Ribosomal proteins from chloroplasts of Nicotiana tabacum L. (cv. Petit Havana) and of SRl, a mutant derived from it, with uniparentally inherited streptomycin resistance, were characterised by two-dimensional gel electrophoresis. From the 67 proteins identified, one has an altered electrophoretic m
A relaxed mutant with an altered ribosomal protein L11
β Scribed by Parker, Jack ;Watson, Robert J. ;Friesen, James D. ;Fiil, Niels P.
- Publisher
- Springer
- Year
- 1976
- Tongue
- English
- Weight
- 415 KB
- Volume
- 144
- Category
- Article
- ISSN
- 0026-8925
No coin nor oath required. For personal study only.
β¦ Synopsis
Relaxed mutants of Escherichia coli have been isolated which have an altered electrophoretic mobility of ribosomal protein L11. It can be shown that reversion to stringency in one of these mutants occurs simultaneously with a reversion of L11 protein to tis normal mobility. The L11 structural gene, rplK, maping near rif, is carried by the bacteriophage lambdacI857S7drifd18, and is most likely identical with relC.
π SIMILAR VOLUMES
Proteins of cytoplasmic ribosomes of the Podospora anserina were analyzed by two dimensional gel electrophoresis. The numbers of proteins were estimated to be 28 in the small subunit and 41 in the large subunit. The L21 protein of the large subunit was found to migrate differently in a cycloheximide