Genetic Dissection of Peroxisome-Associated Matrix Protein Degradation in Arabidopsis thaliana

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dc.citation.firstpage125
dc.citation.issueNumber141
dc.citation.journalTitleGenetics
dc.citation.lastpage141
dc.citation.volumeNumber193
dc.contributor.authorBurkhart, Sarah E.
dc.contributor.authorLingard, Matthew J.
dc.contributor.authorBartel, Bonnie
dc.date.accessioned2018-07-10T18:32:39Z
dc.date.available2018-07-10T18:32:39Z
dc.date.issued2013
dc.description.abstractPeroxisomes are organelles that sequester certain metabolic pathways; many of these pathways generate H2O2, which can damage proteins. However, little is known about how damaged or obsolete peroxisomal proteins are degraded. We exploit developmentally timed peroxisomal content remodeling in Arabidopsis thaliana to elucidate peroxisome-associated protein degradation. Isocitrate lyase (ICL) is a peroxisomal glyoxylate cycle enzyme necessary for early seedling development. A few days after germination, photosynthesis begins and ICL is degraded. We previously found that ICL is stabilized when a peroxisome-associated ubiquitin-conjugating enzyme and its membrane anchor are both mutated, suggesting that matrix proteins might exit the peroxisome for ubiquitin-dependent cytosolic degradation. To identify additional components needed for peroxisome-associated matrix protein degradation, we mutagenized a line expressing GFP–ICL, which is degraded similarly to endogenous ICL, and identified persistent GFP-ICLfluorescence (pfl) mutants. We found three pfl mutants that were defective in PEROXIN14(PEX14/At5g62810), which encodes a peroxisomal membrane protein that assists in importing proteins into the peroxisome matrix, indicating that proteins must enter the peroxisome for efficient degradation. One pflmutant was missing the peroxisomal 3-ketoacyl-CoA thiolase encoded by the PEROXISOME DEFECTIVE1 (PED1/At2g33150) gene, suggesting that peroxisomal metabolism influences the rate of matrix protein degradation. Finally, one pfl mutant that displayed normal matrix protein import carried a novel lesion in PEROXIN6 (PEX6/At1g03000), which encodes a peroxisome-tethered ATPase that is involved in recycling matrix protein receptors back to the cytosol. The isolation of pex6-2 as a pfl mutant supports the hypothesis that matrix proteins can exit the peroxisome for cytosolic degradation.
dc.identifier.citationBurkhart, Sarah E., Lingard, Matthew J. and Bartel, Bonnie. "Genetic Dissection of Peroxisome-Associated Matrix Protein Degradation in Arabidopsis thaliana." <i>Genetics,</i> 193, no. 141 (2013) The Genetics Society of America: 125-141. https://doi.org/10.1534/genetics.112.146100.
dc.identifier.digital125
dc.identifier.doihttps://doi.org/10.1534/genetics.112.146100
dc.identifier.urihttps://hdl.handle.net/1911/102358
dc.language.isoeng
dc.publisherThe Genetics Society of America
dc.rightsArticle is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
dc.subject.keywordorganelle quality control
dc.subject.keywordperoxin
dc.subject.keywordperoxisome
dc.subject.keywordPEX6 AAA ATPase
dc.subject.keywordprotein degradation
dc.titleGenetic Dissection of Peroxisome-Associated Matrix Protein Degradation in Arabidopsis thaliana
dc.typeJournal article
dc.type.dcmiText
dc.type.publicationpublisher version
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