Variations in stoichiometry of ribosomal proteins in Escherichia coli

Deusser, Ellen; Weber, Hans; Subramanian, Alap R.

doi:10.1016/0022-2836(74)90583-x

Cited by 25 publications

(10 citation statements)

References 17 publications

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“…S1 is a component of actively translating polyribosomes but is often lost from tight-coupled ribosome preparations such as ours when cells are slowly cooled in the absence of puromycin, or by co-precipitation with rRNA during acid extaction. 5, [49][50][51] In order to confirm the proposed identities and post-translational modifications, several series of experiments based on enzymatic digestion experiments were performed. These experiments confirmed the identifications of all but the smallest proteins from the large ribosomal subunit (see below).…”

Section: Resultsmentioning

confidence: 99%

A Top-Down/Bottom-Up Study of the Ribosomal Proteins of Caulobacter crescentus

et al. 2006

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Ribosomes from the gram-negative α-proteobacterium Caulobacter crescentus were isolated using standard methods. Proteins were separated using a two-dimensional liquid chromatographic system that allowed the analysis of whole proteins by direct coupling to an ESI-QTOF mass spectrometer and of proteolytic digests by a number of mass spectrometric methods. The masses of 53 of 54 ribosomal proteins were directly measured. Protein identifications and proposed post-translational modifications were supported by proteolysis with trypsin, endoprotease Glu-C and exoproteases carboxypeptidases Y and P. Tryptic peptide mass maps show an average sequence coverage of 62%, and carboxypeptidase C-terminal sequence tagging provided unambiguous identification of the small, highly basic proteins of the large subunit. C. crescentus presents some post-translational modifications that are similar to those of E. coli (e. g. N-terminal acetylation of S9 and S18) along with some unique variations, such as a near absence of L7 and extensive modification of L11. The comprehensive description of this organism's ribosomal proteome provides a foundation for the study of ribosome structure, dependence of post-translational modifications on growth conditions, and the evolution of subcellular organelles.

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Section: Resultsmentioning

confidence: 99%

A Top-Down/Bottom-Up Study of the Ribosomal Proteins of Caulobacter crescentus

et al. 2006

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“…It was reported that free 30 S subunits lose proteins Sl and S2 after formation of the 30 S initiation complex [26]. On the other hand, polysomes contain higher amounts of proteins Sl and S2 (S6, S21, L7 and L12 as well) than run-off ribosomes [27]. Furthermore, polysomes generated under the direction of poly(U) contain approximately one molecule of S 1 per ribosome [28] ; whereas, this is not the case with 30 S subunits.…”

Section: Binding Of Mrnamentioning

confidence: 99%

“…Accordingly, protein S21 was not detected on native 30 S subunits in contrast to monosomes and polysomes [35,38]. It is present in higher amounts in polysomes than in run off ribosomes [27] . Ribosomes of cells grown in rich medium contain two to three times more S21 than those of cells grown in minimal medium [39].…”

Section: Binding Off-met-trnafe'mentioning

confidence: 99%

Active sites in Escherichia coli ribosomes

et al. 1974

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The model of active sites in E. coli ribosome illustrated in the figure is based on the presently available experimental results. It is far from being complete and should not be overinterpreted as an accurate topographical model. More data on the functional role of ribosomal components and on the topography of the subunits can be expected in the near future and will add to the knowledge on the active sites in ribosomes.

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“…The two fractions, however, gave the same proportion of L7 and L12. Evidently, functioning ribosomes (i.e., polysomes) contain both forms of this protein (15).…”

Section: Methodsmentioning

confidence: 99%

“…Nevertheless, the possibility of distinct roles in vivo is suggested by the finding (14) that ribosomes from broth-grown cells contained two to three times as much L12 as ribosomes from cells grown in glucose-minimal medium, while L7 content showed only slight variation under the same conditions. It has also been found recently that polysomal ribosomes may contain a somewhat greater amount of both L7 and L12 than free ribosomes (15).…”

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confidence: 99%

Alteration in the Acetylation Level of Ribosomal Protein L12 During Growth Cycle of Escherichia coli

Ramagopal

Subramanian

1974

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

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The relative content in ribosomes of L7 and L12, the two forms of a protein in the 50S subunit specifically involved in GTP hydrolysis, is found to undergo a striking shift with the growth phase of E. coli. The content of L12 (nonacetylated form) increases during early logarithmic phase, becoming about 85% of the total before midlogarithmic phase. Thereafter, L7 (N-acetylated form) content begins to increase, eventually becoming 75-80% in

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Variations in stoichiometry of ribosomal proteins in Escherichia coli

Cited by 25 publications

References 17 publications

A Top-Down/Bottom-Up Study of the Ribosomal Proteins of Caulobacter crescentus

A Top-Down/Bottom-Up Study of the Ribosomal Proteins of Caulobacter crescentus

Active sites in Escherichia coli ribosomes

Alteration in the Acetylation Level of Ribosomal Protein L12 During Growth Cycle of Escherichia coli

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