Journal
PLANT PHYSIOLOGY
Volume 167, Issue 2, Pages 493-U335Publisher
OXFORD UNIV PRESS INC
DOI: 10.1104/pp.114.254409
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Funding
- Norwegian Research Council [213853/F20]
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The eukaryotic, highly conserved serine (Ser)/threonine-specific protein phosphatase 2A (PP2A) functions as a heterotrimeric complex composed of a catalytic (C), scaffolding (A), and regulatory (B) subunit. In Arabidopsis (Arabidopsis thaliana), five, three, and 17 genes encode different C, A, and B subunits, respectively. We previously found that a B subunit, B'theta, localized to peroxisomes due to its C-terminal targeting signal Ser-Ser-leucine. This work shows that PP2A C2, C5, andA2 subunits interact and colocalize with B'theta in peroxisomes. C and A subunits lack peroxisomal targeting signals, and their peroxisomal import depends on B'theta and appears to occur by piggybacking transport. B'theta knockout mutants were impaired in peroxisomal beta-oxidation as shown by developmental arrest of seedlings germinated without sucrose, accumulation of eicosenoic acid, and resistance to protoauxins indole-butyric acid and 2,4-dichlorophenoxybutyric acid. All of these observations strongly substantiate that a full PP2A complex is present in peroxisomes and positively affects beta-oxidation of fatty acids and protoauxins.
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