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dc.contributor.authorGonzalez, Kim L.
Ratzel, Sarah E.
Burks, Kendall H.
Danan, Charles H.
Wages, Jeanne M.
Zolman, Bethany K.
Bartel, Bonnie
dc.date.accessioned 2018-12-17T18:57:37Z
dc.date.available 2018-12-17T18:57:37Z
dc.date.issued 2018
dc.identifier.citation Gonzalez, 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." PNAS, 115, no. 14 (2018) National Academy of Sciences: E3163-E3172. https://doi.org/10.1073/pnas.1721279115.
dc.identifier.urihttps://hdl.handle.net/1911/103871
dc.description.abstract Peroxisomes 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.
dc.language.iso eng
dc.publisher National Academy of Sciences
dc.title A pex1 missense mutation improves peroxisome function in a subset of Arabidopsis pex6 mutants without restoring PEX5 recycling
dc.type Journal article
dc.citation.journalTitle PNAS
dc.subject.keywordperoxisome
peroxin
pexophagy
AAA ATPase
oil bodies
dc.citation.volumeNumber 115
dc.citation.issueNumber 14
dc.type.dcmi Text
dc.identifier.doihttps://doi.org/10.1073/pnas.1721279115
dc.type.publication publisher version
dc.citation.firstpage E3163
dc.citation.lastpage E3172


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