Repetitive DNA in Escherichia coli: Multiple sequences complementary to small stable RNAs

1979 ◽  
Vol 172 (3) ◽  
pp. 339-343 ◽  
Author(s):  
Stephen C. Bailey ◽  
David Apirion
Keyword(s):  
Escherichia Coli ◽  
Repetitive Dna ◽  
Multiple Sequences ◽  
Small Stable Rnas

Development of SCAR primers based on a repetitive DNA fingerprint for Escherichia coli detection

2013 ◽  
Vol 51 (1) ◽  
pp. 31-35 ◽  
Author(s):  
Aphidech Sangdee ◽  
Sitakan Natphosuk ◽  
Adunwit Srisathan ◽  
Kusavadee Sangdee
Keyword(s):  
Escherichia Coli ◽  
Repetitive Dna ◽  
Dna Fingerprint ◽  
Scar Primers

scholarly journals Intramolecular amplification of the tetracycline resistance determinant of transposon Tn1771 inEscherichia coli

1979 ◽  
Vol 33 (3) ◽  
pp. 253-260 ◽  
Author(s):  
F. Schöffl ◽  
A. Pühler
Keyword(s):  
Molecular Structure ◽  
Escherichia Coli ◽  
Gene Amplification ◽  
Molecular Analysis ◽  
Repetitive Dna ◽  
Tetracycline Resistance ◽  
Conjugative Plasmid ◽  
Resistance Determinant ◽  
Inescherichia Coli ◽  
Very High

SUMMARYStrains ofEscherichia coliharbouring a conjugative plasmid that carries a transposon for tetracycline resistance (Tn1771) were found to be adaptable to very high tetracycline concentrations. The molecular analysis of plasmids isolated from strains with enhanced levels of tetracycline resistance revealed an intramolecular amplification of the resistance determinant of the tetracycline transposon.A model for the molecular structure of the transposon is presented, which suggests that there are three repetitive DNA segments on Tn1771. This accounts for the properties both of transposition and of gene amplification.

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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