Result 1 - 10 of total 30
populaties, extractie en ontwikkelen pottoets : 2022
2023
| Keywords | Life Science |
|---|---|
| Language | Dutch |
| Publisher | UIREKA |
| Publishing country | nl |
| Document type | Book ; Online |
| Database | BASE - Bielefeld Academic Search Engine (life sciences selection) |
Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.
Methods in molecular biology (Clifton, N.J.)
2012 Volume 835, Page(s) 209–217
Abstract: In this chapter a method for the heterologous production of fungal proteins in the yeast Pichia pastoris is described. Starting with cloning of the sequence encoding the gene of interest into the expression vector, this protocol describes P. pastoris ... ...
| Abstract | In this chapter a method for the heterologous production of fungal proteins in the yeast Pichia pastoris is described. Starting with cloning of the sequence encoding the gene of interest into the expression vector, this protocol describes P. pastoris transformation, production of the protein in a fermentor, and purification of the protein. This method has successfully been used for the production of a number of fungal effector proteins. |
|---|---|
| MeSH term(s) | Bioreactors ; Cloning, Molecular/methods ; Fungal Proteins/genetics ; Fungal Proteins/isolation & purification ; Fungal Proteins/metabolism ; Fungi/genetics ; Fungi/metabolism ; Genetic Vectors/genetics ; Industrial Microbiology/methods ; Pichia/genetics ; Pichia/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Transformation, Genetic |
| Chemical Substances | Fungal Proteins ; Recombinant Proteins |
| Language | English |
| Publishing date | 2012 |
| Publishing country | United States |
| Document type | Journal Article |
| ISSN | 1940-6029 |
| ISSN (online) | 1940-6029 |
| DOI | 10.1007/978-1-61779-501-5_13 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.
Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.
2022 Volume 190, Issue 3, Page(s) 2033–2044
Abstract: Chitin is a homopolymer of β-(1,4)-linked N-acetyl-D-glucosamine (GlcNAc) and a major structural component of fungal cell walls. In plants, chitin acts as a microbe-associated molecular pattern (MAMP) that is recognized by lysin motif (LysM)-containing ... ...
| Abstract | Chitin is a homopolymer of β-(1,4)-linked N-acetyl-D-glucosamine (GlcNAc) and a major structural component of fungal cell walls. In plants, chitin acts as a microbe-associated molecular pattern (MAMP) that is recognized by lysin motif (LysM)-containing plant cell surface-localized pattern recognition receptors (PRRs) that activate a plethora of downstream immune responses. To deregulate chitin-induced plant immunity and successfully establish infection, many fungal pathogens secrete LysM domain-containing effector proteins during host colonization. The LysM effector Ecp6 from the tomato (Solanum lycopersicum) leaf mold fungus Cladosporium fulvum can outcompete plant PRRs for chitin binding because two of its three LysM domains cooperate to form a composite groove with ultra-high (pM) chitin-binding affinity. However, most functionally characterized LysM effectors contain only two LysMs, including Magnaporthe oryzae MoSlp1, Verticillium dahliae Vd2LysM, and Colletotrichum higginsianum ChElp1 and ChElp2. Here, we performed modeling, structural, and functional analyses to investigate whether such dual-domain LysM effectors can also form ultra-high chitin-binding affinity grooves through intramolecular LysM dimerization. However, our study suggests that intramolecular LysM dimerization does not occur. Rather, our data support the occurrence of intermolecular LysM dimerization for these effectors, associated with a substantially lower chitin binding affinity than monitored for Ecp6. Interestingly, the intermolecular LysM dimerization allows for the formation of polymeric complexes in the presence of chitin. Possibly, such polymers may precipitate at infection sites to eliminate chitin oligomers, and thus suppress the activation of chitin-induced plant immunity. |
|---|---|
| MeSH term(s) | Chitin/metabolism ; Dimerization ; Fungal Proteins/metabolism ; Plant Immunity ; Lycopersicon esculentum/metabolism ; Plant Diseases/microbiology |
| Chemical Substances | Chitin (1398-61-4) ; Fungal Proteins |
| Language | English |
| Publishing date | 2022-08-23 |
| Publishing country | United States |
| Document type | Journal Article ; Research Support, Non-U.S. Gov't |
| ZDB-ID | 208914-2 |
| ISSN | 1532-2548 ; 0032-0889 |
| ISSN (online) | 1532-2548 |
| ISSN | 0032-0889 |
| DOI | 10.1093/plphys/kiac391 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
| Z 1193: Show issues |
This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.
