Saccharomyces cerevisiae Acyl-CoA Oxidase Follows a Novel, Non-PTS1, Import Pathway into Peroxisomes That Is Dependent on Pex5p

Klein, André; Berg, Marlene van den; Bottger, Gina; Tabak, Henk F.; Distel, Ben

doi:10.1074/jbc.m203254200

Cited by 127 publications

(147 citation statements)

References 79 publications

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“…Recently, Distel and coworkers (Klein et al, 2002) indicated that S. cerevisiae acyl-CoA oxidase, a protein that lacks both a PTS1 and PTS2, interacts with the N-terminus of ScPex5p and Purdue and Lazarow (2001) reported that the region of ScPex5p responsible for this interaction was mapped to residues 136 -292 of ScPex5p, a domain clearly distinct from the TPR repeat region. Whether the corresponding region of HpPex5p is involved in AO binding is the topic of current investigations.…”

Section: Discussionmentioning

confidence: 99%

Routing ofHansenula polymorphaAlcohol Oxidase: An Alternative Peroxisomal Protein-sorting Machinery

Gunkel

Dijk

Veenhuis

et al. 2004

MBoC

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Import of Hansenula polymorpha alcohol oxidase (AO) into peroxisomes is dependent on the PTS1 receptor, HpPex5p. The PTS1 of AO (-LARF) is sufficient to direct reporter proteins to peroxisomes. To study AO sorting in more detail, strains producing mutant AO proteins were constructed. AO containing a mutation in the FAD binding fold was mislocalized to the cytosol. This indicates that the PTS1 of AO is not sufficient for import of AO. AO protein in which the PTS1 was destroyed (؊LARA) was normally sorted to peroxisomes. Moreover, C-terminal deletions of up to 16 amino acids did not significantly affect AO import, indicating that the PTS1 was not necessary for targeting. Consistent with these observations we found that AO import occurred independent from the C-terminal TPR-domain of HpPex5p, known to bind PTS1 peptides. Synthesis of the N-terminal domain (amino acids 1-272) of HpPex5p in pex5 cells restored AO import, whereas other PTS1 proteins were mislocalized to the cytosol. These data indicate that AO is imported via a novel HpPex5p-dependent protein translocation pathway, which does not require the PTS1 of AO and the C-terminal TPR domains of HpPex5p, but involves FAD binding and the N-terminus of HpPex5p.

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Section: Discussionmentioning

confidence: 99%

Routing ofHansenula polymorphaAlcohol Oxidase: An Alternative Peroxisomal Protein-sorting Machinery

Gunkel

Dijk

Veenhuis

et al. 2004

MBoC

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“…This creates a window where they may be temporarily active in the cytosol. In some studies, 15 to 25% of the ␤-oxidation enzyme activities were found in the cytosol of yeast (6,10,14,26). This explains why wild-type yeast can synthesize PHA in the cytosol and why PHA synthesized in wild-type yeast and the pex5 mutants contains PHA monomers with C backbones different in length than the fed fatty acids.…”

Section: Discussionmentioning

confidence: 93%

“…The acyl coenzyme A (acyl-CoA) oxidase Fox1p follows a novel, non-PTS1, import pathway that is also dependent on Pex5p (14). In pex5 mutants, both Fox2p and Fox1p are found in the cytosol but Fox3p is located in peroxisomes (25).…”

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confidence: 99%

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Engineering the Monomer Composition of Polyhydroxyalkanoates Synthesized in Saccharomyces cerevisiae

Zhang

Carlson

Srienc

2006

Appl Environ Microbiol

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Polyhydroxyalkanoates (PHAs) have received considerable interest as renewable-resource-based, biodegradable, and biocompatible plastics with a wide range of potential applications. We have engineered the synthesis of PHA polymers composed of monomers ranging from 4 to 14 carbon atoms in either the cytosol or the peroxisome of Saccharomyces cerevisiae by harnessing intermediates of fatty acid metabolism. Cytosolic PHA production was supported by establishing in the cytosol critical ␤-oxidation chemistries which are found natively in peroxisomes. This platform was utilized to supply medium-chain (C 6 to C 14 ) PHA precursors from both fatty acid degradation and synthesis to a cytosolically expressed medium-chain-length (mcl) polymerase from Pseudomonas oleovorans. Synthesis of short-chain-length PHAs (scl-PHAs) was established in the peroxisome of a wild-type yeast strain by targeting the Ralstonia eutropha scl polymerase to the peroxisome. This strain, harboring a peroxisomally targeted scl-PHA synthase, accumulated PHA up to approximately 7% of its cell dry weight. These results indicate (i) that S. cerevisiae expressing a cytosolic mcl-PHA polymerase or a peroxisomal scl-PHA synthase can use the 3-hydroxyacyl coenzyme A intermediates from fatty acid metabolism to synthesize PHAs and (ii) that fatty acid degradation is also possible in the cytosol as ␤-oxidation might not be confined only to the peroxisomes. Polymers of even-numbered, odd-numbered, or a combination of even-and odd-numbered monomers can be controlled by feeding the appropriate substrates. This ability should permit the rational design and synthesis of polymers with desired material properties.

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“…Pex7p functions in cargo binding, whereas the coreceptors are required for membrane docking and recycling. Evidence exists for a third pathway that is independent of a PTS1, but requires the N‐terminal domain of Pex5p 16, 17. Sometimes referred to as the PTS3 pathway, to date no PTS3 consensus sequence has been described 18.…”

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confidence: 99%

Hansenula polymorphaAat2p is targeted to peroxisomes via a novel Pex20p‐dependent pathway

et al. 2018

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Saccharomyces cerevisiae Aat2p contains a peroxisomal targeting signal type‐1 and localizes to peroxisomes in oleate‐grown cells, but not in glucose‐grown cells. Here, we have investigated Aat2p from the yeast Hansenula polymorpha, which lacks a recognizable peroxisomal targeting signal. Aat2p tagged with GFP at its C terminus displays a dual cytosol‐peroxisome localization in ethanol‐grown cells. The partial peroxisomal localization of Aat2p persisted in the absence of the classical cycling receptors Pex5p and Pex7p but Aat2p targeting to peroxisomes was reduced in cells deleted for the matrix protein import factors PEX1, PEX2 and PEX13. Furthermore, we demonstrate that Aat2p targeting to peroxisomes requires Pex20p. Together, our data identify a Pex20p‐dependent pathway for targeting Aat2p to peroxisomes.

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Saccharomyces cerevisiae Acyl-CoA Oxidase Follows a Novel, Non-PTS1, Import Pathway into Peroxisomes That Is Dependent on Pex5p

Cited by 127 publications

References 79 publications

Routing ofHansenula polymorphaAlcohol Oxidase: An Alternative Peroxisomal Protein-sorting Machinery

Routing ofHansenula polymorphaAlcohol Oxidase: An Alternative Peroxisomal Protein-sorting Machinery

Engineering the Monomer Composition of Polyhydroxyalkanoates Synthesized in Saccharomyces cerevisiae

Hansenula polymorphaAat2p is targeted to peroxisomes via a novel Pex20p‐dependent pathway

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