Characterization of a mutant form of ribosomal protein S1 from Escherichia coli.
نویسندگان
چکیده
منابع مشابه
Primary structure of ribosomal protein S6 from the wild type and a mutant of Escherichia coli.
Ribosomes were isolated from E. coli, strain P, as previously described [S] . After extraction of ribosomal proteins by acetic acid protein S6 was separated from the other proteins by a two step elution procedure followed by a gradient elution on DEAE-cellulose. This resulted in several forms of S6 as described below and elsewhere in detail [4]. Amino acid analyses were done on a Durrum D-500 a...
متن کاملRestoration by ribosomal protein S1 of the defective translation in a temperature-sensitive mutant of Escherichia coli K-12: characterization and genetic studies.
A temperature-sensitive mutant of Escherichia coli was isolated that had a temperature-sensitive defect in ribosomal-wash protein(s) required for translation in vitro of E. coli endogenous messenger ribonucleic acid. It was found that 30S ribosomal protein S1 rescued the defect in the ribosomal-wash protein(s) of the mutant and that the complete restoration to the wild-type level was attained w...
متن کاملThe effect of Escherichia coli ribosomal protein S1 on the translational specificity of bacterial ribosomes.
Ribosomes from Gram-negative bacteria such as Escherichia coli exhibit non-specific translation of bacterial mRNAs. That is, they are able to translate mRNAs from a variety of sources in a manner independent of the "strength" of the Shine-Dalgarno region, in contrast to ribosomes from many Gram-positive bacteria, such as Bacillus subtilis, which show specific translation in only being able to t...
متن کاملRibosomal protein S1 of Escherichia coli is the effector for the regulation of its own synthesis.
To facilitate the study of the regulation of the rpsA gene, a translational fusion between the rpsA gene and the lacZ gene was constructed. Synthesis of the fusion protein was repressed about 10-fold when rpsA was supplied in trans on a multicopy plasmid. This repression is similar to the post-transcriptional regulation previously found for the wild type rpsA gene. Addition of purified protein ...
متن کاملSpecific binding of Escherichia coli ribosomal protein S1 to boxA transcriptional antiterminator RNA.
We show that ribosomal protein S1 specifically binds the boxA transcriptional antiterminator RNAs of bacteriophage lambda and the Escherichia coli ribosomal RNA operons. Although S1 competes with the NusB-S10 antitermination complex for binding to boxA, it does not affect antitermination by the lambda N protein in vitro, and its role, if any, in rRNA synthesis is still unknown.
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1979
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)30003-0