Role of ribosome assembly in Escherichia coli ribosomal RNA degradation

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

DEAD-Box proteins (DBPs) constitute a prominent class of RNA remodeling factors that play a role in virtually all aspects of RNA metabolism. To better define their cellular functions, deletions in the genes encoding each of the Escherichia coli DBPs were combined with mutations in genes encoding different Ribonucleases (RNases). Significantly, double-deletion strains lacking Ribonuclease R (RNase R) and either the DeaD or SrmB DBP were found to display growth defects and an enhanced accumulation of ribosomal RNA (rRNA) fragments. As RNase R is known to play a key role in removing rRNA degradation products, these observations initially suggested that these two DBPs could be directly involved in the same process. However, additional investigations indicated that DeaD and SrmB-dependent rRNA breakdown is caused by delays in ribosome assembly that increase the exposure of nascent RNAs to endonucleolytic cleavage. Consistent with this notion, mutations in factors known to be important for ribosome assembly also resulted in enhanced rRNA breakdown. Additionally, significant levels of rRNA breakdown products could be visualized in growing cells even in the absence of assembly defects. These findings reveal a hitherto unappreciated mechanism of rRNA degradation under conditions of both normal and abnormal ribosome assembly.

Original languageEnglish (US)
Pages (from-to)11048-11060
Number of pages13
JournalNucleic Acids Research
Volume46
Issue number20
DOIs
StatePublished - Nov 16 2018
Externally publishedYes

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Ribosomal RNA
Ribosomes
Escherichia coli
RNA Stability
Proteins
Mutation
Gene Deletion
Ribonucleases
RNA
Growth
Genes

ASJC Scopus subject areas

  • Genetics

Cite this

Role of ribosome assembly in Escherichia coli ribosomal RNA degradation. / Jain, Chaitanya.

In: Nucleic Acids Research, Vol. 46, No. 20, 16.11.2018, p. 11048-11060.

Research output: Contribution to journalArticle

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