scholarly journals Structural features of the binding site for ribosomal protein S8 in Escherichia coli 16S rRNA defined using NMR spectroscopy

1997 ◽  
Vol 94 (6) ◽  
pp. 2139-2144 ◽  
Author(s):  
K. Kalurachchi ◽  
K. Uma ◽  
R. A. Zimmermann ◽  
E. P. Nikonowicz
Keyword(s):  
Escherichia Coli ◽  
Nmr Spectroscopy ◽  
16S Rrna ◽  
Ribosomal Protein ◽  
Binding Site ◽  
Structural Features

Minimal 16S rRNA binding site and role of conserved nucleotides in Escherichia coli ribosomal protein S8 recognition

1993 ◽  
Vol 215 (3) ◽  
pp. 787-792 ◽  
Author(s):  
Marylene MOUGEL ◽  
Christine ALLMANG ◽  
Flore EYERMANN ◽  
Claire CACHIA ◽  
Bernard EHRESMANN ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
16S Rrna ◽  
Ribosomal Protein ◽  
Binding Site

Mutational and Structural Analysis of the RNA Binding Site for Escherichia coli Ribosomal Protein S7

1994 ◽  
Vol 244 (1) ◽  
pp. 74-85 ◽  
Author(s):  
François Dragon ◽  
Catherine Payant ◽  
Léa Brakier-Gingras
Keyword(s):  
Escherichia Coli ◽  
Structural Analysis ◽  
Ribosomal Protein ◽  
Binding Site ◽  
Rna Binding

scholarly journals 16S rRNA Mutations That Confer Tetracycline Resistance in Helicobacter pylori Decrease Drug Binding in Escherichia coli Ribosomes

2005 ◽  
Vol 187 (11) ◽  
pp. 3708-3712 ◽  
Author(s):  
Lisa Nonaka ◽  
Sean R. Connell ◽  
Diane E. Taylor
Keyword(s):  
Escherichia Coli ◽  
Helicobacter Pylori ◽  
16S Rrna ◽  
Binding Site ◽  
Tetracycline Resistance ◽  
Drug Binding ◽  
Multicopy Plasmid ◽  
Wild Type ◽  
E Coli ◽  
H Pylori

ABSTRACT Tetracycline resistance in clinical isolates of Helicobacter pylori has been associated with nucleotide substitutions at positions 965 to 967 in the 16S rRNA. We constructed mutants which had different sequences at 965 to 967 in the 16S rRNA gene present on a multicopy plasmid in Escherichia coli strain TA527, in which all seven rrn genes were deleted. The MICs for tetracycline of all mutants having single, double, or triple substitutions at the 965 to 967 region that were previously found in highly resistant H. pylori isolates were higher than that of the mutant exhibiting the wild-type sequence of tetracycline-susceptible H. pylori. The MIC of the mutant with the 965TTC967 triple substitution was 32 times higher than that of the E. coli mutant with the 965AGA967 substitution present in wild-type H. pylori. The ribosomes extracted from the tetracycline-resistant E. coli 965TTC967 variant bound less tetracycline than E. coli with the wild-type H. pylori sequence at this region. The concentration of tetracycline bound to the ribosome was 40% that of the wild type. The results of this study suggest that tetracycline binding to the primary binding site (Tet-1) of the ribosome at positions 965 to 967 is influenced by its sequence patterns, which form the primary binding site for tetracycline.

scholarly journals RimM and RbfA Are Essential for Efficient Processing of 16S rRNA in Escherichia coli

1998 ◽  
Vol 180 (1) ◽  
pp. 73-82 ◽  
Author(s):  
Göran O. Bylund ◽  
L. Charlotta Wipemo ◽  
L. A. Carina Lundberg ◽  
P. Mikael Wikström
Keyword(s):  
Escherichia Coli ◽  
Growth Rate ◽  
16S Rrna ◽  
Ribosomal Protein ◽  
Slow Growth ◽  
Translational Efficiency ◽  
Ribosome Binding ◽  
Suppressor Mutations ◽  
Binding Factor ◽  
Efficient Processing

ABSTRACT The trmD operon is located at 56.7 min on the genetic map of the Escherichia coli chromosome and contains the genes for ribosomal protein (r-protein) S16, a 21-kDa protein (RimM, formerly called 21K), the tRNA (m1G37)methyltransferase (TrmD), and r-protein L19, in that order. Previously, we have shown that strains from which the rimM gene has been deleted have a sevenfold-reduced growth rate and a reduced translational efficiency. The slow growth and translational deficiency were found to be partly suppressed by mutations in rpsM, which encodes r-protein S13. Further, the RimM protein was shown to have affinity for free ribosomal 30S subunits but not for 30S subunits in the 70S ribosomes. Here we have isolated several new suppressor mutations, most of which seem to be located close to or within the nusA operon at 68.9 min on the chromosome. For at least one of these mutations, increased expression of the ribosome binding factor RbfA is responsible for the suppression of the slow growth and translational deficiency of a ΔrimM mutant. Further, the RimM and RbfA proteins were found to be essential for efficient processing of 16S rRNA.

Dissection of the 16S rRNA binding site for ribosomal protein S4

1990 ◽  
Vol 1050 (1-3) ◽  
pp. 34-37 ◽  
Author(s):  
Amalia Sapag ◽  
Jailaxmi V. Vartikar ◽  
David E. Draper
Keyword(s):  
16S Rrna ◽  
Ribosomal Protein ◽  
Binding Site ◽  
Ribosomal Protein S4
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