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N Brot

Publications and source records attributed to N Brot.

At least 127 records · Page 7Linked to original sources

Synthesis of ribosomal proteins L7L12 in relaxed and stringent strains of Escherichia coli.

The control of the synthesis of ribosomal proteins L7L12 (which lack histidine) was examined during growth and histidine starvation of stringent and relaxed histidine mutants. Since no ribosomes are synthesized during starvation, these proteins, in both the stringent and relaxed organisms, accumulated in the supernatant and were shown to possess both biological and physical characteristics typical of normal L7L12. However, the rate and extent of synthesis of these proteins during starvation is greater in the relaxed strain than in the stringent. These data suggest that the regulation of the synthesis of these proteins, similar to that of ribosomal RNA is regulated by the stringent control system. It was also shown that during normal growth of both organisms, L7L12 is also found in the supernatant as well as on the ribosomes. The L7L12 found in the supernatant under these conditions, however, appears to be different than ribosomal L7L12.

Escherichia coli↗

DNA dependent synthesis of protein L12 from escherichia coli ribosomes, in vitro.

The in vitro synthesis of ribosomal protein L12 has been obtained in a coupled system with DNA extracted from the transducing phage lambdarifd18 as template. In addition, a second protein (molecular weight of 16,000) with immunological, chemical, and ribosome-binding characteristics similar to L12 is formed in this in vitro system. The synthesis of both proteins is depressed by one-half when guanosine-5'-diphosphate-3'-diphosphate is added to the reaction mixture.

Bacterial Proteins↗

The requirement for ribosomal proteins L7 and L12 in peptide-chain termination.

Proteins L7 and L12 from 50S ribosomal subunits of Escherichia coli are required for peptidechain termination. This termination process is inhibited by thiostrepton. Since both thiostrepton-treated ribosomes and those depleted of L7 and L12 have a markedly reduced ability to form release factor.UA[(3)H]A.ribosome complexes, the binding of release factors to the ribosome appears to be the primary site of inhibition.

Anti-Bacterial Agents↗