The primary structure of protein L10 from Escherichia coli ribosomes

The primary structure of protein L27 from the peptidyl-tRNA binding site of Escherichia coli ribosomes.

Bromoacetyl-phenylalanyl-tRNA(phe) bound to 70S E. coli ribosomes reacts covalently with proteins of the 50S subunit. The major reactions are with proteins L2 and L27. In the presence of poly(U), 70S-bound bromoacetyl-phenylalanyl-tRNA(phe) can participate in peptidebond formation with phenylalanyl-tRNA(phe) or puromycin. Most of the products of these reactions are also found covalently attache...

Escherichia coli Ribosomes

Erythromycin binding to Escherichia coli ribosomes required K+ and Mg2+. Under optimal conditions, the dissociation constant for erythromycin binding to E. coli ribosomes was found to be 1.0 x 108M and 1.4 x 108M at 24 C and 5 C, respectively. One molecule of [I4C Jerythromycin was bound to each 70S ribosome at equilibrium. Binding of erythromycin to ribosomes was rapid and reversible. The spec...

Crystallization of Escherichia coli ribosomes.

The knowledge of the structure of the ribosome is an essential requirement to reveal its role at the molecular level in the process of protein biosynthesis. This information is being obtained by a battery of chemical, physical, immunological and genetic methods (for reviews see [1]). Important methods for the study of the three-dimensional structure of the ribosomes are X-ray crystallography an...

Mapping proteins of the 50S subunit from Escherichia coli ribosomes.

Mapping of protein positions in the ribosomal subunits was first achieved for the 30S subunit by means of neutron scattering about 15 years ago. Since the 50S subunit is almost twice as large as the 30S subunit and consists of more proteins, it was difficult to apply classical contrast variation techniques for the localisation of the proteins. Polarisation dependent neutron scattering (spin-con...

Synthesis of Nascent Protein by Ribosomes in Escherichia Coli.