Ribosomal proteins of Escherichia coli II. Proteins from the 30 s subunit

Moore, Peter B.; Traut, Robert R.; Noller, H.; Pearson, P.; Delius, Hajo

doi:10.1016/0022-2836(68)90420-8

Cited by 143 publications

(22 citation statements)

References 28 publications

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“…A homogeneity hypothesis was postulated almost 50 years ago (Moore et al 1968) but was immediately challenged by a series of studies showing that bacterial ribosomes vary in protein composition under different growth conditions (Deusser 1972, Deusser & Wittmann 1972, Milne et al 1975) and depending on functional state (free subunits, monosomes, or polysomes) (Bickle et al 1973). Stoichiometry measurements also indicate that, although most RPs are present in one copy per ribosome, approximately a quarter of RPs are present in less than molar amounts and a few are multicopy (Kurland et al 1969, Traut et al 1969, Weber 1972).…”

Section: Are All Ribosomes the Same?mentioning

confidence: 97%

Translating the Genome in Time and Space: Specialized Ribosomes, RNA Regulons, and RNA-Binding Proteins

Shi

Barna

2015

Annu. Rev. Cell Dev. Biol.

188

178

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A central question in cell and developmental biology is how the information encoded in the genome is differentially interpreted to generate a diverse array of cell types. A growing body of research on posttranscriptional gene regulation is revealing that both global protein synthesis rates and the translation of specific mRNAs are highly specialized in different cell types. How this exquisite translational regulation is achieved is the focus of this review. Two levels of regulation are discussed: the translation machinery and cis-acting elements within mRNAs. Recent evidence shows that the ribosome itself directs how the genome is translated in time and space and reveals surprising functional specificity in individual components of the core translation machinery. We are also just beginning to appreciate the rich regulatory information embedded in the untranslated regions of mRNAs, which direct the selective translation of transcripts. These hidden RNA regulons may interface with a myriad of RNA-binding proteins and specialized translation machinery to provide an additional layer of regulation to how transcripts are spatiotemporally expressed. Understanding this largely unexplored world of translational codes hardwired in the core translation machinery is an exciting new research frontier fundamental to our understanding of gene regulation, organismal development, and evolution.

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Section: Are All Ribosomes the Same?mentioning

confidence: 97%

Translating the Genome in Time and Space: Specialized Ribosomes, RNA Regulons, and RNA-Binding Proteins

Shi

Barna

2015

Annu. Rev. Cell Dev. Biol.

188

178

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“…2a. Standard gels containing 7.5% acrylamide and 0.8% methylene bisacrylamide were run according to Moore et al (16). A standard gel of total 30S proteins is at left; peak-fraction gels are at right.…”

Section: Discussionmentioning

confidence: 99%

Alteration of a 30S Ribosomal Protein Accompanying the ram Mutation in Escherichia coli

Zimmermann

Garvin

Gorini

1971

Proc. Natl. Acad. Sci. U.S.A.

103

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The functional peculiarities of ram mutants correlate with an observed alteration in chromatographic mobility of P4a, a specific protein of the 30S ribosomal subunit. This finding is supported by ribosomnal reconstitution experiments. These facts, together with the known location of the ram mutational site in the vicinity of other 30S genetic determinants, suggest that ram is the structural gene for P4a.The known contrasting roles of ram and strA in determining translational efficiency require that the function of P4a should be explained in relation to PlO (the 30S-subunit protein defined by strA). One consequence of altering P4a, a key protein in ribosome assembly, might be to change the interaction of PlO with the 30S subunit. The functional interrelationship of P4a and PlO is discussed in terms of the possible roles of these two proteins in regulating access of tRNA molecules to the decoding site.A mutation isolated by selection for increased translational ambiguity in Escherichia coli B was found to alter the 30S ribosomal subunit. Strains bearing this lesion, which maps in the strA region, have ribosomes that allow translation of synthetic mRNAs with a level of misreading significantly higher than ribosomes from parental strains; this capacity was shown to be a property of the mutant 30S subunit by exchange of 30S and 50S particles from mutant and parental ribosomes. The new mutation was accordingly called ram, for ribosomal ambiguity (1).A more general interpretation of the nature of ram mutants, however, emerges from a consideration of the procedure used in their selection. The parent was an argF amber mutant whose nutritional block was incomplete due to limited or "leaky" translation through the nonsense codon (2). In the first step of the selection, the strain was made strictly auxotrophic by introducing strAl, a mutant allele of the gene specifying the 30S ribosomal protein P10 (3), known to restrict intrinsic nonsense leakiness (4). In the second step, spontaneous mutants were sought in which the nutritional leakiness of the original parent reappeared. Given the nature of the selection, it is quite possible that ram determines a 30S ribosomal component that does not, in itself, govern translational ambiguity, but which in some way opposes the translational restriction imposed by the strA mutation.This view is supported by the fact that the ram/strA interaction is not limited to translational ambiguity. A further aspect of the phenotype, which seems more general, is that the ram mutation reverses the restriction imposed by strA alleles on the suppression efficiency of mutated tRNAs (4, T). This reversal cannot be attributed to increased ambiguity, as demonstrated in the case of missense suppression; if ram were to introduce ambiguity, a further reduction, rather than an increase, in suppression efficiency would be expected, since the insertion of a specific amino acid is required to correct a missense mutation and restore functional activity to the gene product.The contrasting influence on tra...

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“…When proteins from the 52S ribosomal subunits of several mutants were compared with wild-type proteins by the electrophoretic method of Moore et al (18), a pattern of incompletely resolved bands was obtained. As shown in Fig.…”

Section: Methodsmentioning

confidence: 99%

“…Preliminary electrophoretic analysis was performed with a i3-alanine-acetate disc buffer system and 7.5% (w/v) acrylamide-0.8% (w/v) methylene-bisacrylamide gels, as described by Moore et al (18). Gels were stained in 0.1% (w/v) Coomassie (19,20).…”

Section: Methodsmentioning

confidence: 99%

Altered Chloroplast Ribosomal Proteins Associated with Erythromycin-Resistant Mutants in Two Genetic Systems of Chlamydomonas reinhardi

Mets

Bogorad

1972

Proc. Natl. Acad. Sci. U.S.A.

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The phenotype of several erythromycin-resistant mutants of Chiamydomonas reinhardi was further characterized in terms of the electrophoretic properties of their chloroplast ribosomal proteins. In mutant ery-M2d a single protein of the large (52 S) subunit has altered properties, which probably result from a change in its primary sequence. This mutation is inherited in a Mendelian manner. In mutant ery-Ula, which is inherited in a uniparental manner, a different single protein of the 52 S subunit is altered. This change might result from a change in either the primary sequence of the protein or in some form of secondary modification. These results indicate that these two distinct genetic systems must cooperate in the production of chloroplast ribosomes.

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Ribosomal proteins of Escherichia coli II. Proteins from the 30 s subunit

Cited by 143 publications

References 28 publications

Translating the Genome in Time and Space: Specialized Ribosomes, RNA Regulons, and RNA-Binding Proteins

Translating the Genome in Time and Space: Specialized Ribosomes, RNA Regulons, and RNA-Binding Proteins

Alteration of a 30S Ribosomal Protein Accompanying the ram Mutation in Escherichia coli

Altered Chloroplast Ribosomal Proteins Associated with Erythromycin-Resistant Mutants in Two Genetic Systems of Chlamydomonas reinhardi

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