A Fast Ubiquitination of UHRF1 Oncogene Is a Unique Feature and a Common Mechanism of Thymoquinone in Cancer Cells

Downregulation of the ubiquitin-like containing PHD and ring finger 1 (UHRF1) oncogene in cancer cells response to natural anticancer drugs, including thymoquinone (TQ), is a key event that induces apoptosis. TQ can induce UHRF1 autoubiquitination via E3 ligase activity its RING domain, most likely through downregulation herpes virus-associated ubiquitin-specific protease (HAUSP). In this study, we evaluated whether HAUSP fast ubiquitination are prerequisites for degradation doxorubicin mimic effects on ubiquitination. RNA sequencing was performed investigate differentially expressed genes TQ-treated Jurkat cells. The protein expression UHRF1, Bcl-2 detected by means Western blot analysis. proliferation human colon (HCT-116) analyzed WST-1 assay. data revealed significantly decreased expression. triggered undergo rapid as first step inhibition cell proliferation. TQ-induced associated with downregulation. Like TQ, induced similar dose- time-dependent cells, but did not TQ. Furthermore, without triggering A an indispensable responses doxorubicin. appears trigger oncogene, thereby identifying specific target therapy.