OsCIPK7 point-mutation leads to conformation and kinase-activity change for sensing cold response

J Integr Plant Biol. 2019 Dec;61(12):1194-1200. doi: 10.1111/jipb.12800. Epub 2019 May 2.

Abstract

Calcineurin B-like interacting protein kinases (CIPKs) play important roles via environmental stress. However, less is known how to sense the stress in molecular structure conformation level. Here, an OsCIPK7 mutant via TILLING procedure with a point mutation in the kinase domain showed increased chilling tolerance, which could be potentially used in the molecular breeding. We found that this point mutation of OsCIPK7 led to a conformational change in the activation loop of the kinase domain, subsequently with an increase of protein kinase activity, thus conferred an increased tolerance to chilling stress.

MeSH terms

  • Adaptation, Physiological
  • Amino Acid Sequence
  • Base Sequence
  • Cold Temperature*
  • Oryza / enzymology*
  • Oryza / physiology*
  • Plant Proteins / chemistry*
  • Plant Proteins / genetics*
  • Plant Proteins / metabolism
  • Point Mutation / genetics*
  • Protein Conformation
  • Protein Kinases / metabolism*
  • Spectroscopy, Fourier Transform Infrared

Substances

  • Plant Proteins
  • Protein Kinases