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Biomedical subjects

M Schweiger

Publications and source records attributed to M Schweiger.

At least 217 records · Page 12Linked to original sources

Chromosomal localization of the structural genes of the polypeptide chain elongation factors.

A survey of the polypeptide chain elongation factors in potentially sexually compatible genera was carried out. Factors from Escherichia coli and Proteus mirabilis were found to be clearly distinguishable by immunochemical and electrophoretic techniques. Mapping of the structural genes of these factors was undertaken by a study of the gene products in genetically defined E. coli-P. mirabilis hybrid diploid strains. It was found that the EF G factor mapped within 5 min of the streptomycin resistance locus, but the EF Ts factor did not map in this region.

Bacterial Proteins↗

Control of gene function in bacteriophage Tr. 3. Preventing the shutoff of early enzyme synthesis.

Synthesis of early T4 protein, which is normally shut off at 10 min after infection, continues until lysis when host cells have been preinfected with T3 sam(+). In host cells preinfected with T3 sam(-), synthesis of early enzymes is shut off as normal. Thus, S-adenosylmethionine is required for the turnoff of early T4 functions (at least when host cells have been preinfected with T3).

Aminohydrolases↗

Stimulation of galactokinase synthesis in Escherichia coli by adenosine 3',5'-cyclic monophosphate.

Adenosine 3',5'-cyclic monophosphate (cyAMP) stimulates the rate of synthesis of galactokinase in glycerol-grown Escherichia coli both when production of the enzyme is induced by d-fucose and when it is repressed by glucose in the presence of inducer. cyAMP also stimulates the synthesis of galactokinase in constitutive strains B78A (R(-)) and R10 (O(c)), and overcomes the transient repression of galactokinase synthesis caused by glucose.

Carbon Isotopes↗

T3 and T7 bacteriophage deoxyribonucleic acid-directed enzyme synthesis in vitro.

The T3 phage enzymes S-adenosyl methionine cleaving enzyme and lysozyme and the T7 lysozyme were synthesized in a deoxyribonucleic acid (DNA)-dependent, cell-free system derived from uninfected Escherichia coli. The data presented suggest that these enzymes are encoded in that portion of the DNA which is transcribed early after infection.

Carbon Isotopes↗

Synthesis of phage-specific alpha- and beta-glucosyl transferases directed by T-even DNA in vitro.

-Bacteriophage T4 DNA, when added to a ribonucleic acid- and protein-synthesizing system from uninfected Escherichia coli, directed the in vitro synthesis of virus-specific glucosyl transferases. The T4-specific alpha- and beta-glucosyl transferases are synthesized in vivo early after infection, and function to glucosylate the hydroxymethylcytosine residues of phage DNA. The in vitro glucosyl transferase synthesis was dependent upon transcription of T4 DNA, as well as upon protein synthesis. DNA from T4 mutants unable to induce glucosyl transerases failed to induce enzyme formation in vitro, although protein synthesis was unimpaired.

Chloramphenicol↗

Bacteriophage T4 DNA-dependent in vitro synthesis of lysozyme.

A cell-free system derived from uninfected Escherichia coli previously was shown to synthesize beta-glucosyl transferase in response to T4 DNA. This same in vitro system, when incubated at slightly higher magnesium concentrations, also synthesized enzymatically active lysozyme. The lysozyme activity that appeared was judged to be T4-specific since antibodies prepared against authentic T4-lysozyme inactivated the in vitro synthesized enzyme. DNA from a T4 mutant carrying a deletion in the lysozyme gene stimulated amino acid incorporation to the same extent as wild-type T4 DNA but was inactive in directing the synthesis of lysozyme. Various inhibitors of RNA and protein synthesis inhibited the in vitro synthesis of lysozyme.

Carbon Isotopes↗