Peroxisome protein import: a complex journey

Baker, Alison; Lanyon‐Hogg, Thomas; Warriner, S. L.

doi:10.1042/bst20160036

Cited by 39 publications

(32 citation statements)

References 69 publications

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“…The machinery that transports these proteins to the peroxisome matrix comprises many different components [4][5][6][7]. Most are exclusively dedicated to this taskthese belong to the so-called peroxin family [8].…”

Section: Introductionmentioning

confidence: 99%

Membrane topologies of PEX13 and PEX14 provide new insights on the mechanism of protein import into peroxisomes

et al. 2018

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PEX13 and PEX14 are two core components of the so‐called peroxisomal docking/translocation module, the transmembrane hydrophilic channel through which newly synthesized peroxisomal proteins are translocated into the organelle matrix. The two proteins interact with each other and with PEX5, the peroxisomal matrix protein shuttling receptor, through relatively well characterized domains. However, the topologies of these membrane proteins are still poorly defined. Here, we subjected proteoliposomes containing PEX13 or PEX14 and purified rat liver peroxisomes to protease‐protection assays and analyzed the protected protein fragments by mass spectrometry, Edman degradation and western blotting using antibodies directed to specific domains of the proteins. Our results indicate that PEX14 is a bona fide intrinsic membrane protein with a Nin‐Cout topology, and that PEX13 adopts a Nout‐Cin topology, thus exposing its carboxy‐terminal Src homology 3 [SH3] domain into the organelle matrix. These results reconcile several enigmatic findings previously reported on PEX13 and PEX14 and provide new insights into the organization of the peroxisomal protein import machinery. Enzymes Trypsin, http://www.chem.qmul.ac.uk/iubmb/enzyme/EC3/4/21/4.html; Proteinase K, http://www.chem.qmul.ac.uk/iubmb/enzyme/EC3/4/21/64.html; Tobacco etch virus protease, http://www.chem.qmul.ac.uk/iubmb/enzyme/EC3/4/22/44.html.

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Section: Introductionmentioning

confidence: 99%

Membrane topologies of PEX13 and PEX14 provide new insights on the mechanism of protein import into peroxisomes

et al. 2018

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“…One considerable difference of peroxisomal import to many other cellular protein import systems is that matrix proteins are imported post-translationally in a folded state, or even as protein complexes, across the peroxisomal membrane ( Walton et al. 1995 ; Baker et al. 2016 ).…”

Section: Introductionmentioning

confidence: 99%

Identification and localization of peroxisomal biogenesis proteins indicates the presence of peroxisomes in the cryptophyte Guillardia theta and other ‘chromalveolates’

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Cenci

Heimerl

et al. 2018

Genome Biology and Evolution

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Peroxisomes are single-membrane-bound organelles with a huge metabolic versatility, including the degradation of fatty acids (β-oxidation) and the detoxification of reactive oxygen species as most conserved functions. Although peroxisomes seem to be present in the majority of investigated eukaryotes, where they are responsible for many eclectic and important spatially separated metabolic reactions, knowledge about their existence in the plethora of protists (eukaryotic microorganisms) is scarce. Here, we investigated genomic data of organisms containing complex plastids with red algal ancestry (so-called “chromalveolates”) for the presence of genes encoding peroxins—factors specific for the biogenesis, maintenance, and division of peroxisomes in eukaryotic cells. Our focus was on the cryptophyte Guillardia theta, a marine microalga, which possesses two phylogenetically different nuclei of host and endosymbiont origin, respectively, thus being of enormous evolutionary significance. Besides the identification of a complete set of peroxins in G. theta, we heterologously localized selected factors as GFP fusion proteins via confocal and electron microscopy in the model diatom Phaeodactylum tricornutum. Furthermore, we show that peroxins, and thus most likely peroxisomes, are present in haptophytes as well as eustigmatophytes, brown algae, and alveolates including dinoflagellates, chromerids, and noncoccidian apicomplexans. Our results indicate that diatoms are not the only “chromalveolate” group devoid of the PTS2 receptor Pex7, and thus a PTS2-dependent peroxisomal import pathway, which seems to be absent in haptophytes (Emiliania huxleyi) as well. Moreover, important aspects of peroxisomal biosynthesis and protein import in “chromalveolates”are highlighted.

