A DEAD-box protein regulates ribosome assembly through control of ribosomal protein synthesis

Isabelle Iost, Chaitanya Jain

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

DEAD-box proteins (DBPs) comprise a large family of proteins that most commonly have been identified as regulators of ribosome assembly. The Escherichia coli DBP, SrmB, represents a model bacterial DBP whose absence impairs formation of the large ribosomal subunit (LSU). To define the basis for SrmB function, suppressors of the ribosomal defect of ΔsrmB strains were isolated. The major class of suppressors was found to map to the 5′ untranslated region (UTR) of the rplM-rpsI operon, which encodes the ribosomal proteins (r-proteins) L13 and S9. An analysis of protein abundance indicated that both r-proteins are under-produced in the ΔsrmB strain, but are increased in these suppressors, implicating r-protein underproduction as the molecular basis for the observed ribosomal defects. Reduced r-protein synthesis was determined to be caused by intrinsic transcription termination within the rplM 5′ UTR that is abrogated by SrmB. These results reveal a specific mechanism for DBP regulation of ribosomal assembly, indirectly mediated through its effects on r-protein expression.

Original languageEnglish (US)
Pages (from-to)8193-8206
Number of pages14
JournalNucleic acids research
Volume47
Issue number15
DOIs
StatePublished - Sep 1 2019

ASJC Scopus subject areas

  • Genetics

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