Djamei introduces the fungal pathogen (and culinary delicacy) Ustilago maydis.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.cub.2023.02.069 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Further Characterization of Lipase B from Ustilago maydis Expressed in Pichia pastoris: a Member of the Candida antarctica Lipase B-like Superfamily.
Appl Biochem Biotechnol
January 2025
Unidad de Biotecnología Industrial, Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C, 45019, Zapopan, Jal, Mexico.
Lipases from the basidiomycete fungus Ustilago maydis are promising but underexplored biocatalysts due to their high homology with Candida antarctica lipases. This study provides a comprehensive characterization of a recombinant CALB-like lipase from U. maydis, expressed in Pichia pastoris (rUMLB), and compares its properties with those of the well-studied recombinant lipase B from C.
View Article and Find Full Text PDFBioprocess development for microbial production and purification of cellobiose lipids by the smut fungus Ustilago maydis DSM 4500.
Bioprocess Biosyst Eng
January 2025
Department of Chemical Engineering, Stellenbosch University, Private Bag X1, Matieland, 7602, South Africa.
Cellobiose lipids (CBLs) are a class of glycolipid biosurfactants produced by various fungal strains. These compounds have gained significant interest due to their surface-active and antifungal properties, which are comparable to traditional synthetic surfactants and antimicrobials. Despite their potential applicability in various cosmetic, pharmaceutical, and agricultural formulations, significantly less research has been focused on their production and purification in comparison to other glycolipid biosurfactants, such as mannosylerythritol lipids (MELs) and sophorolipids.
View Article and Find Full Text PDFSampling-free investigation of microbial carbon source preferences on renewable feedstocks via online monitoring of oxygen transfer rate.
Bioprocess Biosyst Eng
December 2024
AVT-Biochemical Engineering, RWTH Aachen University, Forckenbeckstraße 51, 52074, Aachen, Germany.
The transition towards sustainable bioprocesses requires renewable feedstocks to reduce dependency on finite resources. While plant-based feedstocks offer significant potential, their complex composition poses new challenges. The microorganisms often exhibit polyauxic growth when presented with multiple carbon sources simultaneously, consuming them in a distinct order according to their carbon source preferences.
View Article and Find Full Text PDFMicrobial iCLIP2: enhanced mapping of RNA-protein interaction by promoting protein and RNA stability.
RNA
January 2025
Institute of Microbiology, Heinrich Heine University Düsseldorf, Cluster of Excellence on Plant Sciences, 40204 Düsseldorf, Germany
The entire RNA life cycle, spanning from transcription to decay, is intricately regulated by RNA-binding proteins (RBPs). To understand their precise functions, it is crucial to identify direct targets, pinpoint their exact binding sites, and unravel the underlying specificity in vivo. Individual-nucleotide resolution UV cross-linking and immunoprecipitation 2 (iCLIP2) is a state-of-the-art technique that enables the identification of RBP-binding sites at single-nucleotide resolution.
View Article and Find Full Text PDFUstilago maydis Trf2 ensures genome stability by antagonizing Blm-mediated telomere recombination: Fine-tuning DNA repair factor activity at telomeres through opposing regulations.
PLoS Genet
December 2024
Department of Microbiology & Immunology, W. R. Hearst Microbiology Research Center, Weill Cornell Medicine, New York, New York, United States of America.
TRF2 is an essential and conserved double-strand telomere binding protein that stabilizes chromosome ends by suppressing DNA damage response and aberrant DNA repair. Herein we investigated the mechanisms and functions of the Trf2 ortholog in the basidiomycete fungus Ustilago maydis, which manifests strong resemblances to metazoans with regards to the telomere and DNA repair machinery. We showed that UmTrf2 binds to Blm in vitro and inhibits Blm-mediated unwinding of telomeric DNA substrates.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!