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

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

doi:10.1007/s00299-010-0818-8

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

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

Plant and Soil Sciences

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

Abstract

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 language	English
Pages (from-to)	249-259
Number of pages	11
Journal	Plant Cell Reports
Volume	29
Issue number	3
DOIs	https://doi.org/10.1007/s00299-010-0818-8
State	Published - 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).

Funding

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).

Funders	Funder number
Cooperative State Research, Education, and Extension Service	20053530416043
The Kentucky Tobacco Research and Development Center
Kentucky Science and Engineering Foundation	14850206189

Keywords

Arabidopsis thaliana
Cycloheximide
Herbicide tolerance
Hygromycin B
L-Phosphinothricin
Proteolysis

ASJC Scopus subject areas

Agronomy and Crop Science
Plant Science

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10.1007/s00299-010-0818-8

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title = "Arabidopsis sensitivity to protein synthesis inhibitors depends on 26S proteasome activity",

abstract = "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.",

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AU - Kurepa, Jasmina

AU - Karangwa, Consolée

AU - Duke, Liliana Sfichi

AU - Smalle, Jan A.

PY - 2010/3

Y1 - 2010/3

N2 - 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.

AB - 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.

KW - Arabidopsis thaliana

KW - Cycloheximide

KW - Herbicide tolerance

KW - Hygromycin B

KW - L-Phosphinothricin

KW - Proteolysis

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JO - Plant Cell Reports

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

Abstract

Bibliographical note

Funding

Keywords

ASJC Scopus subject areas

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