Characterization of peroxisome-deficient mutants of Hansenula polymorpha

Tan, Xuqiu; Titorenko, Vladimir I.; Klei, Ida J. van der; Sulter, Grietje; Haima, Peter; Waterham, Hans R.; Evers, Melchior E.; Harder, W.; Veenhuis, Marten; Cregg, James M.

doi:10.1007/bf00309784

Cited by 23 publications

(15 citation statements)

References 64 publications

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“…2). This result, similar to the result obtained in cell fractionation experiments of the Pim -mutants of H. polymorpha (Waterham et al 1992;Tan et al 1995), suggests that the majority of peroxisomal enzyme activities remained either soluble in the cytosol or within very small peroxisomes that had not sedimented under the conditions used. As a control, we determined the activity of the mitochondrial enzyme fumarase in the supernatant (S2) and 20,000 × g pellet (P2).…”

Section: Strainsupporting

confidence: 88%

“…Evidence obtained by biochemical and ultrastructural studies suggests that the phenotype of perA21 mutant resembles the phenotype of Pim -mutants of H. polymorpha (Waterham et al 1992;Tan et al 1995). The Pimmutants of H. polymorpha are impaired in the utilization of carbon sources that require functional peroxisomes for metabolism.…”

Section: Discussionmentioning

confidence: 94%

“…It has been reported that peroxisomal enzymes of H. polymorpha are still active in the cytosol (Van der Klei et al 1991;Tan et al 1995), and therefore the possibility that the enzyme acyl CoA:isopenicillin N-acyltransferase could remain active in the cytosol of A. nidulans cannot be ruled out. Nevertheless, since the small peroxisomes present in perA21 cells contained small amounts of peroxisomal enzymes, it is also possible that the presence of a minor fraction of acyl CoA:isopenicillin N-acyltransferase correctly located in peroxisomes is sufficient to produce wild-type levels of penicillin.…”

Section: Discussionmentioning

confidence: 98%

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Characterization of oleate-nonutilizing mutants of Aspergillus nidulans isolated by the 3-amino-1,2,4-triazole positive selection method

Lucas

Valenciano

Domínguez

et al. 1997

Archives of Microbiology

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Conidia of Aspergillus nidulans were mutagenized with ultraviolet light and were incubated on a special selective medium containing the catalase inhibitor 3-amino-1,2,4-triazole. From approximately 5 x 10(7) viable UV-irradiated conidia tested, 423 stable mutants resistant to 3-amino-1,2,4-triazole were recovered, of which 40 were unable to grow on minimal medium with oleic acid as the sole carbon source. These oleate-nonutilizing (Ole-) mutants did not grow on medium with carbon sources requiring functional peroxisomes (oleate, butyrate, acetate, or ethanol), but grew well on medium with carbon sources supposedly not requiring such organelles (glucose, glycerol, l-glutamate, or l-proline). The Ole- mutants carried mutations in one of five nuclear genes affecting acetate utilization: acuJ, acuH, acuE, acuL, and perA. The perA21 strain (DL21) carried a mutation in a gene that is not allelic with any of the known acu loci and displayed a phenotype resembling that described in the Pim- (peroxisome import defective) mutants of Hansenula polymorpha. Hyphae of the perA21 mutant contained a few small peroxisomes with the bulk of peroxisomal enzymes remaining in the 20,000 x g supernatant, but produced wild-type levels of penicillin.

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Section: Strainsupporting

confidence: 88%

Section: Discussionmentioning

confidence: 94%

Section: Discussionmentioning

confidence: 98%

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Characterization of oleate-nonutilizing mutants of Aspergillus nidulans isolated by the 3-amino-1,2,4-triazole positive selection method

