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Localized mutagenesis of the aroE-strA section of the Escherichia coli chromosome coding for ribosomal proteins

✍ Scribed by Berger, I. ;Geyl, D. ;Böck, A. ;Stöffler, G. ;Wittmann, H. G.

Publisher: Springer
Year: 1975
Tongue: English
Weight: 545 KB
Volume: 141
Category: Article
ISSN: 0026-8925
DOI: 10.1007/bf00341800

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✦ Synopsis

In order to obtain E. coli strains altered in ribosomal proteins the following isolation technique was used: Phage P1 grown in a streptomycin resistant E. coli strain, was mutagenized by hydroxylamine or nitrous acid, and was used to transduce into a strain auxotrophic for aroE. Transductants with streptomycin resistance and aroE prototrophy were selected and tested for their growth at various temperatures (20 degrees, 30 degrees and 42 degrees) and their response to different antibiotics. Ribosomes from seventeen transductants with an altered response to temperature or antibiotics were isolated. They were tested for alterations in their ribosomal subunit profiles by sucrose centrifugation and for altered ribosomal proteins by two dimensional gel electrophoresis. Two strains showed accumulation of 50S ribosomal precursors and three strains had an altered 50S protein L18. This protein belongs to the 5S RNA-protein complex having GTPase and ATPase activity.

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