Escherichia coli protein synthesis

Jayaraman, K., McParland, K., Miller, P., and Tso, P.O.P. 1981. Non-ionic oligonucleoside methylphosphonates. 4. Selective inhibition of Escherichia coli protein synthesis and growth by non-ionic oligonucleotides complementary to the 3 end of 16S ribosomal-RNA. Proc. Natl. Acad. Sci. U.S.A. 78 1537-1541. 

Kano-Sueoka, T., Sueoka, N. Leucine-tRNA and cessation of Escherichia coli protein synthesis upon phage T2 infection. Proc. nat. Acad. Sci. (Wash.) 62, 1229-1236 (1969). 

Functional proteins are also involved in high-affinity Ni transport for hydrogenase synthesis. One example is the nikABCDE gene cluster of Escherichia coli 20). NikA is a periplasmic Ni-binding protein. 

L-Asparaginase is an enzyme that may be produced by Escherichia coli. Asparaginase hydrolyzes the reaction of asparagines to aspartic acid and ammonia to deplete lymphoid cells of asparagine, which inhibits protein synthesis. The... 

Piddock, L. J. V., Walters, R. N., and Diver, J. M. (1990). Correlation ofquinolone MIC and inhibition ofDNA, RNA and protein synthesis and induction of the SOS response in Escherichia coli. Antimicrob. Agents Chemother. 34, 2331-2336. 

To establish whether rifaximin, like the other members of the rifamycin family [36, 58], specifically inhibits bacterial RNA synthesis the effect of this antibiotic as well as that of rifampicin and chloramphenicol on RNA (via 3H-uridine incorporation), DNA (via 3H-thymidine incorporation) and protein (via 35S-methionine incorporation) synthesis was studied in growing cultures of Escherichia coli [59], While chloramphenicol reduced protein synthesis, both rifaximin and rifampicin inhibited RNA synthesis in a concentration-dependent fashion. In contrast, none of them affected 3H-thymidine incorporation into DNA. These data suggest that rifaximin, like rifampicin, inhibits RNA synthesis by binding the (3 subunit of the bacterial DNA-dependent RNA polymerase [60],... 

Ribosome activating cytotoxic proteins that irreversibly inhibit protein synthesis in cells, causing cell death. They are obtained from bacteria (Escherichia coli serotype 0157 H7). Verotoxin 1 is almost identical to shiga toxin (C16-A032) and differs only by a single amino acid. Verotoxin 2 has significant differences. 

MIROUX, B., WALKER, J.E., Over-production of proteins in Escherichia coli Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels, J. Mol. Biol. 1996, 260, 289-298. 

Most frequently, extracts of either prokaryotic or eukaryotic origin as such from Escherichia coli, wheat germ or rabbit reticulocytes are employed for cost reasons and availability. While those based on E. coli are unable of post-translational protein modification, eukaryotic extracts do allow synthesis of glycosylated or phosphorylated proteins to some extent when additional components, such as microsomes for glycosylation are added. Care needs to be taken with cell-free systems recombinated from the individual components when a native protein is to be produced that does not fold spontaneously... 

A tRNA molecule is specific for a particular amino acid, though there may be several different forms for each amino acid. Although relatively small, the polynucleotide chain may show several loops or arms because of base pairing along the chain. One arm always ends in the sequence cytosine-cytosine-adenosine. The 3 -hydroxyl of this terminal adenosine unit is used to attach the amino acid via an ester linkage. However, it is now a section of the nucleotide sequence that identifies the tRNA-amino acid combination, and not the amino acid itself. A loop in the RNA molecule contains a specific sequence of bases, termed an anticodon, and this sequence allows the tRNA to bind to a complementary sequence of bases, a codon, on mRNA. The synthesis of a protein from the message carried in mRNA is called translation, and a simplified representation of the process as characterized in the bacterium Escherichia coli is shown below. 

Protein synthesis in prokaryotes is in principle the same as in eukaryotes. However, as the process is simpler and has been better studied in prokaryotes, the details involved in translation are discussed here and on p. 252 using the example of the bacterium Escherichia coli. 

Comeau, D.E. Ikenaka, K. Tsung, K.L. Inouye, M. Primary characterization of the protein products of the Escherichia coli ompB locus structure and regulation of synthesis of the OmpR and EnvZ proteins. J. Bacteriol., 164, 578-584 (1985)... 

Hydroquinone decreased interleukin (IL)-l secretion and protein and RNA synthesis of isolated human peripheral blood monocytes induced by Escherichia coli lipopoly-saccharide at micromolar concentrations (Carbonnelle etal., 1995). Hydroquinone (4 pmol/L) inhibited the growth of bone marrow cells from female C57BL/6 x DBA/2 mice (Seidel et al., 1991) and from male Swiss Webster and C57BL/6J mice (10 pmol/L) (Neun et al., 1992). Hydroquinone (50, 75 or 100 mg/kg bw, single intraperitoneal admi-... 

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