Disparate peroxisome‐related defects in Arabidopsis pex6 and pex26 mutants link peroxisomal retrotranslocation and oil body utilization

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dc.citation.firstpage110en_US
dc.citation.issueNumber1en_US
dc.citation.journalTitleThe Plant Journalen_US
dc.citation.lastpage128en_US
dc.citation.volumeNumber92en_US
dc.contributor.authorGonzalez, Kim L.en_US
dc.contributor.authorFleming, Wendell A.en_US
dc.contributor.authorKao, Yun-Tingen_US
dc.contributor.authorWright, Zachary J.en_US
dc.contributor.authorVenkova, Savina V.en_US
dc.contributor.authorVentura, Meredith J.en_US
dc.contributor.authorBartel, Bonnieen_US
dc.date.accessioned2018-12-17T18:51:35Zen_US
dc.date.available2018-12-17T18:51:35Zen_US
dc.date.issued2017en_US
dc.description.abstractCatabolism of fatty acids stored in oil bodies is essential for seed germination and seedling development in Arabidopsis. This fatty acid breakdown occurs in peroxisomes, organelles that sequester oxidative reactions. Import of peroxisomal enzymes is facilitated by peroxins including PEX5, a receptor that delivers cargo proteins from the cytosol to the peroxisomal matrix. After cargo delivery, a complex of the PEX1 and PEX6 ATPases and the PEX26 tail‐anchored membrane protein removes ubiquitinated PEX5 from the peroxisomal membrane. We identified Arabidopsis pex6 and pex26 mutants by screening for inefficient seedling β‐oxidation phenotypes. The mutants displayed distinct defects in growth, response to a peroxisomally metabolized auxin precursor, and peroxisomal protein import. The low PEX5 levels in these mutants were increased by treatment with a proteasome inhibitor or by combining pex26 with peroxisome‐associated ubiquitination machinery mutants, suggesting that ubiquitinated PEX5 is degraded by the proteasome when the function of PEX6 or PEX26 is reduced. Combining pex26 with mutations that increase PEX5 levels either worsened or improved pex26 physiological and molecular defects, depending on the introduced lesion. Moreover, elevating PEX5 levels via a 35S:PEX5 transgene exacerbated pex26 defects and ameliorated the defects of only a subset of pex6 alleles, implying that decreased PEX5 is not the sole molecular deficiency in these mutants. We found peroxisomes clustered around persisting oil bodies in pex6 and pex26 seedlings, suggesting a role for peroxisomal retrotranslocation machinery in oil body utilization. The disparate phenotypes of these pex alleles may reflect unanticipated functions of the peroxisomal ATPase complex.en_US
dc.identifier.citationGonzalez, Kim L., Fleming, Wendell A., Kao, Yun-Ting, et al.. "Disparate peroxisome‐related defects in Arabidopsis pex6 and pex26 mutants link peroxisomal retrotranslocation and oil body utilization." <i>The Plant Journal,</i> 92, no. 1 (2017) Wiley: 110-128. https://doi.org/10.1111/tpj.13641.en_US
dc.identifier.doihttps://doi.org/10.1111/tpj.13641en_US
dc.identifier.urihttps://hdl.handle.net/1911/103870en_US
dc.language.isoengen_US
dc.publisherWileyen_US
dc.subject.keywordperoxisomesen_US
dc.subject.keywordperoxinsen_US
dc.subject.keywordPEX6en_US
dc.subject.keywordPEX26en_US
dc.subject.keywordArabidopsis thalianaen_US
dc.subject.keywordretrotranslocation machineryen_US
dc.subject.keywordAAA ATPasesen_US
dc.subject.keywordoil bodiesen_US
dc.subject.keywordAt1g03000en_US
dc.subject.keywordAt3g10572en_US
dc.titleDisparate peroxisome‐related defects in Arabidopsis pex6 and pex26 mutants link peroxisomal retrotranslocation and oil body utilizationen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpost-printen_US
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