Metal ions and ribosomal conformation

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Abstract

Divalent metal ions play an important role in preserving the compact structure of ribosomes. This is reflected in the specific viscosity (ηsp) of the ribosomal solution which is increased at elevated temperatures in the presence of EDTA. Dialysis of EDTA-treated ribosomes (unfolded particles) against 1 mM Zn2+, Ni2+, Mn2+, Co2+ and Fe2+ (present in natural ribosomes) results in a sedimentation profile closely similar to that of natural ribosomes, indicating reversibility of the unfolding process caused by EDTA. On the other hand, addition of Mg2+ to the unfolded particles results in intermediate s values only. An extended thermal denaturation scheme of ribosomes, taking into consideration the role of metal ions, is proposed.

Original languageEnglish
Pages (from-to)76-86
Number of pages11
JournalBBA Section Nucleic Acids And Protein Synthesis
Volume195
Issue number1
DOIs
StatePublished - 19 Nov 1969
Externally publishedYes

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