A Plant Pathogen Type III Effector Protein Subverts Translational Regulation to Boost Host Polyamine Levels

Cell Host Microbe. 2019 Nov 13;26(5):638-649.e5. doi: 10.1016/j.chom.2019.09.014. Epub 2019 Oct 15.

Abstract

Pathogenic bacteria inject effector proteins into host cells to manipulate cellular processes and facilitate the infection. Transcription-activator-like effectors (TALEs), an effector class in plant pathogenic bacteria, transcriptionally activate host genes to promote disease. We identify arginine decarboxylase (ADC) genes as the host targets of Brg11, a TALE-like effector from the plant pathogen Ralstonia solanacearum. Brg11 targets a 17-bp sequence that was found to be part of a conserved 50-bp motif, termed the ADC-box, upstream of ADC genes involved in polyamine biosynthesis. The transcribed ADC-box attenuates translation from native ADC mRNAs; however, Brg11 induces truncated ADC mRNAs lacking the ADC-box, thus bypassing this translational control. As a result, Brg11 induces elevated polyamine levels that trigger a defense reaction and likely inhibits bacterial niche competitors but not R. solanacearum. Our findings suggest that Brg11 may give R. solanacearum a competitive advantage and uncover a role for bacterial effectors in regulating ternary microbe-host-microbe interactions.

Keywords: Ralstonia solanacearum; arginine decarboxylase (ADC); microbiota; polyamines; putrescine; rhizosphere; translational regulation; type III effectors; upstream open reading frame (uORF).

MeSH terms

  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Carboxy-Lyases / genetics
  • Carboxy-Lyases / metabolism*
  • Host Microbial Interactions / genetics
  • Plant Diseases / microbiology
  • Plant Leaves / metabolism
  • Plant Roots / metabolism
  • Plants / microbiology
  • Polyamines / metabolism*
  • Protein Biosynthesis / genetics
  • Ralstonia solanacearum / genetics
  • Ralstonia solanacearum / metabolism*

Substances

  • Bacterial Proteins
  • Polyamines
  • Carboxy-Lyases
  • arginine decarboxylase