Specific cross-linking of proteins S7 and L4 to ribosomal RNA, by UV irradiation of Escherichia coli ribosomal subunits

1975 ◽  
Vol 141 (4) ◽  
pp. 343-355 ◽  
Author(s):  
Klaus Möller ◽  
Richard Brimacombe
Keyword(s):  
Escherichia Coli ◽  
Uv Irradiation ◽  
Ribosomal Rna ◽  
Cross Linking ◽  
Ribosomal Subunits

scholarly journals The Use of Formaldehyde in RNA-Protein Cross-linking Studies with Ribosomal Subunits from Escherichia coli

1977 ◽  
Vol 76 (1) ◽  
pp. 175-187 ◽  
Author(s):  
Klaus MOLLER ◽  
Jutta RINKE ◽  
Alexander ROSS ◽  
Gerard BUDDLE ◽  
Richard BRIMACOMBE
Keyword(s):  
Escherichia Coli ◽  
Cross Linking ◽  
Ribosomal Subunits ◽  
Protein Cross Linking

scholarly journals Photochemical cross-linking of initiation factor-3 to Escherichia coli 30 S ribosomal subunits.

1980 ◽  
Vol 255 (21) ◽  
pp. 10526-10531
Author(s):  
L.A. MacKeen ◽  
L. Kahan ◽  
A.J. Wahba ◽  
I. Schwartz
Keyword(s):  
Escherichia Coli ◽  
Initiation Factor ◽  
Cross Linking ◽  
Ribosomal Subunits

Investigation of the tertiary folding of Escherichia coli ribosomal RNA by intra-RNA cross-linking in vivo

1986 ◽  
Vol 191 (1) ◽  
pp. 135-138 ◽  
Author(s):  
Wolfgang Stiege ◽  
Johannes Atmadja ◽  
Monica Zobawa ◽  
Richard Brimacombe
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Rna ◽  
Cross Linking ◽  
Tertiary Folding

Electron Microscopy of EDTA-Treated Ribosomal Subunits from Escherichia coli

1971 ◽  
Vol 29 ◽  
pp. 432-433
Author(s):  
John H. Nisbet ◽  
Henry S. Slayter
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Rna ◽  
Gradient Analysis ◽  
Ribosomal Subunit ◽  
Nuclease Activity ◽  
Final Concentration ◽  
Ribosomal Subunits ◽  
Magnesium Removal ◽  
Low Ionic Strength ◽  
Endogenous Nuclease

Several studies have indicated that treatment of ribosomes and ribosomal subunits with EDTA at low ionic strength results in the formation of slower-sedimenting species which have not lost any significant amount of protein (see, for example, reference 1). Here we attempt to follow morphologically the process of magnesium removal from the 50S ribosomal subunit of Escherichia coli, using strain Q13 which exhibits a low RNase I activity. 50S particles, initially in 0.01M Tris, 0.0001M MgCl2, pH 7.4, were treated with EDTA either by dialysis against 0.002M Tris, 0.001M EDTA, pH 7.4, or by direct addition of a 0.1M solution of EDTA to a final concentration of 0.001M. On sucrose gradients made up in the Tris-EDTA buffer, the particles sedimented as a sharp peak in the 10-12S region, with no detectable slower - sedimenting species. Sucrose gradient analysis of the ribosomal RNA following EDTA treatment of 50S subunits showed that 23S RNA were largely converted to 16S, reflecting a low level of endogenous nuclease activity in the subunit preparation.

A Stable 44S Intermediate in the Autodigestion of 50S Ribosomal Subunits

1971 ◽  
Vol 29 ◽  
pp. 430-431
Author(s):  
John H. Nisbet ◽  
Henry S. Slayter
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Ribosomal Rna ◽  
Gel Electrophoresis ◽  
Type Strain ◽  
Wild Type Strain ◽  
Ribosomal Subunit ◽  
Wild Type ◽  
Ribosomal Subunits ◽  
Type Strains

Wild - type strains of Escherichia coli are known to contain as many as four endogenous nucleases (Ref. 1). These are commonly found associated with the ribosomes after extraction from the cell, but may be removed, with the exception of RNase IV, by washing the ribosomes in NH4Cl (at 0.2 M and higher concentrations). We have examined the effect of these nucleases on the 50S ribosomal subunit of one wild-type strain, K12 (Hfr 3000), by incubating the unwashed particles at 37° in the presence of varying magnesium concentrations.At 10-4 molar magnesium (slower at 10-3 molar), the 50S particle is converted to a species sedimenting at about 44S. About 20% of the total O.D260 is liberated at the same time. Continued incubation leads to the release of more O.D260 material while the RNA remaining in the 44S (Fig. 1) particle is progressively cleaved, eventually to the point where it consists of one principal fragment of molecular weight 0.42 x 106 daltons and several lesser fragments. The ribosomal RNA and proteins have been characterized by acrylamide gel electrophoresis.

scholarly journals Altered ribosomes after inhibition of Escherichia coli by rifampicin

1971 ◽  
Vol 121 (3) ◽  
pp. 391-398 ◽  
Author(s):  
M. R. Blundell ◽  
D. G. Wild
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Rna ◽  
Ribosomal Subunits

Addition of rifampicin to growing cells of Escherichia coli affected the ribosomes. The polyribosomes first decayed to 70S ribosomes. These later dissociated to particles distinct from ribosomal subunits. The altered ribosomes sedimented more slowly than the corresponding subunits and had lost some protein; their ribosomal RNA was intact, but they were more susceptible to degradation by ribonuclease than normal ribosomes. The addition of rifampicin to preparations of lysed cells caused no detectable changes in the ribosome fraction.

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