A Mutant of Escherichia coli Defective in Leucyl, Phenylalanyl-tRNA-Protein Transferase*
AUTOR(ES)
Soffer, R. L.
RESUMO
A mutant of E. coli that lacks leucyl,-phenylalanyl-tRNA-protein transferase (EC 2.3.2.6) has been isolated. Ability to produce the two activities could be introduced into the mutant from an F′ strain whose episome contains genetic material located between 45 and 54 min on the E. coli chromosome. When grown into stationary phase and resuspended in minimal medium with glycerol, the mutant exhibited a marked lag before resuming growth. Revertants that did not show this lag were selected and were found to have regained both transfer activities. Extracts of wild-type, mutant, and revertant strains were compared as acceptors for the enzymatic transfer of radioactive phenylalanine. Analysis of the labeled polypeptides by disc gel electrophoresis indicated that certain potential acceptors may be preferentially acylated in vivo.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=388146Documentos Relacionados
- Modification of a Specific Ribosomal Protein Catalyzed by Leucyl, Phenylalanyl-tRNA:Protein Transferase*
- The N-end rule in Escherichia coli: cloning and analysis of the leucyl, phenylalanyl-tRNA-protein transferase gene aat.
- Pleiotropic phenotype of an Escherichia coli mutant lacking leucyl-, phenylalanyl-transfer ribonucleic acid-protein transferase.
- Regulation of proline catabolism by leucyl,phenylalanyl-tRNA-protein transferase.
- A single mutation affects L-serine deaminase, L-leucyl-, L-phenylalanyl-tRNA protein transferase, and proline oxidase activity in Escherichia coli K-12.