Abstract
An altered form of ribosomal protein S1 from a mutant of Escherichia coli has been isolated and characterized. The mutant protein (denoted m1-S1) has a molecular weight of 57,000 as shown by sodium dodecyl sulfate-gel electrophoresis and the same NH2-terminal sequence as wild type S1. Protein m1-S1 binds poly(U) in the same manner as protein S1 and is active in protein synthesis with either synthetic or natural mRNA. Thus, about 75% of the sequence of protein S1 (which includes the NH2-terminal region) contains essentially all the functional domains of this protein involved in protein biosynthesis.
Highlights
E. coli strain altered in Sl was derived from
We may conclude that, unlike the fragment mentioned earlier (l), ml-S1 has retained ah the essential functional domains of protein Sl which are involved in protein synthesis
We have described the isolation and characterization of a mutant ribosomal protein Sl which has the molecular weight of 57,000, that is, 25% smaller than the molecular weight of wild type protein Sl
Summary
An altered form of ribosomal protein Sl f’rom a mutant of Escherichiu coli has been isolated and characterized. We have generated and isolated in pure form fragments of the Sl molecule which retain one or more of the active sites intact (Ref. 1 and Footnote 1) in order to map the distribution of the active sites along the molecule and possibly to elucidate the biochemical mechanism of the cellular functions of this protein. In connection with these studies, we have isolated and characterized an altered form of protein Sl which is present in a mutant of E. coli. The results presented below show that the mutant protein is 25% shorter than the wild type molecule but has retained the ability to stimulate ribosomes in mRNA translation in an in vitro system
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