A pex1 missense mutation improves peroxisome function in a subset of Arabidopsis pex6 mutants without restoring PEX5 recycling

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dc.citation.firstpageE3163en_US
dc.citation.issueNumber14en_US
dc.citation.journalTitlePNASen_US
dc.citation.lastpageE3172en_US
dc.citation.volumeNumber115en_US
dc.contributor.authorGonzalez, Kim L.en_US
dc.contributor.authorRatzel, Sarah E.en_US
dc.contributor.authorBurks, Kendall H.en_US
dc.contributor.authorDanan, Charles H.en_US
dc.contributor.authorWages, Jeanne M.en_US
dc.contributor.authorZolman, Bethany K.en_US
dc.contributor.authorBartel, Bonnieen_US
dc.date.accessioned2018-12-17T18:57:37Zen_US
dc.date.available2018-12-17T18:57:37Zen_US
dc.date.issued2018en_US
dc.description.abstractPeroxisomes are eukaryotic organelles critical for plant and human development because they house essential metabolic functions, such as fatty acid β-oxidation. The interacting ATPases PEX1 and PEX6 contribute to peroxisome function by recycling PEX5, a cytosolic receptor needed to import proteins targeted to the peroxisomal matrix. Arabidopsis pex6 mutants exhibit low PEX5 levels and defects in peroxisomal matrix protein import, oil body utilization, peroxisomal metabolism, and seedling growth. These defects are hypothesized to stem from impaired PEX5 retrotranslocation leading to PEX5 polyubiquitination and consequent degradation of PEX5 via the proteasome or of the entire organelle via autophagy. We recovered a pex1 missense mutation in a screen for second-site suppressors that restore growth to the pex6-1 mutant. Surprisingly, this pex1-1 mutation ameliorated the metabolic and physiological defects of pex6-1 without restoring PEX5 levels. Similarly, preventing autophagy by introducing an atg7-null allele partially rescued pex6-1 physiological defects without restoring PEX5 levels. atg7 synergistically improved matrix protein import in pex1-1 pex6-1, implying that pex1-1 improves peroxisome function in pex6-1 without impeding autophagy of peroxisomes (i.e., pexophagy). pex1-1 differentially improved peroxisome function in various pex6 alleles but worsened the physiological and molecular defects of a pex26 mutant, which is defective in the tether anchoring the PEX1–PEX6 hexamer to the peroxisome. Our results support the hypothesis that, beyond PEX5 recycling, PEX1 and PEX6 have additional functions in peroxisome homeostasis and perhaps in oil body utilization.en_US
dc.identifier.citationGonzalez, Kim L., Ratzel, Sarah E., Burks, Kendall H., et al.. "A pex1 missense mutation improves peroxisome function in a subset of Arabidopsis pex6 mutants without restoring PEX5 recycling." <i>PNAS,</i> 115, no. 14 (2018) National Academy of Sciences: E3163-E3172. https://doi.org/10.1073/pnas.1721279115.en_US
dc.identifier.doihttps://doi.org/10.1073/pnas.1721279115en_US
dc.identifier.urihttps://hdl.handle.net/1911/103871en_US
dc.language.isoengen_US
dc.publisherNational Academy of Sciencesen_US
dc.subject.keywordperoxisomeen_US
dc.subject.keywordperoxinen_US
dc.subject.keywordpexophagyen_US
dc.subject.keywordAAA ATPaseen_US
dc.subject.keywordoil bodiesen_US
dc.titleA pex1 missense mutation improves peroxisome function in a subset of Arabidopsis pex6 mutants without restoring PEX5 recyclingen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
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