Results 121 to 130 of about 12,101 (163)
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Functional homology between E. coli ribosomal protein L11 and B. megaterium protein BM-L11
Molecular and General Genetics MGG, 1980Ribosomes 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
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The primary structure of rat ribosomal protein L11
Biochemical and Biophysical Research Communications, 1992The 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, 1976Relaxed 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
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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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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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Methylgroups of ribosomal protein L11 are not related to the synthesis of ppGpp
Molecular and General Genetics MGG, 1979Ribosomes carrying either a normally methylated or an undermethylated L11, respectively, were tested with respect to the stringency reaction in the presence of crude stringent factor. Systems with either kind of ribosomes synthesize ppGpp with the same efficiency.
R, Röhl, K H, Nierhaus
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Regulation of synthesis of Escherichia coli ribosomal proteins L1 and L11
Archives of Biochemistry and Biophysics, 1981Abstract The DNA-dependent in vitro synthesis of Escherichia coli ribosomal proteins L1 and L11 system is inhibited by the addition of L1. L11 has no effect on the synthesis of either protein. The inhibition of synthesis of both proteins by L1 appears to be at the level of translation.
N, Brot, P, Caldwell, H, Weissbach
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L16, a bifunctional ribosomal protein and the enhancing effect of L6 and L11
European Journal of Biochemistry, 1986L16 exhibits both peptide bond and transesterification activities when reconstituted into 2 M LiCl core particles. L6 and L11, when reconstituted in a similar manner in the absence of L16, manifest significant transesterification activity. Both L6 and L11 enhance the transesterification activity of L16; L11 being more active than L6 in this respect ...
R M, Baxter, N, Zahid
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Antiphase boundary formation energies in L10 and L11 superstructures
Russian Physics Journal, 1993We described an approach suitable for obtaining an analytical expression for the energy of an antiphase boundary in an ordered alloy in the hard sphere model using pair interatomic interaction potentials. Depending on the orientation of the antiphase boundary, the crystal is subdivided into two-dimensional monatomic packings parallel to the defect, and
M. D. Starostenkov +2 more
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Why is ribosomal protein L11 of Escherichia coli methylated?
1982Escherichia coli spends a significant amount of energy to synthesize one (or more than one) enzyme which further spends energy in transferring nine methyl groups from S-adenosyl-methionine (SAM) to ribosomal protein L11. Our current opinion is that spending this energy is meaningless, because an E.
Jacques Lhoest +6 more
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