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populaties, extractie en ontwikkelen waardplanttoets : Rapportage proefjaar 2021
2022
Abstract: Stengelaaltjes vormen een lastig probleem, doordat ze een brede waardplantreeks hebben. De aaltjes kunnen al in lage dichtheden, die lastig zijn te detecteren, voor schade zorgen. Verder zijn de omstandigheden waaronder de aaltjes actief worden ... ...
| Abstract | Stengelaaltjes vormen een lastig probleem, doordat ze een brede waardplantreeks hebben. De aaltjes kunnen al in lage dichtheden, die lastig zijn te detecteren, voor schade zorgen. Verder zijn de omstandigheden waaronder de aaltjes actief worden onvoldoende bekend en is het daardoor niet goed voorspelbaar wanneer er problemen kunnen optreden. Ook bestaan er verschillende ‘stengelaaltjesrassen’ die morfologisch niet te onderscheiden zijn en deels verschillende waardplanten kennen. Hierdoor is het niet mogelijk om een sluitend advies te geven welke gewassen veilig kunnen worden geteeld. In de PPS LWV19010 – Uireka: naar een integraal duurzame uienteelt in de periode 2020-2023 is onderzoek naar stengelaaltjes opgenomen. Het werkpakket stengelaaltjes beoogt informatie te krijgen over de volgende onderwerpen: bodemeigenschappen die besmetting met stengelaaltjes bevorderen of in stand houden, optimaliseren van extractie van het ruststadium (dauerlarve) van stengelaaltjes uit grond, het ontwikkelen en uiteindelijk uitvoeren van een waardplanttoets met verschillende stengelaaltjesrassen. In dit rapport zijn de resultaten van het onderzoek in 2021 beschreven. |
|---|---|
| Keywords | Life Science |
| Language | Dutch |
| Publisher | UIREKA |
| Publishing country | nl |
| Document type | Book ; Online |
| Database | BASE - Bielefeld Academic Search Engine (life sciences selection) |
Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.
populaties, extractie en ontwikkelen pottoets : Rapportage proefjaar 2020
2021
| Keywords | Life Science |
|---|---|
| Language | Dutch |
| Publisher | UIREKA |
| Publishing country | nl |
| Document type | Book ; Online |
| Database | BASE - Bielefeld Academic Search Engine (life sciences selection) |
Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.
2022 Volume 190, Issue 3
Abstract: Chitin is a homopolymer of β-(1,4)-linked N-acetyl-D-glucosamine (GlcNAc) and a major structural component of fungal cell walls. In plants, chitin acts as a microbe-associated molecular pattern (MAMP) that is recognized by lysin motif (LysM)-containing ... ...
| Abstract | Chitin is a homopolymer of β-(1,4)-linked N-acetyl-D-glucosamine (GlcNAc) and a major structural component of fungal cell walls. In plants, chitin acts as a microbe-associated molecular pattern (MAMP) that is recognized by lysin motif (LysM)-containing plant cell surface-localized pattern recognition receptors (PRRs) that activate a plethora of downstream immune responses. To deregulate chitin-induced plant immunity and successfully establish infection, many fungal pathogens secrete LysM domain-containing effector proteins during host colonization. The LysM effector Ecp6 from the tomato (Solanum lycopersicum) leaf mold fungus Cladosporium fulvum can outcompete plant PRRs for chitin binding because two of its three LysM domains cooperate to form a composite groove with ultra-high (pM) chitin-binding affinity. However, most functionally characterized LysM effectors contain only two LysMs, including Magnaporthe oryzae MoSlp1, Verticillium dahliae Vd2LysM, and Colletotrichum higginsianum ChElp1 and ChElp2. Here, we performed modeling, structural, and functional analyses to investigate whether such dual-domain LysM effectors can also form ultra-high chitin-binding affinity grooves through intramolecular LysM dimerization. However, our study suggests that intramolecular LysM dimerization does not occur. Rather, our data support the occurrence of intermolecular LysM dimerization for these effectors, associated with a substantially lower chitin binding affinity than monitored for Ecp6. Interestingly, the intermolecular LysM dimerization allows for the formation of polymeric complexes in the presence of chitin. Possibly, such polymers may precipitate at infection sites to eliminate chitin oligomers, and thus suppress the activation of chitin-induced plant immunity. |
|---|---|
| Keywords | Life Science |
| Subject code | 540 |
| Language | English |
| Publishing country | nl |
| Document type | Article ; Online |
| ZDB-ID | 208914-2 |
| ISSN | 1532-2548 ; 0032-0889 |
| ISSN (online) | 1532-2548 |
| ISSN | 0032-0889 |
| Database | BASE - Bielefeld Academic Search Engine (life sciences selection) |
| Z 1193: Show issues |
This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.
Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.
2013 Volume 9, Issue 12, Page(s) e1003769
| MeSH term(s) | Animals ; Chitin/metabolism ; Cladosporium/growth & development ; Cladosporium/metabolism ; Cladosporium/pathogenicity ; Food Chain ; Fungal Proteins/chemistry ; Fungal Proteins/metabolism ; Fungi/metabolism ; Humans ; Lysine/chemistry ; Models, Molecular ; Plant Diseases/microbiology ; Plant Proteins/metabolism ; Protein Binding ; Protein Interaction Domains and Motifs ; Virulence Factors/chemistry ; Virulence Factors/physiology |
|---|---|
| Chemical Substances | Fungal Proteins ; Plant Proteins ; Virulence Factors ; Chitin (1398-61-4) ; Lysine (K3Z4F929H6) |
| Language | English |
| Publishing date | 2013-12-12 |
| Publishing country | United States |
| Document type | Journal Article ; Research Support, Non-U.S. Gov't |
| ZDB-ID | 2205412-1 |
| ISSN | 1553-7374 ; 1553-7366 |
| ISSN (online) | 1553-7374 |
| ISSN | 1553-7366 |
| DOI | 10.1371/journal.ppat.1003769 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.
Fungal genetics and biology : FG & B
2016 Volume 112, Page(s) 55–63
Abstract: Among the invaluable benefits of basidiomycete genomics is the dramatically enhanced insight into the potential capacity to biosynthesize natural products. This study focuses on adenylate-forming reductases, which is a group of natural product ... ...
| Abstract | Among the invaluable benefits of basidiomycete genomics is the dramatically enhanced insight into the potential capacity to biosynthesize natural products. This study focuses on adenylate-forming reductases, which is a group of natural product biosynthesis enzymes that resembles non-ribosomal peptide synthetases, yet serves to modify one substrate, rather than to condense two or more building blocks. Phylogenetically, these reductases fall in four classes. The phylogeny of Heterobasidion annosum (Russulales) and Serpula lacrymans (Boletales) adenylate-forming reductases was investigated. We identified a previously unrecognized phylogenetic branch within class III adenylate-forming reductases. Three representatives were heterologously produced and their substrate preferences determined in vitro: NPS9 and NPS11 of S. lacrymans preferred l-threonine and benzoic acid, respectively, while NPS10 of H. annosum accepted phenylpyruvic acid best. We also investigated two class IV adenylate-forming reductases of Coprinopsis cinerea, which each were active with l-alanine, l-valine, and l-serine as substrates. Our results show that adenylate-forming reductases are functionally more diverse than previously recognized. As none of the natural products known from the species investigated in this study includes the identified substrates of their respective reductases, our findings may help further explore the diversity of these basidiomycete secondary metabolomes. |
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| MeSH term(s) | Agaricales/enzymology ; Agaricales/genetics ; Genetic Variation ; Genome, Fungal ; Oxidoreductases/classification ; Oxidoreductases/genetics ; Oxidoreductases/metabolism ; Phylogeny ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Substrate Specificity |
| Chemical Substances | Recombinant Proteins ; Oxidoreductases (EC 1.-) |
| Language | English |
| Publishing date | 2016-07-22 |
| Publishing country | United States |
| Document type | Journal Article ; Research Support, Non-U.S. Gov't |
| ZDB-ID | 1319820-8 |
| ISSN | 1096-0937 ; 1087-1845 ; 0147-5975 |
| ISSN (online) | 1096-0937 |
| ISSN | 1087-1845 ; 0147-5975 |
| DOI | 10.1016/j.fgb.2016.07.008 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
| Zs.A 2431: Show issues | Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG) |
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2019 Volume 112, Issue 2, Page(s) 605–619
Abstract: Fungi defend their ecological niche against antagonists by producing antibiosis molecules. Some of these molecules are only produced upon confrontation with the antagonist. The basidiomycete Coprinopsis cinerea induces the expression of the sesquiterpene ...
