the sites for protein synthesis (see p. 433). There are three distinct size species of rRNA (23S, 16S, and 5S) in prokaryotic cells (Figure 30.2). In the eukaryotic cytosol, there are four rRNA size species (28S, 18S, 5.8S, and 5S). [Note "S" is the Svedberg unit, which is related to the jnolecular weight and shape of the compound.] Together, rRNAs make up eighty percent of the total RNA in the cell. 

There are three major types of RNA that participate in the process of protein synthesis ribosomal RNA (rRNA), transfer RNA (tRNA), and messenger RNA (mRNA). They are unbranched polymers of nucleotides, but differ from DNA by containing ribose instead of deoxyribose and uracil instead of thymine. rRNA is a component of the ribosomes. tRNA serves as an adaptor molecule that carries a spe dfic amino acid to the site of protein synthesis. mRNA carries genetic information from the nuclear DNA to the cytosol, where it is used as the template for protein synthesis. The process of RNA synthesis is called transcription, and its substrates are ribonucleoside triphosphates. The enzyme that synthesizes RNA is RNA polymerase, which is a multisub-irit enzyme. In prokaryotic cells, the core enzyme has four subunits—... 

Mechanism of Action of Florfenicol. The inhibitory activities of chloramphenicol (1, R = NCh). thiamphenicol (1, R = SO2CH3), and florfenicol (2) against a sensitive E cofi strain have been studied. In two different liquid media, both chloramphenicol and florfenicol allowed only 20-30% residual growth at a drug concentration of 2 mg/L, whereas a thiaiuplieiiicul concentration of 25 mg/L was required to produce a similar effect. Florfenicol was also found to be a selective inhibitor of prokaryotic cells. At concentrations of 1 mg/L chloramphenicol and florfenicol, and at a concentration of 25 mg/L, thiamphenicol, inhibited protein synthesis. 

In prokaryotes DNA, RNA, and protein synthesis all take place in the same cellular compartment. In eukaryotes the DNA is compartmentalized in the cell nucleus, and it became clear long before the biochemistry of these three processes was understood that DNA synthesis takes place in the nucleus, whereas the bulk of protein synthesis takes place in the cytoplasm. From these observations on eukaryotes it was self-evident that DNA cannot be directly involved in the synthesis of protein but must somehow transmit its genetic information for protein synthesis to the cytoplasm. Careful experiments with radioactive labels were used to demonstrate that RNA synthesis takes place in the nucleus much of this RNA is degraded rather quickly, but the portion that survives is mostly transferred to the cytoplasm (fig. 28.1). From observations of this kind it became clear that RNA was the prime candidate for the carrier of genetic information for the synthesis of proteins. 

INTRON A region of a gene (i.e., ENA) that is transcribed in the synthesis of RNA, but enzymatically removed (by "splicing") from the final mRNA before its translation into an amino acid sequence in protein introns are characteristic of gene structure in eukaryotic, but not prokaryotic, cells. (See also EXON and CODING SEQUENCE)... 

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