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“…It is well known that the sorting of proteins to peroxisomes mainly depends on either of two types of signal sequences, PTS1 and PTS2 (see Rucktäschel et al, 2011 ; Baker et al, 2016 ; Erdmann, 2016 for reviews and references within). The PTS1 as the most common one, is a tripeptide present at the C-termini of proteins and frequently ends with the sequence S-K-L or its variants with a consensus sequence S/A/C-K/R/H-L/M ( Gould et al, 1989 ; Lametschwandtner et al, 1998 ; Brocard and Hartig, 2006 ; Williams et al, 2012 ; see Dias et al, 2016 ; Meinecke et al, 2016 for reviews and references within).…”

Section: Discussionmentioning

confidence: 99%

“…The PTS1 as the most common one, is a tripeptide present at the C-termini of proteins and frequently ends with the sequence S-K-L or its variants with a consensus sequence S/A/C-K/R/H-L/M ( Gould et al, 1989 ; Lametschwandtner et al, 1998 ; Brocard and Hartig, 2006 ; Williams et al, 2012 ; see Dias et al, 2016 ; Meinecke et al, 2016 for reviews and references within). In contrast to PTS1, the PTS2 functions at internal locations, with a conserved non-apeptide in the N-terminal domain, such as R-L-X5-H-L, and R/K-L/V/I-X5-H/Q-L/A (X: any amino acid) ( Terlecky et al, 1995 ; Petriv et al, 2004 ; see Baker et al, 2016 ; Meinecke et al, 2016 for reviews and references within).…”

Section: Discussionmentioning

confidence: 99%

Subcellular Localization of a Plant Catalase-Phenol Oxidase, AcCATPO, from Amaranthus and Identification of a Non-canonical Peroxisome Targeting Signal

2017

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AcCATPO is a plant catalase-phenol oxidase recently identified from red amaranth. Its physiological function remains unexplored. As the starting step of functional analysis, here we report its subcellular localization and a non-canonical targeting signal. Commonly used bioinformatics programs predicted a peroxisomal localization for AcCATPO, but failed in identification of canonical peroxisomal targeting signals (PTS). The C-terminal GFP tagging led the fusion protein AcCATPO-GFP to the cytosol and the nucleus, but N-terminal tagging directed the GFP-AcCATPO to peroxisomes and nuclei, in transgenic tobacco. Deleting the tripeptide (PTM) at the extreme C-terminus almost ruled out the peroxisomal localization of GFP-AcCATPOΔ3, and removing the C-terminal decapeptide completely excluded peroxisomes as the residence of GFP-AcCATPOΔ10. Furthermore, this decapeptide as a targeting signal could import GFP-10aa to the peroxisome exclusively. Taken together, these results demonstrate that AcCATPO is localized to the peroxisome and the nucleus, and its peroxisomal localization is attributed to a non-canonical PTS1, the C-terminal decapeptide which contains an internal SRL motif and a conserved tripeptide P-S/T-I/M at the extreme of C-terminus. This work may further the study as to the physiological function of AcCATPO, especially clarify its involvement in betalain biosynthesis, and provide a clue to elucidate more non-canonic PTS.

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Peroxisome protein import: a complex journey

Cited by 39 publications

References 69 publications

Membrane topologies of PEX13 and PEX14 provide new insights on the mechanism of protein import into peroxisomes

Membrane topologies of PEX13 and PEX14 provide new insights on the mechanism of protein import into peroxisomes

Identification and localization of peroxisomal biogenesis proteins indicates the presence of peroxisomes in the cryptophyte Guillardia theta and other ‘chromalveolates’

Subcellular Localization of a Plant Catalase-Phenol Oxidase, AcCATPO, from Amaranthus and Identification of a Non-canonical Peroxisome Targeting Signal

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