Protein binding and subunit association activity in particles reconstituted from Escherichia coli MRE600 50S ribosomal components

1976 ◽  
Vol 54 (5) ◽  
pp. 470-476
Author(s):  
F. K. Chu ◽  
P. Y. Maeba
Keyword(s):  
Escherichia Coli ◽  
Protein Binding ◽  
Ribosomal Rna ◽  
Ribosomal Proteins ◽  
Rna Binding ◽  
5S Rna ◽  
Ribonucleoprotein Particles ◽  
Incubation Method ◽  
Do So

Reconstituted 37S and 48S ribonucleoprotein particles were constructed by incubating Escherichia coli ribosomal RNA with total 50S ribosomal proteins by a sequential incubation method. By comparing the protein compositions of the two types of particles, the proteins that bind to 37S complexes to form 48S particles have been determined. Although only 48S particles could associate with 30S subunits, isolated 37S reconstituted particles could do so if incubated with exogenous 50S proteins. The proteins that bind under these conditions and confer upon particles the ability to associate are L2, L11, L15, L18 and L25. The involvement of these proteins in 5S RNA binding is discussed.

scholarly journals Gene activities for ribosomal components in Escherichia coli B/r

1975 ◽  
Vol 150 (3) ◽  
pp. 469-475 ◽  
Author(s):  
H Bremer ◽  
P P Dennis
Keyword(s):  
Escherichia Coli ◽  
Steady State ◽  
Ribosomal Rna ◽  
Growth Rates ◽  
Ribosomal Proteins ◽  
Rrna Genes ◽  
Steady State Growth ◽  
State Growth ◽  
Escherichia Coli B

The relative transcriptional activities of genes coding for ribosomal RNA (rRNA) and ribosomal proteins (r-proteins) at a steady-state growth rates ranging from 0.65 to 2.1 doublings/h can be estimated from previous measurements of the synthesis rates of stable and unstable RNA (Pato & von Meyenburg, 1970; Nierlich, 1972a,b; Bremer et al., 1973; Dennis & Bremer, 1973b, 1974b) and ribosomal proteins (Schleif, 1967; Dennis & Bremer, 1974a). Comparison of these transcriptional activities suggests that the expression of the r-protein genes and rRNA genes is controlled seperately.

scholarly journals Characterization of rapidly labelled ribonucleic acid in Escherichia coli by deoxyribonucleic acid–ribonucleic acid hybridization

1968 ◽  
Vol 110 (2) ◽  
pp. 251-263 ◽  
Author(s):  
G. H. Pigott ◽  
J. E. M. Midgley
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Rna ◽  
Ribonucleic Acid ◽  
Messenger Rna ◽  
Rna Binding ◽  
Hybridization Technique ◽  
E Coli ◽  
K 12 ◽  
Dna 2

1. Rapidly labelled RNA from Escherichia coli K 12 was characterized by hybridization to denatured E. coli DNA on cellulose nitrate membrane filters. The experiments were designed to show that, if sufficient denatured DNA is offered in a single challenge, practically all the rapidly labelled RNA will hybridize. With the technique employed, 75–80% hybridization efficiency could be obtained as a maximum. Even if an excess of DNA sites were offered, this value could not be improved upon in any single challenge of rapidly labelled RNA with denatured E. coli DNA. 2. It was confirmed that the hybridization technique can separate the rapidly labelled RNA into two fractions. One of these (30% of the total) was efficiently hybridized with the low DNA/RNA ratio (10:1, w/w) used in tests. The other fraction (70% of the total) was hybridized to DNA at low efficiencies with the DNA/RNA ratio 10:1, and was hybridized progressively more effectively as the amount of denatured DNA was increased. A practical maximum of 80% hybridization of all the rapidly labelled RNA was first achieved at a DNA/RNA ratio 210:1 (±10:1). This fraction was fully representative of the rapidly labelled RNA with regard to kind and relative amount of materials hybridized. 3. In competition experiments, where additions were made of unlabelled RNA prepared from E. coli DNA, DNA-dependent RNA polymerase (EC 2.7.7.6) and nucleoside 5′-triphosphates, the rapidly labelled RNA fraction hybridized at a low (10:1) DNA/RNA ratio was shown to be competitive with a product from genes other than those responsible for ribosomal RNA synthesis and thus was presumably messenger RNA. At higher DNA/rapidly labelled RNA ratios (200:1), competition with added unlabelled E. coli ribosomal RNA (without messenger RNA contaminants) lowered the hybridization of the rapidly labelled RNA from its 80% maximum to 23%. This proportion of rapidly labelled RNA was not competitive with E. coli ribosomal RNA even when the latter was in large excess. The ribosomal RNA would also not compete with the 23% rapidly labelled RNA bound to DNA at low DNA/RNA ratios. It was thus demonstrated that the major part of E. coli rapidly labelled RNA (70%) is ribosomal RNA, presumably a precursor to the RNA in mature ribosomes. 4. These studies have shown that, when earlier workers used low DNA/RNA ratios (about 10:1) in the assay of messenger RNA in bacterial rapidly labelled RNA, a reasonable estimate of this fraction was achieved. Criticisms that individual messenger RNA species may be synthesized from single DNA sites in E. coli at rates that lead to low efficiencies of messenger RNA binding at low DNA/RNA ratios are refuted. In accordance with earlier results, estimations of the messenger RNA content of E. coli in both rapidly labelled and randomly labelled RNA show that this fraction is 1·8–1·9% of the total RNA. This shows that, if any messenger RNA of relatively long life exists in E. coli, it does not contribute a measurable weight to that of rapidly labelled messenger RNA.

