Structure and macromolecular interactions of 5S RNA. 2. Parameters for the interaction of ribosomal proteins L5, L18, and L25 with 5S RNA from Escherichia coli

Biochemistry ◽  
1978 ◽  
Vol 17 (25) ◽  
pp. 5394-5398 ◽  
Author(s):  
Pierre Spierer ◽  
Alexei A. Bogdanov ◽  
Robert A. Zimmermann
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Proteins ◽  
5S Rna ◽  
Macromolecular Interactions

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.

Structural organization of escherichia coli ribosomes as determined by immuno electron microscopy

1978 ◽  
Vol 36 (2) ◽  
pp. 166-167 ◽  
Author(s):  
G. Stöffler ◽  
R.W. Bald ◽  
J. Dieckhoff ◽  
H. Eckhard ◽  
R. Lührmann ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Escherichia Coli ◽  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Ribosomal Subunit ◽  
Spatial Arrangement ◽  
Small Subunit ◽  
Antibody Binding ◽  
Immuno Electron Microscopy

A central step towards an understanding of the structure and function of the Escherichia coli ribosome, a large multicomponent assembly, is the elucidation of the spatial arrangement of its 54 proteins and its three rRNA molecules. The structural organization of ribosomal components has been investigated by a number of experimental approaches. Specific antibodies directed against each of the 54 ribosomal proteins of Escherichia coli have been performed to examine antibody-subunit complexes by electron microscopy. The position of the bound antibody, specific for a particular protein, can be determined; it indicates the location of the corresponding protein on the ribosomal surface.The three-dimensional distribution of each of the 21 small subunit proteins on the ribosomal surface has been determined by immuno electron microscopy: the 21 proteins have been found exposed with altogether 43 antibody binding sites. Each one of 12 proteins showed antibody binding at remote positions on the subunit surface, indicating highly extended conformations of the proteins concerned within the 30S ribosomal subunit; the remaining proteins are, however, not necessarily globular in shape (Fig. 1).

Posttranslational Modifications of Ribosomal Proteins in Escherichia coli

Acta Naturae ◽  
2011 ◽  
Vol 3 (2) ◽  
pp. 22-33 ◽  
Author(s):  
M V Nesterchuk ◽  
P V Sergiev ◽  
O A Dontsova
Keyword(s):  
Escherichia Coli ◽  
Posttranslational Modifications ◽  
Ribosomal Proteins
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