Cautionary notes on the use of C-terminal BAK1 fusion proteins for functional studies

Plant Cell. 2011 Nov;23(11):3871-8. doi: 10.1105/tpc.111.090779. Epub 2011 Nov 30.

Abstract

Detailed phenotypic characterization reveals that several BAK1 fusion proteins with C-terminal tags strongly impair complementation of bak1 null mutants with respect to responsiveness to the bacterial pathogen-associated molecular patterns flagellin and EF-Tu. This raises concerns about the widespread use of such protein variants of this important regulatory Leu-rich repeat receptor-like kinase (RLK) for functional analyses of RLK-based signaling.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis / drug effects
  • Arabidopsis / genetics
  • Arabidopsis / metabolism
  • Arabidopsis Proteins / genetics*
  • Arabidopsis Proteins / metabolism*
  • Brassinosteroids / metabolism*
  • Flagellin / metabolism
  • Flagellin / pharmacology
  • Mutation
  • Peptide Elongation Factor Tu / metabolism
  • Peptide Elongation Factor Tu / pharmacology
  • Plants, Genetically Modified
  • Protein Kinases / metabolism
  • Protein-Serine-Threonine Kinases / genetics*
  • Protein-Serine-Threonine Kinases / metabolism*
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism*
  • Signal Transduction

Substances

  • Arabidopsis Proteins
  • Brassinosteroids
  • Recombinant Fusion Proteins
  • Flagellin
  • Protein Kinases
  • BAK1 protein, Arabidopsis
  • FLS2 protein, Arabidopsis
  • BRI1 protein, Arabidopsis
  • Protein-Serine-Threonine Kinases
  • Peptide Elongation Factor Tu