The targeting and assembly of peroxisomal proteins: some old rules do not apply

doi:10.1016/S0968-0004(96)80181-2

Trends in Biochemical Sciences

Volume 21, Issue 2, February 1996, Pages 54-58

https://doi.org/10.1016/S0968-0004(96)80181-2 Get rights and content

Several proteins have been identified that catalyze the import of proteins into peroxisomes. Some recognize specific peroxisomal targeting sequences, but most probably work further downstream the import pathway. Recent evidence suggests that peroxisomal targeting and assembly do not follow the same rules as those for targeting and import into other organelles, such as the mitochondria and the endoplasmic reticulum, i.e. the import of unfolded proteins and subsequent folding within the organelle. Specifically, proteins may be translocated into the peroxisomal matrix in a folded or oligomerized state.

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Wound- and pathogen-activated de novo JA synthesis using different ACX isozymes in tea plant (Camellia sinensis)
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Citation Excerpt :
The deduced amino acid sequence of CsACX1 has a carboxy-terminal tripeptide sequence (ARL), which is a peroxisomal targeting signal of the PTS1 type (McNew and Goodman, 1996) found in plant peroxisomal enzymes, such as isocitrate lyase and malate synthase (Comai et al., 1989; Graham et al., 1989; Mori et al., 1991). By contrast, CsACX3 shared a feature with OsACX3 and AtACX3: they all contain an amino-terminal peroxisomal targeting signal of the PTS2 type (Fig. 1a; McNew and Goodman, 1996), which was found in some plant peroxisomal proteins, such as malate dehydrogenase, citrate synthase, and thiolase (Kato et al., 1998) (Fig. 1a). Therefore, plant ACXs have either PTS1 or PTS2 with varying mechanisms of import (Schaller and Stintzi, 2009).
Acyl-CoA oxidase (ACX; EC 1.3.3.6) plays a vital role in the biosynthesis of jasmonic acid (JA) in plant peroxisomes. We previously identified an herbivore-induced gene CsACX1 in tea plant (Camellia sinensis) and showed CsACX1 was involved in the wound-induced synthesis of jasmonic acid (JA). Here, another ACX gene CsACX3 was isolated from tea plant. CsACX3 was predicted to consist of 684 amino acid residues. CsACX3 can be induced by mechanical wounding, JA application, and infestation by the tea geometrid Ectropis obliqua Prout and the tea green leafhopper Empoasca (Matsumurasca) onukii Matsuda. These expression patterns are consistent with the previously reported expression pattern of CsACX1 under such treatments. Recombinant CsACX3 showed preference for medium-chain acyl-coA oxidase substrates (C₈- to C₁₄-CoA). CsACX3 expression could also be induced by the infection of a pathogen Colletotrichum gloeosporioides (Cgl), and the increased ACX activities in tea plants were correlated with the Cgl-induced CsACX3 expression. Cgl could not induce the expression of CsACX1, which showed preference for C₁₂- to C₁₆-CoA substrates. The constitutive expression of CsACX3 rescued wound-induced JA biosynthesis and enhanced the Cgl-induced JA biosynthesis in Arabidopsis mutant atacx1. However, constitutive expression of CsACX1 could not enhance the Cgl-induced JA biosynthesis in atacx1 plant. These results indicate that CsACX1 and CsACX3 functions overlap and have distinct roles in the wound- and pathogen-activated de novo JA synthesis via enzymatic routes that utilize different ACX isozymes in tea plant.
The involvement of a herbivore-induced acyl-CoA oxidase gene, CsACX1, in the synthesis of jasmonic acid and its expression in flower opening in tea plant (Camellia sinensis)
2019, Plant Physiology and Biochemistry
Citation Excerpt :
A similar one is seen in the deduced amino acid sequences of LeACX1A (AKL), GmACX1-1 (ARL), and AtACX1 (ARL). In contrast, AtACX2, AtACX3, and AtACX4 contain an amino-terminal targeting signal of the PTS2 type (McNew and Goodman, 1996) (Fig. 2). QRT-PCR analysis revealed that mechanical wounding, herbivore infestation, and JA treatment result in an obvious increase in the transcript levels of CsACX1 (Fig. 3).
The biosynthesis of jasmonic acid (JA) in plant peroxisomes requires the action of acyl-CoA oxidase (ACX; EC 1.3.3.6). Multiple isoforms of ACXs have been identified in various annual herbaceous plants, but the genes encoding these enzymes in perennial woody plants are yet to be fully investigated. In this study, an ACX gene named CsACX1 (GeneBank accession: KX650077.1) was isolated from tea plant (Camellia sinensis L.). CsACX1 was predicted to consist of 664 amino acid residues. Transcriptional analysis revealed that CsACX1 can be induced by mechanical wounding, JA application, and infestation by the tea geometrid Ectropis obliqua Prout and the tea green leafhopper Empoasca (Matsumurasca) onukii Matsuda. To further elucidate the function of CsACX1, it was heterologously expressed in a bacterial system and characterized. Recombinant CsACX1 showed preference for C₁₂ ∼ C₁₆-CoA substrates. The constitutive expression of CsACX1 can rescue wound-related JA biosynthesis in Arabidopsis mutant acx1. CsACX1 was expressed in different organs, predominantly in flowers. Notably, CsACX1 transcripts were detected up-regulated during flower opening, and the JA levels were correlated with CsACX1 expression. All these results enrich our knowledge of the regulatory pathway involved in the JA biosynthesis in tea, and helps further understand the defense mechanism of tea plant against insects.
Ubiquitination of the glycosomal matrix protein receptor PEX5 in Trypanosoma brucei by PEX4 displays novel features
2013, Biochimica et Biophysica Acta - Molecular Cell Research