Structures of prokaryotic ribosomal proteins: implications for RNA binding and evolution

1995 ◽  
Vol 73 (11-12) ◽  
pp. 979-986 ◽  
Author(s):  
V. Ramakrishnan ◽  
Sue Ellen Gerchman ◽  
Jadwiga H. Kycia ◽  
Christopher Davies ◽  
Barbara L. Golden ◽  
...  
Keyword(s):  
Antibiotic Resistance ◽  
High Resolution ◽  
Ribosomal Rna ◽  
Ribosomal Proteins ◽  
Bacillus Stearothermophilus ◽  
Rna Binding ◽  
X Ray ◽  
X Ray Crystallography ◽  
Binding Regions

After along hiatus, the pace of determination of the structures of ribosomal proteins has accelerated dramatically. We discuss here the structures of five ribosomal proteins from Bacillus stearothermophilus: S5, S17, L6, L9, and L14. These structures represent several new motifs. Each of these structures has revealed new insights, and we have developed criteria for recognizing RNA-binding regions of each protein and correlating the structures with such properties as antibiotic resistance. The information here should also prove invaluable in an eventual high-resolution picture of the intact ribosome.Key words: ribosome, ribosomal proteins, ribosomal RNA, X-ray crystallography, NMR.

Ribosomal RNA: the message or matrix for ribosomal proteins

1976 ◽  
Vol 54 (2) ◽  
pp. 192-193
Author(s):  
D. R. Miller ◽  
A. T. Matheson ◽  
L. P. Visentin
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Ribosomal Protein ◽  
Ribosomal Rna ◽  
Ribosomal Proteins ◽  
Protein Sequences ◽  
Amino Acid Sequences ◽  
16S Ribosomal Rna ◽  
Degree Of Similarity

The known nucleotide sequence of Escherichia coli 16S ribosomal RNA has been converted to amino acid sequences in all possible ways, and compared to known ribosomal protein sequences. The degree of similarity is precisely what one would expect by chance alone, providing additional evidence that ribosomal proteins cannot be coded for by ribosomal RNA.

Diverse relationships between metal ions and the ribosome

2021 ◽  
Author(s):  
Genki Akanuma
Keyword(s):  
Gene Expression ◽  
Secondary Structure ◽  
Metal Ions ◽  
Structural Stability ◽  
Ribosomal Rna ◽  
Ribosomal Proteins ◽  
Rna Binding ◽  
Cellular Homeostasis ◽  
Ribosomal Subunits ◽  
Translational Activity

Abstract The ribosome requires metal ions for structural stability and translational activity. These metal ions are important for stabilizing the secondary structure of ribosomal RNA, binding of ribosomal proteins to the ribosome, and for interaction of ribosomal subunits. In this review, various relationships between ribosomes and metal ions, especially Mg2+ and Zn2+, are presented. Mg2+ regulates gene expression by modulating the translational stability and synthesis of ribosomes, which in turn contribute to the cellular homeostasis of Mg2+. In addition, Mg2+ can partly complement the function of ribosomal proteins. Conversely, a reduction in the cellular concentration of Zn2+ induces replacement of ribosomal proteins, which mobilizes free-Zn2+ in the cell and represses translation activity. Evolutional relationships between these metal ions and the ribosome are also discussed.

scholarly journals Rerouting of ribosomal proteins into splicing in plant organelles

2020 ◽  
Vol 117 (47) ◽  
pp. 29979-29987
Author(s):  
Chuande Wang ◽  
Rachel Fourdin ◽  
Martine Quadrado ◽  
Céline Dargel-Graffin ◽  
Dimitri Tolleter ◽  
...  
Keyword(s):  
Ribosomal Rna ◽  
Ribosomal Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Binding Capacity ◽  
Evolutionary Strategy ◽  
Conserved Domain ◽  
The Family ◽  
Plastid Ribosomes ◽  
Plant Organelles

Production and expression of RNA requires the action of multiple RNA-binding proteins (RBPs). New RBPs are most often created by novel combinations of dedicated RNA-binding modules. However, recruiting existing genes to create new RBPs is also an important evolutionary strategy. In this report, we analyzed the eight-member uL18 ribosomal protein family inArabidopsis. uL18 proteins share a short structurally conserved domain that binds the 5S ribosomal RNA (rRNA) and allows its incorporation into ribosomes. Our results indicate thatArabidopsisuL18-Like proteins are targeted to either mitochondria or chloroplasts. While two members of the family are found in organelle ribosomes, we show here that two uL18-type proteins function as factors necessary for the splicing of certain mitochondrial and plastid group II introns. These two proteins do not cosediment with mitochondrial or plastid ribosomes but instead associate with the introns whose splicing they promote. Our study thus reveals that the RNA-binding capacity of uL18 ribosomal proteins has been repurposed to create factors that facilitate the splicing of organellar introns.

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