Iron-mediated degradation of ribosomes under oxidative stress is attenuated by manganese

Daniel G.J. Smethurst, Nikolay Kovalev, Erica R. McKenzie, Dimitri G. Pestov, Natalia Shcherbik

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

Protein biosynthesis is fundamental to cellular life and requires the efficient functioning of the translational machinery. At the center of this machinery is the ribosome, a ribonucleoprotein complex that depends heavily on Mg2+for structure. Recent work has indicated that other metal cations can substitute for Mg2+, raising questions about the role different metals may play in the maintenance of the ribosome under oxidative stress conditions. Here, we assess ribosomal integrity following oxidative stress both in vitro and in cells to elucidate details of the interactions between Fe2+and the ribosome and identifyMn2+as a factor capable of attenuating oxidant-induced Fe2+-mediated degradation of rRNA.We report that Fe2+promotes degradation of all rRNA species of the yeast ribosome and that it is bound directly to RNA molecules. Furthermore, we demonstrate that Mn2+competes with Fe2+for rRNA-binding sites and that protection of ribosomes from Fe2+-mediated rRNA hydrolysis correlates with the restoration of cell viability. Our data, therefore, suggest a relationship between these two transitionmetals in controlling ribosome stability under oxidative stress.

Original languageEnglish (US)
Pages (from-to)17200-17214
Number of pages15
JournalJournal of Biological Chemistry
Volume295
Issue number50
DOIs
StatePublished - Dec 11 2020

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Iron-mediated degradation of ribosomes under oxidative stress is attenuated by manganese'. Together they form a unique fingerprint.

Cite this