Peroxisomal Biogenesis and Acquistion of Membrane Proteins

Trelease, Richard N.

doi:10.1007/978-94-015-9858-3_10

Cited by 9 publications

(9 citation statements)

References 126 publications

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“…To define precisely the regions within the N-terminal half (residues 1 to 156) of p33 responsible for its targeting to peroxisomes and pER, we examined amino acid sequences within the protein that resemble a prototypic membrane peroxisomal targeting signal (mPTS) present in most other PMPs (i.e., a stretch of several positively charged residues adjacent to at least one TMD) (reviewed in Trelease, 2002). We also focused on sequences of the p33 homologs from CymRSV and CNV that include the protein's two TMDs and adjacent hydrophilic domains and that were necessary for targeting to peroxisomes in yeast cells (Navarro et al, 2004;Panavas et al, 2005).…”

Section: The N-terminal Half Of P33 Possesses Both Peroxisome and Permentioning

confidence: 99%

Localization of the Tomato Bushy Stunt Virus Replication Protein p33 Reveals a Peroxisome-to-Endoplasmic Reticulum Sorting Pathway[W]

et al. 2005

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Tomato bushy stunt virus (TBSV), a positive-strand RNA virus, causes extensive inward vesiculations of the peroxisomal boundary membrane and formation of peroxisomal multivesicular bodies (pMVBs). Although pMVBs are known to contain protein components of the viral membrane-bound RNA replication complex, the mechanisms of protein targeting to peroxisomal membranes and participation in pMVB biogenesis are not well understood. We show that the TBSV 33-kD replication protein (p33), expressed on its own, targets initially from the cytosol to peroxisomes, causing their progressive aggregation and eventually the formation of peroxisomal ghosts. These altered peroxisomes are distinct from pMVBs; they lack internal vesicles and are surrounded by novel cytosolic vesicles that contain p33 and appear to be derived from evaginations of the peroxisomal boundary membrane. Concomitant with these changes in peroxisomes, p33 and resident peroxisomal membrane proteins are relocalized to the peroxisomal endoplasmic reticulum (pER) subdomain. This sorting of p33 is disrupted by the coexpression of a dominant-negative mutant of ADP-ribosylation factor1, implicating coatomer in vesicle formation at peroxisomes. Mutational analysis of p33 revealed that its intracellular sorting is also mediated by several targeting signals, including three peroxisomal targeting elements that function cooperatively, plus a pER targeting signal resembling an Arg-based motif responsible for vesicle-mediated retrieval of escaped ER membrane proteins from the Golgi. These results provide insight into virus-induced intracellular rearrangements and reveal a peroxisome-to-pER sorting pathway, raising new mechanistic questions regarding the biogenesis of peroxisomes in plants.

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Section: The N-terminal Half Of P33 Possesses Both Peroxisome and Permentioning

confidence: 99%

Localization of the Tomato Bushy Stunt Virus Replication Protein p33 Reveals a Peroxisome-to-Endoplasmic Reticulum Sorting Pathway[W]

et al. 2005

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“…PMPs are divided into two groups based on their posttranslational sorting pathway (Titorenko and Rachubinski, 2001;Trelease, 2002). Group I PMPs sort indirectly through the ER from their site of synthesis in the cytosol to forming or pre-existing peroxisomes, whereas group II PMPs sort directly to peroxisomes.…”

Section: Intracellular Trafficking Of Atpex11 Isoformsmentioning

confidence: 99%

Five Arabidopsis peroxin 11 homologs individually promote peroxisome elongation, duplication or aggregation

Lingard

Trelease

2006

Journal of Cell Science

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116

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Pex11 homologs and dynamin-related proteins uniquely regulate peroxisome division (cell-cycle-dependent duplication) and proliferation (cell-cycle-independent multiplication). Arabidopsis plants possess five Pex11 homologs designated in this study as AtPex11a, -b, -c, -d and -e. Transcripts for four isoforms were found in Arabidopsis plant parts and in cells in suspension culture; by contrast, AtPex11a transcripts were found only in developing siliques. Within 2.5 hours after biolistic bombardments, myc-tagged or GFP-tagged AtPex11 a, -b, -c, -d and -e individually sorted from the cytosol directly to peroxisomes; none trafficked indirectly through the endoplasmic reticulum. Both termini of myc-tagged AtPex11 b, -c, -d and -e faced the cytosol, whereas the N- and C-termini of myc-AtPex11a faced the cytosol and matrix, respectively. In AtPex11a- or AtPex11e-transformed cells, peroxisomes doubled in number. Those peroxisomes bearing myc-AtPex11a, but not myc-AtPex11e, elongated prior to duplication. In cells transformed with AtPex11c or AtPex11d, peroxisomes elongated without subsequent fission. In AtPex11b-transformed cells, peroxisomes were aggregated and rounded. A C-terminal dilysine motif, present in AtPex11c, -d and -e, was not necessary for AtPex11d-induced peroxisome elongation. However, deletion of the motif from myc-AtPex11e led to peroxisome elongation and fission, indicating that the motif in this isoform promotes fission without elongation. In summary, all five overexpressed AtPex11 isoforms sort directly to peroxisomal membranes where they individually promote duplication (AtPex11a, -e), aggregation (AtPex11b), or elongation without fission (AtPex11c, -d).

