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

Kiel, Jan A.K.W.; Berg, M. A.; Fusetti, Fabrizia; Poolman, Bert; Bovenberg, Roel A. L.; Veenhuis, Marten; Klei, Ida J. van der

doi:10.1007/s10142-009-0110-6

Cited by 84 publications

(100 citation statements)

References 65 publications

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“…Protein Family-Previously, we identified a putative peroxisomal Lon protease (designated Pln) in the fungus P. chrysogenum by in silico identification of proteins that contain a putative peroxisomal targeting signal 1 (PTS1 (26). We confirmed the peroxisomal localization of this protein by fluorescence microscopy using cells producing a GFP-Pln fusion protein in conjunction with DsRed-SKL as a peroxisomal matrix marker (Fig.…”

Section: P Chrysogenum Peroxisomes Contain a Protease Of The Lon Amentioning

confidence: 76%

“…Biochemical Methods-Crude extract of P. chrysogenum cells were prepared as described previously (26). Protein concentrations were determined using the RC-DC assay system or BioRad assay kit (Bio-Rad) using bovine serum albumin (BSA) as a standard.…”

Section: Generation and Purification Of A Proteolytically Inactive Plnmentioning

confidence: 99%

“…SDS-PAGE and Western blotting were carried out in accordance with established procedures. P. chrysogenum cell fractionation and peroxisome isolation were performed as described previously (26). Catalase activity was measured spectrophotometrically as described before (14).…”

Section: Generation and Purification Of A Proteolytically Inactive Plnmentioning

confidence: 99%

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Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone

Bartoszewska

Williams

Kikhney

et al. 2012

Journal of Biological Chemistry

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Background: A putative Lon protease has been identified in peroxisomes of various species (Pln). Results: Pln is an ATP-dependent protease that digests unfolded substrates e.g. oxidatively damaged catalase-peroxidase, and displays chaperone-like activity, circumventing accumulation of protein aggregates in peroxisomes that compromise organelle function. Conclusion: Pln is a bifunctional protein with chaperone and protease activities. Significance: Pln is crucial for peroxisome proteostasis.

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Section: P Chrysogenum Peroxisomes Contain a Protease Of The Lon Amentioning

confidence: 76%

Section: Generation and Purification Of A Proteolytically Inactive Plnmentioning

confidence: 99%

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Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone

Bartoszewska

Williams

Kikhney

et al. 2012

Journal of Biological Chemistry

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“…Sequence alignment of yeast and fungal Aat2 proteins revealed that most contain either a PTS1 or PTS2 33, whereas Aat2p from Penicillium rubens displays both. However, H. polymorpha Aat2p does not possess a recognizable PTS, similar to Aat2p from several other yeast species (Fig.…”

Section: Resultsmentioning

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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“…Moreover, several authors (131 -133) determined that the optimum pH for the in vitro conversion of IPN into PenN in A. chrysogenum cell-free extracts was 7.0, near the estimated pH of the peroxisomal lumen (107) . Additionally, the CefD1 and CefD2 homologous proteins have been identified in the peroxisome matrix of P. chrysogenum by mass spectrometry (134) .…”

Section: Role Of Two Peroxisomal Membrane Transporters In Cephalospormentioning

confidence: 99%

Transport of substrates into peroxisomes: the paradigm of β-lactam biosynthetic intermediates

Martı́n

Garcı́a-Estrada

Ullán

2013

BioMolecular Concepts

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Peroxisomes are ubiquitous organelles that enclose catalases, fatty acid-oxidizing enzymes, and a variety of proteins involved in different cellular processes. Interestingly, the late enzymes involved in penicillin biosynthesis, and the isopenicillin N epimerization enzymes involved in cephalosporin biosynthesis are located inside peroxisomes in the producer fungi Penicillium chrysogenum and Acremonium chrysogenum. Peroxisome proteins are targeted to those organelles by peroxisomal targeting signals located at the C-terminus (PTS1) or near the N-terminal end (PTS2) of those proteins. Peroxisomal membrane proteins (PMPs) are largely recruited by the interaction with specific sequences in the Pex19 protein. The compartmentalization into peroxisomes of several steps of the biosynthesis of penicillin, cephalosporin, and other secondary metabolites raises the question of how the precursors and/or intermediates of the biosynthesis of β -lactam antibiotics are transported into peroxisomes and the mechanisms of secretion of the final products (penicillin or cephalosporin) from peroxisomes to the extracellular medium. Recent advances in peroxisome proteomics, immunoelectron microscopy, and fluorescence labeling have shown that the transport of these intermediates is mediated by membrane proteins of the major facilitator superfamily class (drug/H + antiporters) containing 12 transmembrane-spanning domains (TMS). In some cases, the transport of the substrates (e.g., fatty acids) or intermediates may be mediated by ATP-binding cassette (ABC) transporters. Knowledge on the transport and secretion mechanisms is of paramount importance to understand the complex mechanisms of cell differentiation and their crosstalk with the biosynthesis of different secondary metabolites that act as biochemical signals between the producer cells and also as communication signals with competing microorganisms (e.g., antimicrobial agents or plant elicitors).

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

Cited by 84 publications

References 65 publications

Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone

Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone

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

Transport of substrates into peroxisomes: the paradigm of β-lactam biosynthetic intermediates

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