Peroxisomes: simple in function but complex in maintenance

Tabak, Henk F.; Braakman, Ineke; Distel, Ben

doi:10.1016/s0962-8924(99)01650-5

Cited by 68 publications

(53 citation statements)

References 43 publications

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“…With the exceptions of pRTL2/CAT-pAPXϩ29, pRTL2/CATpAPXϩ36-TMD⌬TMD rev , and pRTL2/CAT-pAPXϩ36-TMD⌬PMP47T-MD 4 , all CAT-pAPX constructs were generated by annealing either one or two sets of appropriate complementary synthetic oligonucleotides coding for a serine-serine/arginine linker (a single serine linker only for CAT-pAPXϩRKRMK and CAT-pAPXϩ11) and selected amino acid residues within the C terminus of cottonseed peroxisomal APX (see Table I). Double-stranded oligonucleotides were ligated via XbaI complementary ends into XbaI-digested pRTL2/CAT-XbaI.…”

Section: Methodsmentioning

confidence: 99%

“…Next, two sets of appropriate synthetic doublestranded oligonucleotides possessing HpaI and BspEI complementary ends coding for amino acid residues in an order reverse to those in the TMD of wild-type peroxisomal APX were ligated into HpaI-BspEIdigested pCR2.1/pAPXϩ36-HpaI-BspEI, digested with XbaI, and then ligated into XbaI-digested pRTL2/CAT-XbaI to yield pRTL2/CATpAPXϩ36-TMD⌬TMD rev . To construct pRTL2/CAT-pAPXϩ36-T-MD⌬PMP47TMD 4 , two sets of appropriate synthetic double-stranded oligonucleotides possessing HpaI and BspEI complementary ends were ligated into HpaI-BspEI-digested pCR2.1/pAPXϩ36-HpaI-BspEI. pCR2.1/pAPXϩ36-TMD⌬PMP47TMD 4 -HpaI-BspEI was then digested with XbaI and ligated into XbaI-digested pRTL2/CAT-XbaI to yield pRTL2/CAT-pAPXϩ36-TMD⌬PMP47TMD 4 .…”

Section: Methodsmentioning

confidence: 99%

“…1 Most of our understanding of the molecular mechanisms responsible for sorting and import of PTS1-and PTS2-bearing proteins has come from studies of yeast and cultured mammalian cells with defects in peroxisomal biogenesis (pex mutants) (1). Characterization of these mutants has led to the isolation of a number of genes (PEX) and gene products (peroxins) (2)(3)(4). More recently, information related to the targeting signals and sorting/insertion/assembly of peroxisomal membrane proteins (PMPs) has become available.…”

mentioning

confidence: 99%

“…24). Nevertheless, important implications of this indirect PMP sorting pathway are that the ER serves as the initial targeting site of the nascent PMP and as the source of new or differentiating peroxisomes (2,4,24,25).…”

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confidence: 99%

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The Sorting Signals for Peroxisomal Membrane-bound Ascorbate Peroxidase Are within Its C-terminal Tail

Mullen

Trelease

2000

Journal of Biological Chemistry

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Peroxisomal ascorbate peroxidase (APX) is a carboxyl tail-anchored, type II (N cytosol -C matrix ) integral membrane protein that functions in the regeneration of NAD ؉ in glyoxysomes of germinated oilseeds and protection of peroxisomes in other organisms from toxic H 2 O 2 . Recently we showed that cottonseed peroxisomal APX was sorted post-translationally from the cytosol to peroxisomes via a novel reticular/circular membranous network that was interpreted to be a subdomain of the endoplasmic reticulum (ER), named peroxisomal ER (pER). Here we report on the molecular signals responsible for sorting peroxisomal APX. Deletions or site-specific substitutions of certain amino acid residues within the hydrophilic C-terminal-most eight-amino acid residues (includes a positively charged domain found in most peroxisomal integral membrane-destined proteins) abolished sorting of peroxisomal APX to peroxisomes via pER. However, the C-terminal tail was not sufficient for sorting chloramphenicol acetyltransferase to peroxisomes via pER, whereas the peptide plus most of the immediately adjacent 21-amino acid transmembrane domain (TMD) of peroxisomal APX was sufficient for sorting. Replacement of the peroxisomal APX TMD with an artificial TMD (devoid of putative sorting sequences) plus the peroxisomal APX C-terminal tail also sorted chloramphenicol acetyltransferase to peroxisomes via pER, indicating that the peroxisomal APX TMD does not possess essential sorting information. Instead, the TMD appears to confer the proper context required for the conserved positively charged domain to function within peroxisomal APX as an overlapping pER sorting signal and a membrane peroxisome targeting signal type 2.Peroxisomes are single membrane-bound organelles that do not contain DNA nor protein-synthesizing machinery. Data published thus far indicate that they acquire their nuclearencoded matrix and boundary membrane protein constituents from the cytosol in a regulated, post-translational manner. For instance, proteins destined for the peroxisomal matrix are sorted by at least two evolutionarily conserved targeting signals, the type 1 and type 2 peroxisomal targeting signal (PTS).

