Interaction of the cytoplasmic membrane and ribosomes in Escherichia coli; Altered ribosomal proteins in sucrose-dependent spectinomycin-resistant mutants

1977 ◽  
Vol 155 (1) ◽  
pp. 53-60 ◽  
Author(s):  
Munehiko Dombou ◽  
Takeshi Mizuno ◽  
Shoji Mizushima
1973 ◽  
Vol 127 (2) ◽  
pp. 175-189 ◽  
Author(s):  
H. G. Wittmann ◽  
G. Stöffler ◽  
D. Apirion ◽  
L. Rosen ◽  
K. Tanaka ◽  
...  

Author(s):  
G. Stöffler ◽  
R.W. Bald ◽  
J. Dieckhoff ◽  
H. Eckhard ◽  
R. Lührmann ◽  
...  

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).


Acta Naturae ◽  
2011 ◽  
Vol 3 (2) ◽  
pp. 22-33 ◽  
Author(s):  
M V Nesterchuk ◽  
P V Sergiev ◽  
O A Dontsova

1992 ◽  
Vol 267 (8) ◽  
pp. 5339-5345
Author(s):  
B Traxler ◽  
C Lee ◽  
D Boyd ◽  
J Beckwith

Sign in / Sign up

Export Citation Format

Share Document