Developmental Analysis of a Putative ATP/ADP Carrier Protein Localized on Glyoxysomal Membranes During the Peroxisome Transition in Pumpkin Cotyledons

Fukao, Youichiro; Hayashi, Yasuko; Mano, Shoji; Hayashi, Makoto; Nishimura, Mikio

doi:10.1093/pcp/pce108

Cited by 45 publications

(32 citation statements)

References 24 publications

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“…The peroxisomal localization of Arabidopsis PMP38 in pumpkin (Cucurbita sp) has already been demonstrated by cell fractionation and immunocytochemical analysis in an earlier study (Fukao et al, 2001). Because the abundance of the PMP38 protein was coregulated with that of the fatty acid b-oxidation enzymes during postgerminative growth, this transporter was proposed to be involved in fatty acid degradation as a putative peroxisomal ATP carrier (Fukao et al, 2001). However, PMP38 most likely has a different substrate specificity, and our results strongly indicate that PMP38 does not function in transport of ATP across the peroxisomal membrane.…”

Section: Discussionmentioning

confidence: 91%

“…One of the candidate genes, At2g39970, is annotated as peroxisomal membrane protein 38 kD (PMP38) and was previously proposed to represent a peroxisomal ATP carrier (Fukao et al, 2001). However, biochemical data investigating its transport function or mutants deficient in this protein have not yet been reported.…”

Section: Identification Of Genes Encoding Putative Peroxisomal Atp Camentioning

confidence: 99%

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Peroxisomal ATP Import Is Essential for Seedling Development inArabidopsis thaliana

et al. 2008

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Several recent proteomic studies of plant peroxisomes indicate that the peroxisomal matrix harbors multiple ATPdependent enzymes and chaperones. However, it is unknown whether plant peroxisomes are able to produce ATP by substrate-level phosphorylation or whether external ATP fuels the energy-dependent reactions within peroxisomes. The existence of transport proteins that supply plant peroxisomes with energy for fatty acid oxidation and other ATP-dependent processes has not previously been demonstrated. Here, we describe two Arabidopsis thaliana genes that encode peroxisomal adenine nucleotide carriers, PNC1 and PNC2. Both proteins, when fused to enhanced yellow fluorescent protein, are targeted to peroxisomes. Complementation of a yeast mutant deficient in peroxisomal ATP import and in vitro transport assays using recombinant transporter proteins revealed that PNC1 and PNC2 catalyze the counterexchange of ATP with ADP or AMP. Transgenic Arabidopsis lines repressing both PNC genes were generated using ethanol-inducible RNA interference. A detailed analysis of these plants showed that an impaired peroxisomal ATP import inhibits fatty acid breakdown during early seedling growth and other b-oxidation reactions, such as auxin biosynthesis. We show conclusively that PNC1 and PNC2 are essential for supplying peroxisomes with ATP, indicating that no other ATP generating systems exist inside plant peroxisomes.

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Section: Discussionmentioning

confidence: 91%

Section: Identification Of Genes Encoding Putative Peroxisomal Atp Camentioning

confidence: 99%

Peroxisomal ATP Import Is Essential for Seedling Development inArabidopsis thaliana

et al. 2008

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“…To rule out the possibility of nonspecific interactions occurring due to random collisions on the peroxisomal membrane, combinations with other membrane proteins, PMP38 and PEX12, were tested. No interactions were detected using these negative controls (Figures 5I and 5J;Fukao et al, 2001;Mano et al, 2006).…”

Section: Protein-protein Interactions Among Apem9 Pex6 and Pex1mentioning

confidence: 96%

ArabidopsisABERRANT PEROXISOME MORPHOLOGY9 Is a Peroxin That Recruits the PEX1-PEX6 Complex to Peroxisomes

et al. 2011

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Peroxisomes have pivotal roles in several metabolic processes, such as the detoxification of H 2 O 2 and b-oxidation of fatty acids, and their functions are tightly regulated by multiple factors involved in peroxisome biogenesis, including protein transport. This study describes the isolation of an embryonic lethal Arabidopsis thaliana mutant, aberrant peroxisome morphology9 (apem9), which is compromised in protein transport into peroxisomes. The APEM9 gene was found to encode an unknown protein. Compared with apem9 having the nucleotide substitution, the knockdown mutants showed severe defects in peroxisomal functions and plant growth. We showed that expression of APEM9 altered PEROXIN6 (PEX6) subcellular localization from the cytosol to peroxisomes. In addition, we showed that PEX1 and PEX6 comprise a heterooligomer and that this complex was recruited to peroxisomal membranes via protein-protein interactions of APEM9 with PEX6. These findings show that APEM9 functions as an anchoring protein, similar to Pex26 in mammals and Pex15p in yeast. Interestingly, however, the identities of amino acids among these anchoring proteins are quite low. These results indicate that although the association of the PEX1-PEX6 complex with peroxisomal membranes is essential for peroxisomal functions, the protein that anchors this complex evolved uniquely in plants.

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“…The peroxisomal NAD + transporter PXN is an abundant protein of the peroxisomal membrane identified as PMP38 by independent proteomic approaches (Fukao et al, 2001;Reumann et al, 2007Reumann et al, , 2009Eubel et al, 2008) and from a screen for mutants with abnormal peroxisome morphology . This protein exhibits high sequence similarity to the PNCs; however, recombinant Arabidopsis PXN transports NAD + in vitro in exchange for NADH, AMP, or ADP (Bernhardt et al, 2012).…”

Section: Pxn Serves As a Peroxisomal Nad + Transportermentioning

confidence: 99%

Plant Peroxisomes: Biogenesis and Function

et al. 2012

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Peroxisomes are eukaryotic organelles that are highly dynamic both in morphology and metabolism. Plant peroxisomes are involved in numerous processes, including primary and secondary metabolism, development, and responses to abiotic and biotic stresses. Considerable progress has been made in the identification of factors involved in peroxisomal biogenesis, revealing mechanisms that are both shared with and diverged from non-plant systems. Furthermore, recent advances have begun to reveal an unexpectedly large plant peroxisomal proteome and have increased our understanding of metabolic pathways in peroxisomes. Coordination of the biosynthesis, import, biochemical activity, and degradation of peroxisomal proteins allows for highly dynamic responses of peroxisomal metabolism to meet the needs of a plant. Knowledge gained from plant peroxisomal research will be instrumental to fully understanding the organelle's dynamic behavior and defining peroxisomal metabolic networks, thus allowing the development of molecular strategies for rational engineering of plant metabolism, biomass production, stress tolerance, and pathogen defense.

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Developmental Analysis of a Putative ATP/ADP Carrier Protein Localized on Glyoxysomal Membranes During the Peroxisome Transition in Pumpkin Cotyledons

Cited by 45 publications

References 24 publications

Peroxisomal ATP Import Is Essential for Seedling Development inArabidopsis thaliana

Peroxisomal ATP Import Is Essential for Seedling Development inArabidopsis thaliana

ArabidopsisABERRANT PEROXISOME MORPHOLOGY9 Is a Peroxin That Recruits the PEX1-PEX6 Complex to Peroxisomes

Plant Peroxisomes: Biogenesis and Function

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