Arabidopsis sensitivity to protein synthesis inhibitors depends on 26S proteasome activity

Jasmina Kurepa, Consolée Karangwa, Liliana Sfichi Duke, Jan A. Smalle

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


The 26S proteasome (26SP), the central protease of the ubiquitin-dependent proteolysis pathway, controls the regulated proteolysis of functional proteins and the removal of misfolded and damaged proteins. In Arabidopsis, cellular and stress response phenotypes of a number of mutants with partially impaired 26SP function have been reported. Here, we describe the responses of proteasome mutants to protein synthesis inhibitors. We show that the rpt2a-3, rpn10-1 and rpn12a-1 mutants are hypersensitive to the antibiotic hygromycin B, and tolerant to the translation inhibitor cycloheximide (CHX) and herbicide L-phosphinothricin (PPT). In addition to the novel mechanism for herbicide tolerance, our data suggests that the combination of hygromycin B, CHX and PPT growth-response assays could be used as a facile diagnostic tool to detect altered 26SP function in plant mutants and transgenic lines.

Original languageEnglish
Pages (from-to)249-259
Number of pages11
JournalPlant Cell Reports
Issue number3
StatePublished - Mar 2010

Bibliographical note

Funding Information:
Acknowledgments We are grateful to Dr. Songhu Wang and Yan Li for critical reading of the manuscript. This work was supported by grants from the Kentucky Tobacco Research and Development Center, the USDA Cooperative State Research, Education and Extension Service (Grant number 20053530416043) and the Kentucky Science and Engineering Foundation (Grant number 14850206189).


  • Arabidopsis thaliana
  • Cycloheximide
  • Herbicide tolerance
  • Hygromycin B
  • L-Phosphinothricin
  • Proteolysis

ASJC Scopus subject areas

  • Agronomy and Crop Science
  • Plant Science


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