Dec 25, 2024 · SUV39H1 (SUV39H1 Histone Lysine Methyltransferase) is a Protein Coding gene. Diseases associated with SUV39H1 include Hyperoxaluria, Primary, Type I and Hutchinson-Gilford Progeria Syndrome. Among its related pathways are RNA Polymerase I Promoter Opening and PKMTs methylate histone lysines.

Jan 12, 2024 · We show here that the genetic disruption of SUV39H1, which encodes a histone-3, lysine-9 methyl-transferase, enhances the early expansion, long-term persistence, and overall antitumor efficacy of human CAR T cells in leukemia and prostate cancer models.

Jul 16, 2021 · SUV39H1 and SUV39H2 were the first protein lysine methyltransferases that were identified more than 20 years ago. Both enzymes introduce di- and trimethylation at histone H3 lysine 9 (H3K9) and have important roles in the maintenance of heterochromatin and …

SUV39H1 is a prognosis and immune microenvironment-related biomarker in diffuse large B-cell lymphoma. Decreased SUV39H1 at the promoter region leads to increased CREMalpha and accelerates autoimmune response in CD4[+] T cells from …

Sep 19, 2024 · In this study, we conducted a high-throughput screen utilizing a compound library containing 288 epigenetic drugs, leading to the identification of chaetocin as the most potent NB inhibitor by...

Jul 18, 2016 · Our results establish an unexpected feature of Suv39h1, distinct from the KMT activity, with a major role for heterochromatin formation. We discuss how linking Suv39h1 to the SUMO pathway...

Jan 12, 2024 · We show that targeting SUV39H1 histone methyltransferase enhances 41BB-based CAR T-cell long-term protection against tumor relapses and rechallenges by increasing stemness/memory differentiation. This opens a safe path to …

Nov 15, 2007 · The histone deacetylase SIRT1 is shown to target the SUV39H1 enzyme and contribute to elevated levels of SUV39H1 activity and H3K9me3 in heterochromatin.

SUV39H1 mediates epigenetic events in the pathophysiology of hematopoietic disorders. We found that inhibition of Hsp90 by Chaetocin and 17-AAG had ability to induce degradation of SUV39H1 through proteasome pathway. In addition, SUV39H1 interacted with Hsp90 through co-chaperone HOP.

SUV39H1 trimethylates Lys-138 of the Mycobacterium tuberculosis histone-like protein HupB thereby inhibiting biofilm formation. Repressing the gene activity of suv39h1 increases susceptibility of THP1 macrophages to mycobacterial infection.