The NH2-terminal domain of Escherichia coli ribosomal protein L11. Its three-dimensional location and its role in the binding of release factors 1 and 2.

Ribosomes from three previously described mutants of Escherichia coli lacking L11 ( AM68 , AM76 , and AM77 ) supported in vitro termination with release factor 1 very poorly, but with release factor 2 had a severalfold elevation in activity for this function compared with ribosomes from a control strain or from a mutant containing unmethylated L11. L11 exerts its effect on the binding of the factors into a functional ribosomal complex with the termination codon. Reconstitution of L11 back into the L11-lacking ribosomes restored them to the control phenotype.

Multiple amino acid substitutions between murine gamma 2a heavy chain Fc regions of Ig1a and Ig1b allotypic forms.

The complete amino acid sequence of the murine gamma 2a heavy chain CBPC-101 Fc region of allotype Ig1b was determined by automated and manual Edman degradation procedures. Both chemical and enzymatic cleavages were used to obtain peptides which were purified by gel filtration followed by high-pressure liquid chromatography. The sequence was in good agreement with that predicted from the nucleotide sequence of a gamma 2a gene of allotype Ig1b except for two positions.

Mechanism of allosteric activation of glycogen phosphorylase probed by the reactivity of essential arginine residues. Identification of an arginine residue involved in the binding of glucose 1-phosphate.

We have previously reported the physicochemical and kinetic properties of glycogen phosphorylase modified by arginine-specific reagent under different conditions [Dreyfus, M., Vandenbunder, B., & Buc, H.

Purification and primary structure determination of the N-terminal blocked protein, L11, from Escherichia coli ribosomes.

Protein L11 was isolated from the 50-S subunit of Escherichia coli ribosomes, using two salt extractions and two chromatographic separations on CM-cellulose. The unusual behavior of the protein when run on sodium dodecyl sulfate electrophoresis showed multiple bands. The complete primary structure of protein L11 is presented in detail.

Identification of methylated amino acids during sequence analysis. Application to the Escherichia coli ribosomal protein L11.

Three methylated amino acid residues, one residue of N-trimethylalanine and two of N epsilon,N epsilon,N epsilon-trimethyllysine residues, are present in protein L11. The methods used for the identification and location of these unusual amino acids in the sequence of protein L11 are described. Temperature and pH modifications to the eluting buffers enabled the detection of the methylated derivatives of lysine and arginine with a Durrum analyser using routine 90 min amino acid analyses.