Trypanosomatids contain peroxisome-like organelles called glycosomes. Peroxisomal biogenesis involves a cytosolic receptor, PEX5, which, after its insertion into the organellar membrane, delivers proteins to the matrix. In yeasts and mammalian cells, transient PEX5 monoubiquitination at the membrane serves as the signal for its retrieval from the organelle for re-use. When its recycling is impaired, PEX5 is polyubiquitinated for proteasomal degradation. Stably monoubiquitinated TbPEX5 was detected in cytosolic fractions of Trypanosoma brucei, indicative for its role as physiological intermediate in receptor recycling. This modification's resistance to dithiothreitol suggests ubiquitin conjugation of a lysine residue. T. brucei PEX4, the functional homologue of the ubiquitin-conjugating (UBC) enzyme responsible for PEX5 monoubiquitination in yeast, was identified. It is associated with the cytosolic face of the glycosomal membrane, probably anchored by an identified putative TbPEX22. The involvement of TbPEX4 in TbPEX5 ubiquitination was demonstrated using procyclic ∆PEX4 trypanosomes. Surprisingly, glycosomal matrix protein import was only mildly affected in this mutant. Since other UBC homologues were upregulated, it might be possible that these have partially rescued PEX4's function in PEX5 ubiquitination. In addition, the altered expression of UBCs, notably of candidates involved in cell-cycle control, could be responsible for observed morphological and motility defects of the ∆PEX4 mutant.
Peroxisomal protein translocation
2010, Biochimica et Biophysica Acta - Molecular Cell Research
Peroxisomes perform a wide variety of metabolic processes in eukaryotic organisms. Mutations that affect peroxisome function or formation have profound phenotypic consequences, the latter demonstrated by peroxisome biogenesis disorders which are often fatal. The biogenesis of peroxisomes conceptually consists of: (1) the formation of the peroxisomal membrane, (2) the import of peroxisomal matrix enzymes and (3) the proliferation of the organelles. Proteins involved in these processes are collectively called peroxins, encoded by PEX-genes. To date 32 peroxins are known, which perform functions in peroxisome biogenesis that are conserved from yeast to man. In this article, we focus on the current status of knowledge about the topogenesis of the peroxisomal membrane proteins, and the import of proteins into the peroxisomal matrix.
Engineering of the pyruvate dehydrogenase bypass in Saccharomyces cerevisiae for high-level production of isoprenoids
2007, Metabolic Engineering
Amorphadiene, a sesquiterpene precursor to the anti-malarial drug artemisinin, is synthesized by the cyclization of farnesyl pyrophosphate (FPP). Saccharomyces cerevisiae produces FPP through the mevalonate pathway using acetyl-CoA as a starting compound. In order to enhance the supply of acetyl-CoA to the mevalonate pathway and achieve high-level production of amorphadiene, we engineered the pyruvate dehydrogenase bypass in S. cerevisiae. Overproduction of acetaldehyde dehydrogenase and introduction of a Salmonella enterica acetyl-CoA synthetase variant increased the carbon flux into the mevalonate pathway resulting in increased amorphadiene production. This work will be generally applicable to the production of a broad range of isoprenoids in yeast.
Molecular organization of peroxisomal enzymes: Protein-protein interactions in the membrane and in the matrix
2006, Archives of Biochemistry and Biophysics
The β-oxidation of fatty acids in peroxisomes produces hydrogen peroxide (H₂O₂₎, a toxic metabolite, as a bi-product. Fatty acids β-oxidation activity is deficient in X-linked adrenoleukodystrophy (X-ALD) because of mutation in ALD-gene resulting in loss of very long chain acyl-CoA synthetase (VLCS) activity. It is also affected in disease with catalase negative peroxisomes as a result of inactivation by H₂O₂. Therefore, the following studies were undertaken to delineate the molecular interactions between both the ALD-gene product (adrenoleukodystrophy protein, ALDP) and VLCS as well as H₂O₂ degrading enzyme catalase and proteins of peroxisomal β-oxidation. Studies using a yeast two hybrid system and surface plasmon resonance techniques indicate that ALDP, a peroxisomal membrane protein, physically interacts with VLCS. Loss of these interactions in X-ALD cells may result in a deficiency in VLCS activity. The yeast two-hybrid system studies also indicated that catalase physically interacts with l-bifunctional enzyme (l-BFE). Interactions between catalase and l-BFE were further supported by affinity purification, using a catalase-linked resin. The affinity bound 74-kDa protein, was identified as l-BFE by Western blot with specific antibodies and by proteomic analysis. Additional support for their interaction comes from immunoprecipitation of l-BFE with antibodies against catalase as a catalase- l-BFE complex. siRNA for l-BFE decreased the specific activity and protein levels of catalase without changing its subcellular distribution. These observations indicate that l-BFE might help in oligomerization and possibly in the localization of catalase at the site of H₂O₂ production in the peroxisomal β-oxidation pathway.

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¹: is at the Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY 10021, USA

²: is at the Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75235-9041, USA

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Trends in Biochemical Sciences

The targeting and assembly of peroxisomal proteins: some old rules do not apply

Curr. Opin. Cell Biol.

FEBS Lett.

FEBS Lett.

J. Biol. Chem.

J. Biol. Chem.

J. Biol. Chem.

J. Biol. Chem.

J. Biol. Chem.

Biochem. Biophys. Res. Comm.

J. Cell Biol.

J. Biol. Chem.

Biochem. Biophys. Res. Commun.

Cell

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Annu. Rev. Biochem.

Annu. Rev. Biochem.

J. Cell Biol.

J. Cell Biol.

Mol. Gen. Genet.

J. Cell Biol.

J. Cell Biol.