| Abstract | Fungi defend their ecological niche against antagonists by producing antibiosis molecules. Some of these molecules are only produced upon confrontation with the antagonist. The basidiomycete Coprinopsis cinerea induces the expression of the sesquiterpene synthase-encoding gene cop6 and its two neighboring genes coding for cytochrome P450 monooxygenases in response to bacteria. We further investigated this regulation of cop6 and examined if the gene product is involved in the production of antibacterials. Cell-free supernatants of axenic cultures of the Gram-positive bacterium Bacillus subtilis were sufficient to induce cop6 transcription assessed using a fluorescent reporter strain. Use of this strain in a microfluidic device revealed that the cop6 gene was induced in all hyphae directly exposed to the supernatant and that induction occurred within less than one hour. Targeted replacement of the cop6 gene demonstrated the requirement of the encoded synthase for the biosynthesis of the sesquiterpene lagopodin B, a previously reported antibacterial compound from related species. Accordingly, lagopodin B from C. cinerea inhibited the growth of several Gram-positive bacteria including B. subtilis but not Gram-negative bacteria. Our results demonstrate that the C. cinerea vegetative mycelium responds to soluble compounds of a bacterial culture supernatant by local production of an antibacterial secondary metabolite. |
|---|---|
| MeSH term(s) | Agaricales/enzymology ; Agaricales/genetics ; Agaricales/metabolism ; Anti-Bacterial Agents/metabolism ; Anti-Bacterial Agents/pharmacology ; Bacillus subtilis/physiology ; Cytochrome P-450 Enzyme System/genetics ; Cytochrome P-450 Enzyme System/metabolism ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Gram-Negative Bacteria/drug effects ; Gram-Negative Bacteria/growth & development ; Sesquiterpenes/metabolism ; Sesquiterpenes/pharmacology |
| Chemical Substances | Anti-Bacterial Agents ; Fungal Proteins ; Sesquiterpenes ; Cytochrome P-450 Enzyme System (9035-51-2) |
| Language | English |
| Publishing date | 2019-05-29 |
| Publishing country | England |
| Document type | Journal Article ; Research Support, Non-U.S. Gov't |
| ZDB-ID | 619315-8 |
| ISSN | 1365-2958 ; 0950-382X |
| ISSN (online) | 1365-2958 |
| ISSN | 0950-382X |
| DOI | 10.1111/mmi.14277 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
| Zs.A 2502: Show issues | Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG) |
This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.
2020 Volume 16, Issue 6, Page(s) e1008652
Abstract: Plants trigger immune responses upon recognition of fungal cell wall chitin, followed by the release of various antimicrobials, including chitinase enzymes that hydrolyze chitin. In turn, many fungal pathogens secrete LysM effectors that prevent chitin ... ...
| Abstract | Plants trigger immune responses upon recognition of fungal cell wall chitin, followed by the release of various antimicrobials, including chitinase enzymes that hydrolyze chitin. In turn, many fungal pathogens secrete LysM effectors that prevent chitin recognition by the host through scavenging of chitin oligomers. We previously showed that intrachain LysM dimerization of the Cladosporium fulvum effector Ecp6 confers an ultrahigh-affinity binding groove that competitively sequesters chitin oligomers from host immune receptors. Additionally, particular LysM effectors are found to protect fungal hyphae against chitinase hydrolysis during host colonization. However, the molecular basis for the protection of fungal cell walls against hydrolysis remained unclear. Here, we determined a crystal structure of the single LysM domain-containing effector Mg1LysM of the wheat pathogen Zymoseptoria tritici and reveal that Mg1LysM is involved in the formation of two kinds of dimers; a chitin-dependent dimer as well as a chitin-independent homodimer. In this manner, Mg1LysM gains the capacity to form a supramolecular structure by chitin-induced oligomerization of chitin-independent Mg1LysM homodimers, a property that confers protection to fungal cell walls against host chitinases. |
|---|---|
| MeSH term(s) | Ascomycota/chemistry ; Ascomycota/genetics ; Ascomycota/metabolism ; Chitin/chemistry ; Chitin/genetics ; Chitin/metabolism ; Cladosporium/chemistry ; Cladosporium/genetics ; Fungal Proteins/chemistry ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Hyphae/chemistry ; Hyphae/genetics ; Hyphae/metabolism ; Plant Diseases/genetics ; Plant Diseases/microbiology ; Protein Multimerization ; Protein Structure, Quaternary ; Triticum/genetics ; Triticum/metabolism ; Triticum/microbiology |
| Chemical Substances | Fungal Proteins ; Chitin (1398-61-4) |
| Language | English |
| Publishing date | 2020-06-23 |
| Publishing country | United States |
| Document type | Journal Article ; Research Support, Non-U.S. Gov't |
| ZDB-ID | 2205412-1 |
| ISSN | 1553-7374 ; 1553-7366 |
| ISSN (online) | 1553-7374 |
| ISSN | 1553-7366 |
| DOI | 10.1371/journal.ppat.1008652 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.