Localization of isopenicillin N synthase in Penicillium chrysogenum PQ-96

Kurzątkowski, W; Palissa, H.; Liempt, Henk van; Döhren, Hans von; Kleinkauf, Horst; Wolf, W. P.; KURYŁOWICZ, WŁODZIMIERZ

doi:10.1007/bf00169760

Cited by 14 publications

(12 citation statements)

References 7 publications

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“…For electron microscopy ultrathin sections of hyphae from the periphery and central parts of pellets were prepared by the procedure of Strunk (1978) modified by Kurzatkowski et al (1991). Immunolabelling on ultrathin sections was carried out basically according to Kurzatkowski et al (1991).…”

Section: Methodsmentioning

confidence: 99%

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In situ localization of manganese peroxidase production in mycelial pellets of Phanerochaete chrysosporium

Jimenez-Tobon

Kurzątkowski²,

Rozbicka³

et al. 2003

Microbiology

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The ultrastructure of Phanerochaete chrysosporium hyphae from pellets in submerged liquid cultures was investigated in order to learn more about the interrelation between fungal architecture and manganese peroxidase (MnP) production. At day 2 of cultivation, some subapical regions of hyphae in the outer and middle zones of the pellet initiated differentiation into intercalary thick-walled chlamydospore-like cells of about 10 mm diameter. At the periphery of the cytoplasm of these cells, a large number of mitochondria and Golgi-like vesicles were observed. The sites of MnP production were localized at different stages of cultivation by an immunolabelling procedure. The immunomarker of MnP was mainly concentrated in the chlamydospore-like cells and principally distributed in Golgi-like vesicles located at the periphery of the cytoplasm. The apices of hyphae in the outer layer of the pellets were apparently minor sites of MnP production. Maximal MnP release into the culture supernatant coincided with apparent autolysis of the chlamydospore-like cells. Production of extracellular autolytic chitinase and protease coincided with the disappearance of these structures from the pellets. The chlamydospore-like cells observed in the mycelial pellets of P. chrysosporium could be metabolically active entities operating as an enzyme reservoir, delivering their content into the surrounding medium possibly by an enzyme-mediated autolytic process.

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Section: Methodsmentioning

confidence: 99%

“…Immunolabelling on ultrathin sections was carried out basically according to Kurzatkowski et al (1991). For the immunodetection of MnP, a rabbit antiserum obtained according to Jiménez-Tobon (1999) was raised against a highly purified preparation of the H3 enzyme isoform (Orth et al, 1994).…”

Section: Methodsmentioning

confidence: 99%

In situ localization of manganese peroxidase production in mycelial pellets of Phanerochaete chrysosporium

Jimenez-Tobon

Kurzątkowski²,

Rozbicka³

et al. 2003

Microbiology

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“…IPNS appeared to be a soluble cytosolic enzyme (van der Lende et al, 2002a), although its activity in cell free extracts seems to be stimulated by sonification (for review, see van de Kamp et al, 1999) -it suggests a partial compartmentalization of IPNS. This enzyme was also reported to be associated with membranous structures (Kurzątkowski et al, 1991). The enzyme IAT was located in peroxisomes -also called microbodies (Müller et al, 1995;van der Lende et al, 2002a).…”

Section: Introductionmentioning

confidence: 96%

“…Localization of the pathway of Pen G biosynthesis in P. chrysogenum cells has been studied using transmis-sion electron microscopy (Kurzątkowski et al, 1991), immuno-gold electron microscopy (Kurzątkowski et al, 1991;Müller et al, 1995;van der Lende et al, 2002a), cell fractionation (Müller et al, 1995;van der Lende et al, 2002a), biochemical and genetic methods (Martin et al, 2012). Nevertheless, at present, the reports concerning the cellular localization of ACVS and IPNS are ambiguous.…”

Section: Introductionmentioning

confidence: 99%

Compartmentalization in Penicillin G Biosynthesis by Penicillium chrysogenum PQ-96

Kurzątkowski¹,

Staniszewska²,

Bondaryk³

et al. 2014

Pol J Microbiol

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The arrangement of organelles in the sub-apical productive non-growing vacuolated hyphal cells of the high- and the low-penicillin-pro- ducing strains Penicillium chrysogenum was compared using transmission electron microscopy. In the productive cells of the high-yielding strain the endoplasmic reticulum and the polyribosomes with associated peroxisomes are frequently arranged at the periphery of the cytoplasm and around the vacuoles. At the high activity of penicillin G biosynthesis the immuno-label of the cytosolic isopenicillin N synthase is concentrated at the polyribosomes arranged in the peripheral cytoplasm and along the tonoplast as well as around the peroxisomes. On the basis of the obtained results the compartmentalization of the pathway of penicillin G biosymthesis is discussed. The obtained results support the phenylacetic acid detoxification hypothesis of penicillin G biosynthesis.

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“…Electron microscopy. After 24 h of induction of invertase secretion, the mycelium was collected by centrifugation at 2 000´g for 10 min and processed for electron microscopy as described previously (Kurzątkowski et al, 1991). Ultrathin sections were examined under a JEM100C transmission electron microscope (JEOL Ltd., Tokyo, Japan) at 80 kV.…”

Section: Methodsmentioning

confidence: 99%

Protein production and secretion in an Aspergillus nidulans mutant impaired in glycosylation.

Perlińska-Lenart

Kurzątkowski²,

Janas³

et al. 2005

Acta Biochim Pol

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O-glycosylation has been considered a limiting factor in protein secretion in filamentous fungi. Overexpression of the yeast DPM1 gene encoding dolichylphosphate mannose synthase (DPMS) in an Aspergillus nidulans mutant (BWB26A) deficient in O-glycosylation caused an increase in the number of secretory vesicles and changes in protein secretion. However, the secretory proteins, primarily O-mannosylated glucoamylase and N-glycosylated invertase, were mainly trapped in the periplasmic space. Different glycoforms of invertase were found insite the cells, in the periplasmic space and in the cultivation medium. Our data point to the importance of the cell wall as a barrier in protein secretion.Elucidation of the regulatory mechanisms and limiting factors in O-glycosylation of secreted proteins is an important task, since the efficiency of protein secretion appears to be related to their O-glycosylation (Kubicek et al., 1987;Kruszewska et al., 1999;Agaphonov et al., 2001). It has been shown for Trichoderma reesei that inhibition of O-glycosylation, in Vol. 52 No. 1/2005 195-205 QUARTERLY .

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Localization of isopenicillin N synthase in Penicillium chrysogenum PQ-96

Cited by 14 publications

References 7 publications

In situ localization of manganese peroxidase production in mycelial pellets of Phanerochaete chrysosporium

In situ localization of manganese peroxidase production in mycelial pellets of Phanerochaete chrysosporium

Compartmentalization in Penicillin G Biosynthesis by Penicillium chrysogenum PQ-96

Protein production and secretion in an Aspergillus nidulans mutant impaired in glycosylation.

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