RUVBL1 Protein, Human (sf9, His)

RUVBL1 protein possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (3' to 5') activity, with hexamerization considered crucial for ATP hydrolysis, and adjacent subunits in the ring-like structure contributing to the ATPase activity. As a component of the NuA4 histone acetyltransferase complex, RUVBL1 is involved in the transcriptional activation of select genes, primarily through the acetylation of nucleosomal histones H4 and H2A. This modification can alter nucleosome-DNA interactions and promote interaction with other proteins that positively regulate transcription. The NuA4 complex, including the ATPase and helicase activities, is, in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. The NuA4 complex may also play a direct role in DNA repair when recruited to sites of DNA damage. Furthermore, RUVBL1 is a component of a SWR1-like complex responsible for the removal of histone H2A.Z/H2AZ1 from the nucleosome and is proposed as a core component of the chromatin remodeling INO80 complex, which exhibits DNA- and nucleosome-activated ATPase activity and catalyzes ATP-dependent nucleosome sliding. RUVBL1 is essential for cell proliferation, plays a role in oncogenic transformation by MYC, and modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex. Additionally, RUVBL1 may bind plasminogen at the cell surface, enhancing plasminogen activation.