Abstract
A previously isolated thermosensitive mutant [Springer, M., Graffe, M. & Grunberg-Manago, M. (6977) Mol. Gen. Genet. 151, 17-26] exhibits two defects in vitro, one in the initiation factor IF3 and the other in the L-phenylalanine: tRNA-Phe ligase (EC 6.1.1.20). Specialized lambda transducing phages that transduced this mutant to thermoresistance were selected. In vitro studies showed that the transductants had a normal IF3 activity. One of these transducing phages was shown to code for a protein synthesized under the control of Escherichia coli promoters, which has the same molecular weight as IF3. This protein crossreacts specifically with IF3 antisera and comigrates with pure IF3 in a two-dimensional gel system.
MeSH Terms
Bacterial Proteins/biosynthesis
Coliphages/genetics
DNA, Recombinant/metabolism
Escherichia coli/genetics
Genotype
Kinetics
Lysogeny
Molecular Weight
Peptide Initiation Factors
Protein Biosynthesis
Transduction, Genetic
Viral Proteins/biosynthesis
Chemicals
Bacterial Proteins
DNA, Recombinant
Peptide Initiation Factors
Viral Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Springer M
Graffe M
Hennecke H
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23 references, click to expand
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