In Planta Evidence for the Involvement of a Ubiquitin Conjugating Enzyme (UBC E2 clade) in Negative Regulation of Disease Resistance

One of the three main components of the ubiquitylation system is an ubiquitin-conjugating enzyme (UBC, E2) that attaches ubiquitin (Ub) to a substrate. A strong link has been discovered between ubiquitylation and regulation of plant defense responses against plant pathogens. In this study, the role...

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Bibliographic Details
Published in:Plant molecular biology reporter 2013-04, Vol.31 (2), p.323-334
Main Authors: Unver, Turgay, Turktas, Mine, Budak, Hikmet
Format: Article
Language:English
Subjects:
Bioinformatics
Biomedical and Life Sciences
Disease resistance
Enzymes
Gene silencing
Homology
Hsp90 protein
Inoculation
Life Sciences
Localization
Metabolomics
mRNA
Original Paper
Pathogens
Plant Breeding/Biotechnology
Plant Sciences
Proteomics
Ubiquitin
Ubiquitin-conjugating enzyme
Viruses
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Summary:One of the three main components of the ubiquitylation system is an ubiquitin-conjugating enzyme (UBC, E2) that attaches ubiquitin (Ub) to a substrate. A strong link has been discovered between ubiquitylation and regulation of plant defense responses against plant pathogens. In this study, the role of UBC in response to pathogen attack is investigated in Arabidopsis thaliana as it has three Ubc gene homologs (Ubc1-1, Ubc2-1, and Ubc3-1). Analysis of single mutants of these three Ubc genes revealed enhanced disease resistance. Moreover, virus-induced gene silencing (VIGS) analysis revealed an enhanced level of resistance of Nicotiana benthamiana following inoculation with avirulent Pto DC3000 and virulent Pto DC3000 hopQ1-1 strains. In addition, RAR1, SGT1, and HSP90 mRNA levels are up-regulated following Ubc2 silencing. This study shows that UBC2 negatively regulates disease resistance via SGT1 level. Sub-cellular localization assay of UBC2 protein indicates its nuclear and cytoplasmic localization in planta.
ISSN:0735-9640
1572-9818
DOI:10.1007/s11105-012-0502-y