Fusarium verticillioides produces fumonisin mycotoxins during colonization of maize. Currently, molecular mechanisms underlying responsiveness of F.verticillioides to extracellular cues during pathogenesis are poorly understood. In this study, insertional mutants were created and screened to identify genes involved in responses to extracellular starch. In one mutant, the restriction enzyme-mediated integration cassette disrupted a gene (UBL1) encoding a UBR-Box/RING domain E3 ubiquitin ligase involved in the N-end rule pathway. Disruption of UBL1 in F.verticillioides (Δubl1) influenced conidiation, hyphal morphology, pigmentation and amylolysis. Disruption of UBL1 also impaired kernel colonization, but the ratio of fumonisin B1 per unit growth was not significantly reduced. The inability of a Δubl1 mutant to recognize an N-end rule degron confirmed involvement of UBL1 in the N-end rule pathway. Additionally, Ubl1 physically interacted with two G protein α subunits of F.verticillioides, thus implicating UBL1 in G protein-mediated sensing of the external environment. Furthermore, deletion of the UBL1 orthologue in F.graminearum reduced virulence on wheat and maize, thus indicating that UBL1 has a broader role in virulence among Fusarium species. This study provides the first linkage between the N-end rule pathway and fungal pathogenesis, and illustrates a new mechanism through which fungi respond to the external environment.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1111/1462-2920.12333 | DOI Listing |
Anticancer Agents Med Chem
January 2025
Department of Chemistry, Illinois State University, Normal, Il, USA.
Many oncoproteins are important therapeutic targets because of their critical role in inducing rapid cell proliferation, which represents one of the salient hallmarks of cancer. Chronic Myeloid Leukemia (CML) is a cancer of hematopoietic stem cells that is caused by the oncogene BCR-ABL1. BCR-ABL1 encodes a constitutively active tyrosine kinase protein that leads to the uncontrolled proliferation of myeloid cells, which is a hallmark of CML.
View Article and Find Full Text PDFSheng Li Xue Bao
December 2024
Oujiang Laboratory (Zhejiang Lab for Regenerative Medicine, Vision and Brain Health), Wenzhou 325000, China.
The N-end rule pathway is a protein degradation pathway mediated by the ubiquitin-proteasome system, which specifically targets and degrades target proteins by recognizing specific residues at the N-terminus of the proteins. The residues which play a crucial role in the N-end rule pathway are called degrons, also known as N-degrons, as they are usually unstable at the N-terminal end of the protein. Currently, several N-end rule pathways have been identified in the eukaryotes, including the Arg/N-end rule, Ac/N-end rule, and Pro/N-end rule pathways, as well as the recently discovered Gly/N-end rule pathway.
View Article and Find Full Text PDFNutrients
December 2024
Department of Clinical Engineering, Faculty of Health Care Sciences, Jikei University of Health Care Sciences, Osaka 532-0003, Japan.
Background: On 1 January 2024, a 7.6 magnitude earthquake struck the Noto Peninsula. We entered the disaster area to provide relief and set up a makeshift clinic in an evacuation center to evaluate the quality and quantity of food provided there.
View Article and Find Full Text PDFBiochem Pharmacol
January 2025
Amity Institute of Molecular Medicine and Stem Cell Research, Amity University Uttar Pradesh, Noida 201311, India. Electronic address:
Regulated protein degradation plays a crucial role in maintaining proteostasis along with protein refolding and compartmentalisation which collectively control biological functions. The N-end rule pathway is a major ubiquitin-dependent protein degradation system. The short-lived protein substrates containing destabilizing amino acid residues (N-degrons) are recognized by E3 ubiquitin ligases containing UBR box domains (N-recognin) for degradation.
View Article and Find Full Text PDFbioRxiv
November 2024
Department of Molecular & Cellular Pharmacology, University of Miami Miller School of Medicine, Miami, FL, USA.
Cell death regulation is essential for stress adaptation and/or signal response. Past studies have shown that eukaryotic cell death is mediated by an evolutionarily conserved enzyme, arginyltransferase1 (Ate1). The downregulation of Ate1, as seen in many types of cancer, prominently increases cellular tolerance to a variety of stressing conditions.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!