Lucas

Valenciano

Domínguez

et al. 1997

Archives of Microbiology

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“…The search for genes defective in PBD patients has been greatly aided by genetic screens for peroxisome biogenesis (pex) mutants in several divergent yeasts (Erdmann et al 1989;Gould et al 1992;Liu et al 1992;Tan et al 1995). Yeast serves as an excellent model system because the process of peroxisome biogenesis is evolutionarily very well conserved.…”

mentioning

confidence: 99%

The Role of the Endoplasmic Reticulum in Peroxisome Biogenesis

Dimitrov

Lam

Schekman

2013

Cold Spring Harbor Perspectives in Biology

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Peroxisomes are essential cellular organelles involved in lipid metabolism. Patients affected by severe peroxisome biogenesis disorders rarely survive their first year. Genetic screens in several model organisms have identified more than 30 PEX genes that are required for the formation of functional peroxisomes. Despite significant work on the PEX genes, the biogenic origin of peroxisomes remains controversial. For at least two decades, the prevailing model postulated that peroxisomes propagate by growth and fission of preexisting peroxisomes. In this review, we focus on the recent evidence supporting a new, semiautonomous model of peroxisomal biogenesis. According to this model, peroxisomal membrane proteins (PMPs) traffic from the endoplasmic reticulum (ER) to the peroxisome by a vesicular budding, targeting, and fusion process while peroxisomal matrix proteins are imported into the organelle by an autonomous, posttranslational mechanism. We highlight the contradictory conclusions reached to answer the question of how PMPs are inserted into the ER. We then review what we know and what still remains to be elucidated about the mechanism of PMP exit from the ER and the contribution of preperoxisomal vesicles to mature peroxisomes. Finally, we discuss discrepancies in our understanding of de novo peroxisome biogenesis in wild-type cells. We anticipate that resolving these key issues will lead to a more complete picture of peroxisome biogenesis.

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“…In either case, the presence of a wild-type allele may account for the restricted nature of the import defect. Although not common, dominant negative alleles for two genes involved in peroxisome biogenesis have been described (53). Interestingly these dominant negative alleles yield a peroxisome import defect when present with a wild-type allele in diploid cells of the yeast Hansenula polymorpha but peroxisome deficiency when alone in haploids.…”

Section: Discussionmentioning

confidence: 99%

Functional Identification of a Leishmania Gene Related to the Peroxin 2 Gene Reveals Common Ancestry of Glycosomes and Peroxisomes

Flaspohler

Rickoll

Beverley

et al. 1997

Molecular and Cellular Biology

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Glycosomes are membrane-bounded microbody organelles that compartmentalize glycolysis as well as other important metabolic processes in trypanosomatids. The compartmentalization of these enzymatic reactions is hypothesized to play a crucial role in parasite physiology. Although the metabolic role of glycosomes differs substantially from that of the peroxisomes that are found in other eukaryotes, similarities in signals targeting proteins to these organelles suggest that glycosomes and peroxisomes may have evolved from a common ancestor. To examine this hypothesis, as well as gain insights into the function of the glycosome, we used a positive genetic selection procedure to isolate the first Leishmania mutant (gim1-1 [glycosome import] mutant) with a defect in the import of glycosomal proteins. The mutant retains glycosomes but mislocalizes a subset glycosomal proteins to the cytoplasm. Unexpectedly, the gim1-1 mutant lacks lipid bodies, suggesting a heretofore unknown role of the glycosome. We used genetic approaches to identify a gene, GIM1, that is able to restore import and lipid bodies. A nonsense mutation was found in one allele of this gene in the mutant line. The predicted Gim1 protein is related the peroxin 2 family of integral membrane proteins, which are required for peroxisome biogenesis. The similarities in sequence and function provide strong support for the common origin model of glycosomes and peroxisomes. The novel phenotype of gim1-1 and distinctive role of Leishmania glycosomes suggest that future studies of this system will provide a new perspective on microbody biogenesis and function.

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Characterization of peroxisome-deficient mutants of Hansenula polymorpha

Cited by 23 publications

References 64 publications

Characterization of oleate-nonutilizing mutants of Aspergillus nidulans isolated by the 3-amino-1,2,4-triazole positive selection method

Characterization of oleate-nonutilizing mutants of Aspergillus nidulans isolated by the 3-amino-1,2,4-triazole positive selection method

The Role of the Endoplasmic Reticulum in Peroxisome Biogenesis

Functional Identification of a Leishmania Gene Related to the Peroxin 2 Gene Reveals Common Ancestry of Glycosomes and Peroxisomes

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