A nuclear mutation conferring thiostrepton resistance in Chlamydomonas reinhardtii affects a chloroplast ribosomal protein related to Escherichia coli ribosomal protein L11

1993 ◽  
Vol 241-241 (5-6) ◽  
pp. 564-572 ◽  
Author(s):  
K.B. McElwain ◽  
J.E. Boynton ◽  
N.W. Gillham
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Protein ◽  
Chlamydomonas Reinhardtii ◽  
Nuclear Mutation ◽  
Ribosomal Protein L11

Why is ribosomal protein L11 of Escherichia coli methylated?

1982 ◽  
pp. 79-82 ◽  
Author(s):  
Jacques Lhoest ◽  
Françoise Hespel ◽  
Jean F Lontie ◽  
Eugenio Andrade ◽  
Colette Digneffe ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Protein ◽  
Ribosomal Protein L11

scholarly journals Mutants of Escherichia coli lacking ribosomal protein L11.

1980 ◽  
Vol 255 (21) ◽  
pp. 10517-10522
Author(s):  
G. Stöffler ◽  
E. Cundliffe ◽  
M. Stöffler-Meilicke ◽  
E.R. Dabbs
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Protein ◽  
Ribosomal Protein L11

scholarly journals Involvement of the N Terminus of Ribosomal Protein L11 in Regulation of the RelA Protein of Escherichia coli

2001 ◽  
Vol 183 (22) ◽  
pp. 6532-6537 ◽  
Author(s):  
Xiaoming Yang ◽  
Edward E. Ishiguro
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Ribosomal Protein ◽  
Stringent Response ◽  
Direct Interaction ◽  
Binding Activity ◽  
Site Directed Mutagenesis ◽  
Ribosome Binding ◽  
N Terminus ◽  
Ribosomal Protein L11

ABSTRACT Amino acid-deprived rplK (previously known asrelC) mutants of Escherichia coli cannot activate (p)ppGpp synthetase I (RelA) and consequently exhibit relaxed phenotypes. The rplK gene encodes ribosomal protein L11, suggesting that L11 is involved in regulating the activity of RelA. To investigate the role of L11 in the stringent response, a derivative ofrplK encoding L11 lacking the N-terminal 36 amino acids (designated ′L11) was constructed. Bacteria overexpressing ′L11 exhibited a relaxed phenotype, and this was associated with an inhibition of RelA-dependent (p)ppGpp synthesis during amino acid deprivation. In contrast, bacteria overexpressing normal L11 exhibited a typical stringent response. The overexpressed ′L11 was incorporated into ribosomes and had no effect on the ribosome-binding activity of RelA. By several methods (yeast two-hybrid, affinity blotting, and copurification), no direct interaction was observed between the C-terminal ribosome-binding domain of RelA and L11. To determine whether the proline-rich helix of L11 was involved in RelA regulation, the Pro-22 residue was replaced with Leu by site-directed mutagenesis. The overexpression of the Leu-22 mutant derivative of L11 resulted in a relaxed phenotype. These results indicate that the proline-rich helix in the N terminus of L11 is involved in regulating the activity of RelA.

scholarly journals The binding site for ribosomal protein L11 within 23 S ribosomal RNA of Escherichia coli.

1981 ◽  
Vol 256 (23) ◽  
pp. 12301-12305 ◽  
Author(s):  
F.J. Schmidt ◽  
J. Thompson ◽  
K. Lee ◽  
J. Dijk ◽  
E. Cundliffe
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Protein ◽  
Binding Site ◽  
Ribosomal Rna ◽  
Ribosomal Protein L11
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