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Ribosomal Protein L11 Selectively Stabilizes a Tertiary Structure of the GTPase Center rRNA Domain

open access: yesJournal of Molecular Biology, 2020
The GTPase Center (GAC) RNA domain in bacterial 23S rRNA is directly bound by ribosomal protein L11, and this complex is essential to ribosome function.
Robb Welty   +2 more
exaly   +2 more sources
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Expression of the L11-L1 operon in mutants of Escherichia coli lacking the ribosomal proteins L1 or L11

Molecular and General Genetics MGG, 1981
Using a variety of immunological techniques, the supernatant levels of ribosomal proteins were measured in mutants lacking the ribosomal proteins L1 or L11, and in wild-type strains. There was a 2.5--5-fold elevation of protein L11 level in the supernatant of strains lacking protein L1, compared to wild-type.
G, Stöffler, R, Hasenbank, E R, Dabbs
openaire   +2 more sources

Functional homology between E. coli ribosomal protein L11 and B. megaterium protein BM-L11

Molecular and General Genetics MGG, 1980
Ribosomes from the thiostrepton-resistant mutant MJ1 of Bacillus megaterium completely lack a protein designated BM-L11. When assayed in vitro, such ribosomes show an impaired ability to hydrolyse GTP in the presence of the elongation factor EF-G and are unable to support the synthesis of (p)ppGpp in response to the stringent factor.
M J, Stark   +3 more
openaire   +2 more sources

Ribosomal Proteins L11 and L10.(L12)4 and the Antibiotic Thiostrepton Interact with Overlapping Regions of the 23 S rRNA Backbone in the Ribosomal GTPase Centre

open access: yesJournal of Molecular Biology, 1993
Udgivelsesdato: 1993-Dec-20The Escherichia coli ribosomal protein (r-protein) L11 and its binding site on 23 S ribosomal RNA (rRNA) are associated with ribosomal hydrolysis of guanosine 5'-triphosphate (GTP). We have used hydroxyl radical footprinting to
Stephen Douthwaite
exaly   +2 more sources

The Flexible N-terminal Domain of Ribosomal Protein L11 from Escherichia coli Is Necessary for the Activation of Stringent Factor

open access: yesJournal of Molecular Biology, 2007
The stringent response is activated by the binding of stringent factor to stalled ribosomes that have an unacylated tRNA in the ribosomal aminoacyl-site. Ribosomes lacking ribosomal protein L11 are deficient in 2 stimulating stringent factor.
Holmberg Schiavone, Lovisa,   +1 more
exaly   +2 more sources

The primary structure of rat ribosomal protein L11

Biochemical and Biophysical Research Communications, 1992
The amino acid sequence of the rat 60S ribosomal subunit protein L11 was deduced from the sequence of nucleotides in a recombinant cDNA. Ribosomal protein L11 has 178 amino acids and a molecular weight of 20,239. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 6-8 copies of the L11 gene. The mRNA for the protein is about 800
Y L, Chan, J, Olvera, V, Paz, I G, Wool
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A relaxed mutant with an altered ribosomal protein L11

Molecular and General Genetics MGG, 1976
Relaxed mutants of Escherichia coli have been isolated which have an altered electrophoretic mobility of ribosomal protein L11. It can be shown that reversion to stringency in one of these mutants occurs simultaneously with a reversion of L11 protein to tis normal mobility. The L11 structural gene, rplK, maping near rif, is carried by the bacteriophage
Jack Parker   +3 more
openaire   +2 more sources

On the biological role of ribosomal protein BM-L11 of Bacillus megaterium, homologous with Escherichia coli ribosomal protein L11

Journal of Molecular Biology, 1979
Abstract Ribosomes from a thiostrepton-resistant mutant of Bacillus megaterium lack a protein, BM-L11, which is homologous with Escherichia coli ribosomal protein L11. Such ribosomes retain partial activity in cell-free synthesis of polyphenylalanine and can be restored to full activity by reconstitution with protein BM-L11.
M, Stark, E, Cundliffe
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