[5S RNA: structure and function].
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Adenosine Triphosphatases↗
Biomedical subjects
R L Villems
Publications and source records attributed to R L Villems.
[Stimulation of peptidyltransferase activity of 50S subunits by alcohols].
We have demonstrated that in certain conditions 50S subunits can transfer peptide moiety from peptidyl-tRNA to puromycin in the absence of alcohol. Monovalent cations NH4+ and K+ support this reaction, while Na+ and Li+ are ineffective. Optimal concentration for NH4+ is 1.8 M. Mg2+ ion concentrations above 12 mM are needed as well as an elevated temperature (30 degrees C). Using the alcohol-free puromycin reaction of 50S subunits we show that alcohol activates the peptidyl transferase center, but does not participate in the puromycin reaction. Neither does it change the protein composition of subunits.
Acyltransferases↗
[Conformational isomers of rat liver 5S ribosomal RNA].
The rat liver 5S RNA when denaturated by urea or EDTA, or even without any special treatment, undergoes conformational changes leading to the formation of three electrophoretically distinct isomeres of the molecules with relative mobilities 0.39, 0.44 and 0.47. The band with the slowest mobility corresponds apparently to the native 5S RNA since it is specific for both freshy isolated and renaturated 5S RNA. Moreover, it was found that denaturation of the immobilized 5 S RNA decreases significantly its ability to form a complex with the rat liver 60S ribosomal subunit proteins L6, L7, L8, L18 and L35.
Binding Sites↗