Penicillium chrysogenum Pex5p mediates differential sorting of PTS1 proteins to microbodies of the methylotrophic yeast Hansenula polymorpha

Kiel, Jan A.K.W.; Berg, Marco van den; Bovenberg, Roel A. L.; Klei, Ida J. van der; Veenhuis, Marten

doi:10.1016/j.fgb.2004.02.006

Cited by 24 publications

(26 citation statements)

References 45 publications

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“…This was based on the observation that a PTS signal from a heterologous protein can target a marker protein into microbodies in baker's yeast as well as in mammalian cells (see Gould et al 1990;Purdue and Lazarow 1996). Moreover, the fusion of -SKL-COOH to the C terminus of the normally cytosolic GFP protein results in its sorting to microbodies in all eukaryotes including P. chrysogenum (see Kiel et al 2004).…”

Section: Discussionmentioning

confidence: 99%

“…Recently, we demonstrated that P. chrysogenum Pex5p could efficiently sort catalase (-SKI-COOH), dihydroxyacetone synthase (-NKL-COOH), and eGFP.SKL into microbodies in the yeast Hansenula polymorpha (Kiel et al 2004). Thus, the P. chrysogenum PTS1 receptor can recognize highly diverse signals, which is consistent with the identification of 45 different putative PTS1 signals.…”

Section: Discussionmentioning

confidence: 99%

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Matching the proteome to the genome: the microbody of penicillin-producing Penicillium chrysogenum cells

Kiel

Berg

Fusetti

et al. 2009

Funct Integr Genomics

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In the filamentous fungus Penicillium chrysogenum, microbodies are essential for penicillin biosynthesis. To better understand the role of these organelles in antibiotics production, we determined the matrix enzyme contents of P. chrysogenum microbodies. Using a novel in silico approach, we first obtained a catalogue of 200 P. chrysogenum proteins with putative microbody targeting signals (PTSs). This included two orthologs of proteins involved in cephalosporin biosynthesis, which we demonstrate to be bona fide microbody matrix constituents. Subsequently, we performed a proteomics based inventory of P. chrysogenum microbody matrix proteins using nano-LC-MS/MS analysis. We identified 89 microbody proteins, 79 with a PTS, including the two known microbody-borne penicillin biosynthesis enzymes, isopenicillin N:acyl CoA acyltransferase and phenylacetyl-CoA ligase. Comparative analysis revealed that 69 out of 79 PTS proteins identified experimentally were in the reference list. A prominent microbody protein was identified as a novel fumarate reductase-cytochrome b5 fusion protein, which contains an internal PTS2 between the two functional domains. We show that this protein indeed localizes to P. chrysogenum microbodies.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Matching the proteome to the genome: the microbody of penicillin-producing Penicillium chrysogenum cells

Kiel

Berg

Fusetti

et al. 2009

Funct Integr Genomics

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“…Attempts to isolate P. chrysogenum peroxin deletion mutants have so far not been successful (8,9). However, high peroxisome abundance caused by overproduction of peroxin Pc-Pex11p led to a twofold increase in penicillin production (10), emphasizing the importance of these organelles for P. chrysogenum.…”

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Contribution of Peroxisomes to Penicillin Biosynthesis in Aspergillus nidulans

2009

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Peroxisomal localization of the third enzyme of the penicillin biosynthesis pathway of Aspergillus nidulans, acyl-coenzyme A:IPN acyltransferase (IAT), is mediated by its atypical peroxisomal targeting signal 1 (PTS1). However, mislocalization of IAT by deletion of either its PTS1 or of genes encoding proteins involved in peroxisome formation or transport does not completely abolish penicillin biosynthesis. This is in contrast to the effects of IAT mislocalization in Penicillium chrysogenum.

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“…A second exception is the ascomycete fungus Penicillium chrysogenum. In this fungus, a strain with a mutation in the PEX5 gene, required for transport of peroxisomally targeted proteins, shows poor growth, while isolation of mutants with mutation in PEX1 or PEX6 was not possible, suggesting that these genes may be essential (31,33). A recent report from another ascomycete, M. grisea, suggests that growth rate of the pex6 mutant strain is also slightly reduced (60).…”

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confidence: 99%

Peroxisome Function Regulates Growth on Glucose in the Basidiomycete Fungus Cryptococcus neoformans

Idnurm¹,

Giles²,

Perfect

et al. 2007

Eukaryot Cell

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The function of the peroxisomes was examined in the pathogenic basidiomycete Cryptococcus neoformans. Recent studies reveal the glyoxylate pathway is required for virulence of diverse microbial pathogens of plants and animals. One exception is C. neoformans, in which isocitrate lyase (encoded by ICL1) was previously shown not to be required for virulence, and here this was extended to exclude also a role for malate synthase (encoded by MLS1). The role of peroxisomes, in which the glyoxylate pathway enzymes are localized in many organisms, was examined by mutation of two genes (PEX1 and PEX6) encoding AAA (ATPases associated with various cellular activities)-type proteins required for peroxisome formation. The pex1 and pex6 deletion mutants were unable to localize the fluorescent DsRED-SKL protein to peroxisomal punctate structures, in contrast to wild-type cells. pex1 and pex6 single mutants and a pex1 pex6 double mutant exhibit identical phenotypes, including abolished growth on fatty acids but no growth difference on acetate. Because both icl1 and mls1 mutants are unable to grow on acetate as the sole carbon source, these findings demonstrate that the glyoxylate pathway can function efficiently outside the peroxisome in C. neoformans. The pex1 mutant exhibits wild-type virulence in a murine inhalation model and in an insect host, demonstrating that peroxisomes are not required for virulence under these conditions. An unusual phenotype of the pex1 and pex6 mutants was that they grew poorly with glucose as the carbon source, but nearly wild type with galactose, which suggested impaired hexokinase function and that C. neoformans peroxisomes might function analogously to the glycosomes of the trypanosomid parasites. Deletion of the hexokinase HXK2 gene reduced growth in the presence of glucose and suppressed the growth defect of the pex1 mutant on glucose. The hexokinase 2 protein of C. neoformans contains a predicted peroxisome targeting signal (type 2) motif; however, Hxk2 fused to fluorescent proteins was not localized to peroxisomes. Thus, we hypothesize that glucose or glycolytic metabolites are utilized in the peroxisome by an as yet unidentified enzyme or regulate a pathway required by the fungus in the absence of peroxisomes.

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Penicillium chrysogenum Pex5p mediates differential sorting of PTS1 proteins to microbodies of the methylotrophic yeast Hansenula polymorpha

Cited by 24 publications

References 45 publications

Matching the proteome to the genome: the microbody of penicillin-producing Penicillium chrysogenum cells

Matching the proteome to the genome: the microbody of penicillin-producing Penicillium chrysogenum cells

Contribution of Peroxisomes to Penicillin Biosynthesis in Aspergillus nidulans

Peroxisome Function Regulates Growth on Glucose in the Basidiomycete Fungus Cryptococcus neoformans

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