Expression of cell cycle regulatory genes and morphological alterations in response to salt stress in Arabidopsis thaliana

Planta. 2000 Oct;211(5):632-40. doi: 10.1007/s004250000334.


Hyperosmotic stress severely affects plant growth and development. To examine the effect of salt stress on cell cycle activity in Arabidopsis thaliana (L.) Heynh., the transcriptional regulation of a cyclin-dependent kinase, CDC2aAt, and two mitotic cyclins, Arath;CycB1;1 and Arath;CycA2;1, was studied by using the beta-glucuronidase (gus) reporter gene. Moreover, the mRNA abundance of these cell cycle genes as well as CDC2bAt were monitored during salt stress. Upon NaCl treatment, the promoter activities and transcript levels of all cell cycle genes diminished initially in the shoot apex and were subsequently induced during salt-stress adaptation. Additionally, the promoter activities of CDC2aAt and CycA2;1 decreased in the vascular cylinder of the root in correlation with reduced lateral root formation. In the root tips, a regression of CDC2aAt, CycA2;1, and CycB1;1:gus expression was observed, concomitant with a shrinkage of the root meristem and inhibition of root growth. Our data indicate that salt stress interferes with cell cycle regulation at the transcriptional level, resulting in an adaptive growth response.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis / cytology
  • Arabidopsis / genetics
  • Arabidopsis / physiology*
  • Cell Cycle / drug effects
  • Cell Cycle / genetics*
  • Cyclin-Dependent Kinases / genetics*
  • Cyclins / genetics*
  • Gene Expression Regulation, Plant*
  • Genes, Reporter
  • Glucuronidase / genetics
  • Plant Roots / cytology
  • Plant Roots / physiology
  • Plant Shoots / cytology
  • Plant Shoots / physiology
  • Plants, Genetically Modified
  • Promoter Regions, Genetic* / drug effects
  • Reverse Transcriptase Polymerase Chain Reaction
  • Saline Solution, Hypertonic / pharmacology


  • Cyclins
  • Saline Solution, Hypertonic
  • Cyclin-Dependent Kinases
  • Glucuronidase