Modulation of RNA polymerase II phosphorylation downstream of pathogen perception orchestrates plant immunity

Cell Host Microbe. 2014 Dec 10;16(6):748-58. doi: 10.1016/j.chom.2014.10.018. Epub 2014 Nov 26.

Abstract

Perception of microbe-associated molecular patterns (MAMPs) elicits host transcriptional reprogramming as part of the immune response. Although pathogen perception is well studied, the signaling networks orchestrating immune gene expression remain less clear. In a genetic screen for components involved in the early immune gene transcription reprogramming, we identified Arabidopsis RNA polymerase II C-terminal domain (CTD) phosphatase-like 3 (CPL3) as a negative regulator of immune gene expression. MAMP perception induced rapid and transient cyclin-dependent kinase C (CDKC)-mediated phosphorylation of Arabidopsis CTD. The CDKCs, which are in turn phosphorylated and activated by a canonical MAP kinase (MAPK) cascade, represent a point of signaling convergence downstream of multiple immune receptors. CPL3 directly dephosphorylated CTD to counteract MAPK-mediated CDKC regulation. Thus, modulation of the phosphorylation dynamics of eukaryotic RNA polymerase II transcription machinery by MAPKs, CTD kinases, and phosphatases constitutes an essential mechanism for rapid orchestration of host immune gene expression and defense upon pathogen attacks.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Arabidopsis / enzymology*
  • Arabidopsis / genetics
  • Arabidopsis / immunology
  • Arabidopsis / microbiology
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism
  • Cyclin-Dependent Kinases / genetics
  • Cyclin-Dependent Kinases / metabolism
  • Gene Expression Regulation, Plant
  • Mitogen-Activated Protein Kinase Kinases / genetics
  • Mitogen-Activated Protein Kinase Kinases / metabolism
  • Phosphoprotein Phosphatases / genetics
  • Phosphoprotein Phosphatases / metabolism
  • Phosphorylation
  • Plant Diseases / immunology
  • Plant Diseases / microbiology
  • Protein Structure, Tertiary
  • Pseudomonas syringae / physiology
  • RNA Polymerase II / chemistry
  • RNA Polymerase II / genetics
  • RNA Polymerase II / metabolism*

Substances

  • Arabidopsis Proteins
  • Cyclin-Dependent Kinases
  • Mitogen-Activated Protein Kinase Kinases
  • RNA Polymerase II
  • At2g33540 protein, Arabidopsis
  • Phosphoprotein Phosphatases