The effects of Escherichia coli and yeast DNA insertions on the growth of lambda bacteriophage

Science ◽  
1977 ◽  
Vol 196 (4286) ◽  
pp. 212-215 ◽  
Author(s):  
Cameron ◽  
R. Davis
Keyword(s):  
Escherichia Coli ◽  
Lambda Bacteriophage

scholarly journals Expression of the argA Gene Carried by a Defective Lambda Bacteriophage of Escherichia coli

1976 ◽  
Vol 125 (3) ◽  
pp. 1217-1219 ◽  
Author(s):  
Thomas Leisinger ◽  
Dieter Haas ◽  
Norman Kelker
Keyword(s):  
Escherichia Coli ◽  
Lambda Bacteriophage

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).

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