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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The Sorting Signals for Peroxisomal Membrane-bound Ascorbate Peroxidase Are within Its C-terminal Tail

Mullen

Trelease

2000

Journal of Biological Chemistry

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“…Peroxisomes are involved in various catabolic and anabolic pathways such as the photorespiration cycle, fatty acid ␤-oxidation, the glyoxalate cycle, ureide metabolism, and the generation of cellular messengers like superoxide radicals and nitric oxide (Tabak et al, 1999;Corpas et al, 2001). Unlike chloroplasts and mitochondria, peroxisomes do not possess their own DNA.…”

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confidence: 99%

Simultaneous Visualization of Peroxisomes and Cytoskeletal Elements Reveals Actin and Not Microtubule-Based Peroxisome Motility in Plants,

2002

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Peroxisomes were visualized in living plant cells using a yellow fluorescent protein tagged with a peroxisomal targeting signal consisting of the SKL motif. Simultaneous visualization of peroxisomes and microfilaments/microtubules was accomplished in onion (Allium cepa) epidermal cells transiently expressing the yellow fluorescent protein-peroxi construct, a green fluorescent protein-mTalin construct that labels filamentous-actin filaments, and a green fluorescent proteinmicrotubule-binding domain construct that labels microtubules. The covisualization of peroxisomes and cytoskeletal elements revealed that, contrary to the reports from animal cells, peroxisomes in plants appear to associate with actin filaments and not microtubules. That peroxisome movement is actin based was shown by pharmacological studies. For this analysis we used onion epidermal cells and various cell types of Arabidopsis including trichomes, root hairs, and root cortex cells exhibiting different modes of growth. In transient onion epidermis assay and in transgenic Arabidopsis plants, an interference with the actin cytoskeleton resulted in progressive loss of saltatory movement followed by the aggregation and a complete cessation of peroxisome motility within 30 min of drug application. Microtubule depolymerization or stabilization had no effect.

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Identification of peroxisomal membrane proteins ofSaccharomyces cerevisiae by mass spectrometry

et al. 2001

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The identification of peroxisomal membrane proteins is very important to understand the import mechanisms of substrates and proteins into these organelles and the pathogenesis of human peroxisomal disorders like the Zellweger Syndrom. Peroxisomal membrane proteins were identified after separation by gel electrophoresis, tryptic digestion and mass spectrometric analysis. Using matrix assisted laser desorption/ionization-mass spectrometry (MALDI-MS) and nanoliquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS), it was possible to identify 45 proteins of isolated yeast peroxisomal membranes.

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Peroxisomes: simple in function but complex in maintenance

Cited by 68 publications

References 43 publications

The Sorting Signals for Peroxisomal Membrane-bound Ascorbate Peroxidase Are within Its C-terminal Tail

The Sorting Signals for Peroxisomal Membrane-bound Ascorbate Peroxidase Are within Its C-terminal Tail

Simultaneous Visualization of Peroxisomes and Cytoskeletal Elements Reveals Actin and Not Microtubule-Based Peroxisome Motility in Plants,

Identification of peroxisomal membrane proteins ofSaccharomyces cerevisiae by mass spectrometry

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