Influence of translation on RppH-dependent mRNA degradation in Escherichia coli

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Published on: August 22, 2017

Jamie Richards1, Daniel J Luciano, Joel G Belasco

  • 1Kimmel Center for Biology and Medicine at the Skirball Institute, New York University School of Medicine, New York, NY 10016, USA.

Molecular Microbiology
|September 20, 2012
PubMed

Insights

Ribosome binding to mRNA influences its degradation in Escherichia coli by RNase E. Poor ribosome binding promotes 5' end-independent mRNA decay, impacting gene expression regulation.

Area of Science:

  • Bacteriology
  • Molecular Biology
  • Gene Regulation

Background:

  • Escherichia coli RNase E degrades mRNA via direct or 5' end-dependent pathways.
  • The 5' end-dependent pathway involves RppH converting 5'-triphosphate to monophosphate for RNase E binding.
  • Factors influencing pathway preference in mRNA decay are not fully understood.

Purpose of the Study:

  • To investigate the impact of ribosome binding and translocation on RNase E-mediated mRNA degradation pathways.
  • To elucidate how transcript features dictate the dominant decay mechanism.

Main Methods:

  • Utilized yeiP and trxB as model transcripts in Escherichia coli.
  • Assessed mRNA decay rates under conditions affecting ribosome binding and translocation (e.g., chloramphenicol treatment).

Main Results:

  • Ribosome binding impedes both RNase E degradation pathways.
  • Reduced ribosome binding disproportionately favors 5' end-independent decay.
  • Chloramphenicol inhibits RNase E cleavage downstream of the initiation codon but not upstream.
  • RNase E binding to a 5'-monophosphate enhances cleavage within the 5' untranslated region.

Conclusions:

  • Ribosome binding and translocation significantly influence 5' end-dependent mRNA degradation in E. coli.
  • These interactions dictate the balance between direct and 5' end-dependent decay pathways.
  • A model is proposed for mRNA decay events following pyrophosphate removal.

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