Lysine methyltransferases transfer methyl groups in specific lysine sites, which regulates a variety of important biological processes in eukaryotes. In this study, we characterized a novel homolog of the yeast methyltransferase DOT1 in . , and observed the roles of in . . Deletion of showed a significant decrease in conidiation, but an increase in sclerotia formation. A change in viability to multiple stresses was also found in the Δ mutant. Additionally, aflatoxin (AF) production was found severely impaired in the Δ mutant. Further analysis by qRT-PCR revealed that the transcription of AF structural genes and their regulator gene were prominently suppressed in the Δ mutant. Furthermore, our data revealed that Dot1 is important for colonizing maize seeds in . . Our research indicates that Dot1 is involved in fungal development, aflatoxin biosynthesis and fungal virulence in . , which might provide a potential target for controlling . with new strategies.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5535179 | PMC |
| http://dx.doi.org/10.3390/toxins9070232 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Pan‑cancer analysis on the role of KMT2C expression in tumor progression and immunotherapy.
Oncol Lett
September 2024
Institute of Clinical Immunology, First Affiliated Hospital of Anhui Medical University, Hefei, Anhui 230022, P.R. China.
Histone lysine N-methyltransferase 2C (KMT2C) is involved in transcriptional regulation and DNA damage repair. Mutations in KMT2C have been implicated in the progression, metastasis, and drug resistance of multiple cancer types. However, the roles of KMT2C in the regulation of tumor prognosis, immune cell infiltration and the immune microenvironment in these multiple cancer types remain unclear.
View Article and Find Full Text PDFYeast Npl3 regulates replicative senescence outside of TERRA R-loop resolution and co-transcriptional processing.
Nucleosides Nucleotides Nucleic Acids
July 2024
Department of Biology, Saint Joseph's University, Philadelphia, Pennsylvania, USA.
Eukaryotic cells without telomerase experience progressively shorter telomeres with each round of cell division until cell cycle arrest is initiated, leading to replicative senescence. When yeast which encodes the RNA template of telomerase, is deleted, senescence is accompanied by increased expression of TERRA (non-coding telomere repeat-containing RNA). Deletion of Npl3, an RNA-processing protein with telomere maintenance functions, accelerates senescence in cells and significantly increases TERRA levels.
View Article and Find Full Text PDFDOT1-like histone lysine methyltransferase is critical for adult vessel maintenance and functions.
Anim Biosci
September 2024
Department of Stem Cell and Regenerative Biotechnology, Institute of Advanced Regenerative Science, Konkuk University, Seoul 05029, Korea.
Objective: Disruptor of telomeric silencing 1-like (DOT1L) is the only known histone H3K79 methyltransferase essential for the development of the embryonic cardiovascular system, including the heart, blood vessels, and lymphatic vessels, through transcriptional regulation. Our previous study demonstrated that Dot1l deletion results in aberrant lymphatic development and function. However, its precise function in the postnatal cardiovascular system remains unknown.
View Article and Find Full Text PDFTwo DOT1 enzymes cooperatively mediate efficient ubiquitin-independent histone H3 lysine 76 tri-methylation in kinetoplastids.
Nat Commun
March 2024
Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA, USA.
In higher eukaryotes, a single DOT1 histone H3 lysine 79 (H3K79) methyltransferase processively produces H3K79me2/me3 through histone H2B mono-ubiquitin interaction, while the kinetoplastid Trypanosoma brucei di-methyltransferase DOT1A and tri-methyltransferase DOT1B efficiently methylate the homologous H3K76 without H2B mono-ubiquitination. Based on structural and biochemical analyses of DOT1A, we identify key residues in the methyltransferase motifs VI and X for efficient ubiquitin-independent H3K76 methylation in kinetoplastids. Substitution of a basic to an acidic residue within motif VI (GxK) is essential to stabilize the DOT1A enzyme-substrate complex, while substitution of the motif X sequence VYGE by CAKS renders a rigid active-site loop flexible, implying a distinct mechanism of substrate recognition.
View Article and Find Full Text PDFDOT1L stimulates MYC/Mondo transcription factor activity by promoting its degradation cycle on chromatin.
bioRxiv
February 2024
Department of Biochemistry & Cell Biology, Boston University School of Medicine, Boston, MA, 02118, USA.
The proto-oncogene c-MYC is a key representative of the MYC transcription factor network regulating growth and metabolism. MML-1 (Myc- and Mondo-like) is its homolog in . The functional and molecular cooperation between c-MYC and H3 lysine 79 methyltransferase DOT1L was demonstrated in several human cancer types, and we have earlier discovered the connection between MML-1 and DOT-1.
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!