Abstract Small 40S Artemia salina and large 50S Escherichia coli ribosomal subunits can be assembled into 73S hybrid monosomes active in model assays for protein synthesis. The reciprocal combination–small 30S E coli and large 60S A salina–fails to form hybrids. The 73S hybrid particles strongly resemble homologous 70S E coli and 80S A salina monosomes. The morphologic differences between the corresponding eukaryotic and prokaryotic ribosomal particles, established by electron microscopy, do not significantly affect the assembly and mutual orientation of 40S A salina and 50S E coli subunits in the heterologous monosome. The fact that the structure of the interface, the supposed site of protein synthesis, is preserved in the active hybrid implies that retention or loss of biologic activity of hybrid ribosomes is determined by the extent of conformational changes in the interface.
Abstract The small (40 S) ribosomal subunits of embryos of the brine shrimp Artemia salina and the large (50 S) subunits of Escherichia coli can engage in limited, coordinated h...
We have isolated and characterized mutants which lack one or two of sixteen of the proteins of the Escherichia coli ribosome. The mutation responsible in each case mapped close ...
Structures of 70 S ribosome complexes containing messenger RNA and transfer RNA (tRNA), or tRNA analogs, have been solved by x-ray crystallography at up to 7.8 angstrom resoluti...
The 7.8 angstrom crystal structure of the 70 S ribosome reveals a discrete double-helical bridge (B4) that projects from the 50 S subunit, making contact with the 30 S subunit. ...
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