PMID: 6402016Mar 10, 1983Paper

The lasting ribosome alteration produced by virginiamycin M disappears upon removal of certain ribosomal proteins

Biochimica Et Biophysica Acta
P MoureauC G Cocito

Abstract

Transient incubation of bacterial ribosomes with virginiamycin M produces a lasting damage of 50 S ribosomal subunits, whereby the elongation of peptide chains is still blocked after removal of the antibiotic. To elucidate the mechanism of this inactivation, ribosomal proteins were stepwise removed from 50 S subunits previously incubated with virginiamycin M, and cores were submitted to three functional tests. Total removal of proteins L7, L8, L12 and L16, and partial removal of L6, L9, L10 and L11, resulted in a loss of the virginiamycin M-induced alteration. When the split protein fractions were added back to these cores, unaltered functional particles were obtained. The reconstituted subunits, on the other hand, proved fully sensitive to virginiamycin M in vitro as they underwent, upon transient contact with the antibiotic, an alteration comparable to that of native particles. It is concluded that the virginiamycin M-induced ribosome damage is due to the production of a stable conformational change of the 50 S subunit. These data parallel those of an accompanying paper (Cocito, C., Vanlinden, F. and Branlant, C. (1983) Biochim. Biophys. Acta 739, 158-163) showing the intactness of all rRNA species from ribosomes treated in v...Continue Reading

References

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Citations

Feb 2, 2011·Proceedings of the National Academy of Sciences of the United States of America·Matthew J BelousoffAda Yonath
Feb 15, 2001·Expert Opinion on Investigational Drugs·G Bonfiglio, P M Furneri

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