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“…Sometimes, this sequence is referred to as a membrane PTS (mPTS). However, it is not as conserved as conventional PTS1 and PTS2 sequences, and the definition of a consensus sequence for membrane targeting of peroxisomal proteins is difficult (Trelease, 2002). In general, two import pathways for proteins destined for the peroxisomal membrane are discussed.…”

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confidence: 99%

Novel Proteins, Putative Membrane Transporters, and an Integrated Metabolic Network Are Revealed by Quantitative Proteomic Analysis of Arabidopsis Cell Culture Peroxisomes

et al. 2008

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Peroxisomes play key roles in energy metabolism, cell signaling, and plant development. A better understanding of these important functions will be achieved with a more complete definition of the peroxisome proteome. The isolation of peroxisomes and their separation from mitochondria and other major membrane systems have been significant challenges in the Arabidopsis (Arabidopsis thaliana) model system. In this study, we present new data on the Arabidopsis peroxisome proteome obtained using two new technical advances that have not previously been applied to studies of plant peroxisomes. First, we followed density gradient centrifugation with free-flow electrophoresis to improve the separation of peroxisomes from mitochondria. Second, we used quantitative proteomics to identify proteins enriched in the peroxisome fractions relative to mitochondrial fractions. We provide evidence for peroxisomal localization of 89 proteins, 36 of which have not previously been identified in other analyses of Arabidopsis peroxisomes. Chimeric green fluorescent protein constructs of 35 proteins have been used to confirm their localization in peroxisomes or to identify endoplasmic reticulum contaminants. The distribution of many of these peroxisomal proteins between soluble, membrane-associated, and integral membrane locations has also been determined. This core peroxisomal proteome from nonphotosynthetic cultured cells contains a proportion of proteins that cannot be predicted to be peroxisomal due to the lack of recognizable peroxisomal targeting sequence 1 (PTS1) or PTS2 signals. Proteins identified are likely to be components in peroxisome biogenesis, b-oxidation for fatty acid degradation and hormone biosynthesis, photorespiration, and metabolite transport. A considerable number of the proteins found in peroxisomes have no known function, and potential roles of these proteins in peroxisomal metabolism are discussed. This is aided by a metabolic network analysis that reveals a tight integration of functions and highlights specific metabolite nodes that most probably represent entry and exit metabolites that could require transport across the peroxisomal membrane.Within the plant cell, energy metabolism is mainly distributed among three distinct organelles: plastids, mitochondria, and peroxisomes. Although the proteomes of both plastids and mitochondria have been investigated extensively, comparatively little systematic analysis of the protein content of plant peroxisomes has been undertaken. The main obstacle for proteomics of plant peroxisomes is the availability of purified organelles from model plants that are also amenable to mass spectrometry (MS)-based identification by matching to protein sequence data. Whereas the preparation of peroxisomes in sufficient amounts and purity from spinach (Spinacia oleracea), cucumber (Cucumis sativus), pea (Pisum sativum), and soybean (Glycine max) for proteomic purposes is possible (Schwitzguebel and Siegenthaler, 1984;Corpas et al., 1994;Lopez-Huertas et al., 1999;Arai et al., 2008), the ...

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Peroxisomal Biogenesis and Acquistion of Membrane Proteins

Cited by 9 publications

References 126 publications

Localization of the Tomato Bushy Stunt Virus Replication Protein p33 Reveals a Peroxisome-to-Endoplasmic Reticulum Sorting Pathway[W]

Localization of the Tomato Bushy Stunt Virus Replication Protein p33 Reveals a Peroxisome-to-Endoplasmic Reticulum Sorting Pathway[W]

Five Arabidopsis peroxin 11 homologs individually promote peroxisome elongation, duplication or aggregation

Novel Proteins, Putative Membrane Transporters, and an Integrated Metabolic Network Are Revealed by Quantitative Proteomic Analysis of Arabidopsis Cell Culture Peroxisomes

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